UniProt UniProt http://www.uniprot.org Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. The Journal of biological chemistry 2011 imex curation Grishin AM., Ajamian E., Tao L., Zhang L., Menard R., Cygler M. mirek@bri.nrc.ca 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro oxidoreduct assay oxidoreductase assay oxidoreduct assay predetermined predetermined participant predetermined Grishin AM., Ajamian E., Tao L., Zhang L., Menard R., Cygler M. It is not clear from the Materials and Methods which of these proteins were tagged when the different combination of subunits were purified for this experiment. mirek@bri.nrc.ca Accepted 2018-NOV-28 AT 16:57 GMT AT 16:57 GMT by LIVIAP The Journal of biological chemistry 2011 imex curation Agree for EBI-20642411/acteyl-CoA, not for the others which are listed as tetrameric by PDB and P41212 in Table 3, except for EBI-20627953 - "(PaaAC)2 heterotetramer (dimer of heterodimers)". Yes, the two small molecule names are synonyms - if in doubt consult ChEBI which has long lists of synonyms. Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. The Journal of biological chemistry 2011 imex curation Grishin AM., Ajamian E., Tao L., Zhang L., Menard R., Cygler M. mirek@bri.nrc.ca 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation ecoli Escherichia coli (strain K12) pull down pull down western blot western blot Immuno blot Immuno blot Grishin AM., Ajamian E., Tao L., Zhang L., Menard R., Cygler M. mirek@bri.nrc.ca Accepted 2018-NOV-28 AT 16:57 GMT AT 16:57 GMT by LIVIAP The Journal of biological chemistry 2011 imex curation Agree for EBI-20642411/acteyl-CoA, not for the others which are listed as tetrameric by PDB and P41212 in Table 3, except for EBI-20627953 - "(PaaAC)2 heterotetramer (dimer of heterodimers)". Yes, the two small molecule names are synonyms - if in doubt consult ChEBI which has long lists of synonyms. Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. Structural and functional studies of the Escherichia coli phenylacetyl-CoA monooxygenase complex. The Journal of biological chemistry 2011 imex curation Grishin AM., Ajamian E., Tao L., Zhang L., Menard R., Cygler M. mirek@bri.nrc.ca 09-May-2019: Contacted by IntAct-Help. Only protein-protein interactions imex curation in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Grishin AM., Ajamian E., Tao L., Zhang L., Menard R., Cygler M. mirek@bri.nrc.ca Accepted 2018-NOV-28 AT 16:57 GMT AT 16:57 GMT by LIVIAP The Journal of biological chemistry 2011 imex curation Agree for EBI-20642411/acteyl-CoA, not for the others which are listed as tetrameric by PDB and P41212 in Table 3, except for EBI-20627953 - "(PaaAC)2 heterotetramer (dimer of heterodimers)". Yes, the two small molecule names are synonyms - if in doubt consult ChEBI which has long lists of synonyms. phenylacetyl-coa phenylacetyl-CoA Coenzyme A, S-(benzeneacetate) Phenylacetyl coenzyme A Phenylacetyl-CoA Phenylacetyl-coa Phenylacetyl-coenzyme A 3'-phosphoadenosine 5'-{3-[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-{[3-oxo-3-({2-[(phenylacetyl)sulfanyl]ethyl}amino)propyl]amino}butyl] dihydrogen diphosphate} small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) paab_ecoli 1,2-phenylacetyl-CoA epoxidase, subunit B ynbF paaB b1389 JW1384 1,2-phenylacetyl-CoA monooxygenase, subunit B protein protein ecoli Escherichia coli (strain K12) MSNVYWPLYEVFVRGKQGLSHRHVGSLHAADERMALENARDAYTRRSEGCSIWVVKASEIVASQPEERGEFFDPAESKVYRHPTFYTIPDGIEHM D2866DB428CF90AF coenzyme a coenzyme A [(2R,3S,4R,5R)-5-(6-amino-9H-purin-9-yl)-4-hydroxy-3-(phosphonooxy)tetrahydrofuran-2-yl]methyl (3R)-3-hydroxy-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)-2,2-dimethyl-4-oxobutyl dihydrogen diphosphate 3'-phosphoadenosine-(5')diphospho(4')pantatheine CoA CoA-SH CoASH Coenzym A Coenzyme A COENZYME A HSCoA Koenzym A 3'-phosphoadenosine 5'-{3-[(3R)-3-hydroxy-2,2-dimethyl-4-oxo-4-({3-oxo-3-[(2-sulfanylethyl)amino]propyl}amino)butyl] dihydrogen diphosphate} small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) acetyl-coa small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) paae_ecoli 1,2-phenylacetyl-CoA epoxidase, subunit E paaE b1392 JW1387 ydbR 1,2-phenylacetyl-CoA epoxidase, reductase subunit 1,2-phenylacetyl-CoA monooxygenase, subunit E protein protein ecoli Escherichia coli (strain K12) MTTFHSLTVAKVESETRDAVTITFAVPQPLQEAYRFRPGQHLTLKASFDGEELRRCYSICRSYLPGEISVAVKAIEGGRFSRYAREHIRQGMTLEVMVPQGHFGYQPQAERQGRYLAIAAGSGITPMLAIIATTLQTEPESQFTLIYGNRTSQSMMFRQALADLKDKYPQRLQLLCIFSQETLDSDLLHGRIDGEKLQSLGASLINFRLYDEAFICGPAAMMDDAETALKALGMPDKTIHLERFNTPGTRVKRSVNVQSDGQKVTVRQDGRDREIVLNADDESILDAALRQGADLPYACKGGVCATCKCKVLRGKVAMETNYSLEPDELAAGYVLSCQALPLTSDVVVDFDAKGMA D719C1CA81DA5FFA 3-hydroxybutanoyl-coa 3-hydroxybutanoyl-CoA 3-Hydroxybutanoyl-CoA 3-Hydroxybutyryl-coa 3-Hydroxybutyryl-coenzyme A beta-Hydroxybutyryl-coa beta-Hydroxybutyryl-coenzyme A Coenzyme A, S-(3-hydroxybutanoate) S-(3-hydroxybutanoyl)-CoA S-(3-hydroxybutanoyl)-coenzyme A S-(3-hydroxybutyryl)-CoA S-(3-hydroxybutyryl)-coenzyme A 3'-phosphoadenosine 5'-{3-[(3R)-3-hydroxy-4-{[3-({2-[(3-hydroxybutanoyl)sulfanyl]ethyl}amino)-3-oxopropyl]amino}-2,2-dimethyl-4-oxobutyl] dihydrogen diphosphate} small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) paac_ecoli 1,2-phenylacetyl-CoA epoxidase, subunit C paaC b1390 JW1385 ydbP 1,2-phenylacetyl-CoA epoxidase, structural subunit beta 1,2-phenylacetyl-CoA monooxygenase, subunit C protein protein ecoli Escherichia coli (strain K12) MNQLTAYTLRLGDNCLVLSQRLGEWCGHAPELEIDLALANIGLDLLGQARNFLSYAAELAGEGDEDTLAFTRDERQFSNLLLVEQPNGNFADTIARQYFIDAWHVALFTRLMESRDPQLAAISAKAIKEARYHLRFSRGWLERLGNGTDVSGQKMQQAINKLWRFTAELFDADEIDIALSEEGIAVDPRTLRAAWEAEVFAGINEATLNVPQEQAYRTGGKKGLHTEHLGPMLAEMQYLQRVLPGQQW 024AD161DF8E4380 benzoyl-coa benzoyl-CoA Benzoyl-CoA benzoyl-coenzyme A benzoyl-S-coenzyme A S-Benzoate coenzyme A S-benzoyl-coenzyme A 3'-phosphoadenosine 5'-(3-{(3R)-4-[(3-{[2-(benzoylsulfanyl)ethyl]amino}-3-oxopropyl)amino]-3-hydroxy-2,2-dimethyl-4-oxobutyl} dihydrogen diphosphate) small molecule small molecule chemical synthesis Chemical synthesis (Chemical synthesis) paaa_ecoli 1,2-phenylacetyl-CoA epoxidase, subunit A ydbO paaA b1388 JW1383 1,2-phenylacetyl-CoA epoxidase, catalytic subunit alpha 1,2-phenylacetyl-CoA monooxygenase, subunit A protein protein ecoli Escherichia coli (strain K12) MTQEERFEQRIAQETAIEPQDWMPDAYRKTLIRQIGQHAHSEIVGMLPEGNWITRAPTLRRKAILLAKVQDEAGHGLYLYSAAETLGCAREDIYQKMLDGRMKYSSIFNYPTLSWADIGVIGWLVDGAAIVNQVALCRTSYGPYARAMVKICKEESFHQRQGFEACMALAQGSEAQKQMLQDAINRFWWPALMMFGPNDDNSPNSARSLTWKIKRFTNDELRQRFVDNTVPQVEMLGMTVPDPDLHFDTESGHYRFGEIDWQEFNEVINGRGICNQERLDAKRKAWEEGTWVREAALAHAQKQHARKVA 83AEC6D7AC084073 paaa-paac-1 2 12 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed 10 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Table 1 paac-paab-1 2 5 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed 10 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range physical association physical association Table 1 Interaction only observed in the absence of salt. paac-paaa-1 2 5 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed 12 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed 10 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range association association Table 1 paac-paaa-2 2 5 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed 12 unspecified role unspecified role bait bait over-expressed over expressed level over-expressed n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range 10 unspecified role unspecified role prey prey over-expressed over expressed level over-expressed association association Table 1 paaa-paab-1 1 4 enzyme target enzyme target substrate substrate neutral component neutral component purified purified 8 ancillary ancillary neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 10 ancillary ancillary neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 5 ancillary ancillary neutral component neutral component purified purified ecoli Escherichia coli (strain K12) 12 enzyme enzyme neutral component neutral component purified purified ecoli Escherichia coli (strain K12) redox reaction oxidoreductase activity electron transfer reaction redox reaction In vitro reconstitution of the oxygenase subunits showed that each of the PaaA, B, C, and E subunits are necessary for catalysis Addition of PAAD_ECOLI (P76080) had no effect on reaction rate. Deletion of any other subunit decreased reaction rate. Table 4 paaa-paac-2 3 10 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 42 40 direct interaction direct interaction Rworking 0.234 Rfree 0.267 2.65A Table 3 We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. 3_hydroxybutanoyl_coa-paaa-1 3 9 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Rworking 0.195 Rfree 0.23 2.03A Table 3 We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. acetyl_coa-paaa-1 3 7 unspecified role unspecified role neutral component neutral component purified purified 10 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Rworking 0.206 Rfree 0.259 2.97A Table 3 We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. benzoyl_coa-paaa-1 3 11 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Rworking 0.188 Rfree 0.225 2.06A Table 3 We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. coenzyme a-paaa-1 3 12 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 6 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Rworking 0.19 Rfree 0.224 2.15A Table 3 We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives. paaa-paac-3 3 4 unspecified role unspecified role neutral component neutral component 10 unspecified role unspecified role neutral component neutral component purified purified n-terminal his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag n-term range n-terminal range n-term range n-term range n-terminal range n-term range region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) 12 unspecified role unspecified role neutral component neutral component purified purified region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain ecoli Escherichia coli (strain K12) direct interaction direct interaction Rworking 0.186 Rfree 0.233 2.25A Table 3 We have determined the crystal structure of the PaaAC complex in a ligand-free form and with several CoA derivatives.