IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Crystal structure of naphthalene dioxygenase: side-on binding of dioxygen to iron. Science (0036-8075) 2003 Karlsson A., Parales JV., Parales RE., Gibson DT., Eklund H., Ramaswamy S. PDBe - Data obtained from the Protein Data Bank Europe in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Karlsson A., Parales JV., Parales RE., Gibson DT., Eklund H., Ramaswamy S. PDBe - Data obtained from the Protein Data Bank Europe Science (0036-8075) 2003 Substrate binding site of naphthalene 1,2-dioxygenase: functional implications of indole binding. Substrate binding site of naphthalene 1,2-dioxygenase: functional implications of indole binding. J. Mol. Biol. (0022-2836) 2000 Carredano E., Karlsson A., Kauppi B., Choudhury D., Parales RE., Parales JV., Lee K., Gibson DT., Eklund H., Ramaswamy S. PDBe - Data obtained from the Protein Data Bank Europe in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Carredano E., Karlsson A., Kauppi B., Choudhury D., Parales RE., Parales JV., Lee K., Gibson DT., Eklund H., Ramaswamy S. PDBe - Data obtained from the Protein Data Bank Europe J. Mol. Biol. (0022-2836) 2000 p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit. p-Cresol methylhydroxylase: alteration of the structure of the flavoprotein subunit upon its binding to the cytochrome subunit. Biochemistry (0006-2960) 2005 Cunane LM., Chen ZW., McIntire WS., Mathews FS. PDBe - Data obtained from the Protein Data Bank Europe in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Cunane LM., Chen ZW., McIntire WS., Mathews FS. PDBe - Data obtained from the Protein Data Bank Europe Biochemistry (0006-2960) 2005 The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates. The axial tyrosinate Fe3+ ligand in protocatechuate 3,4-dioxygenase influences substrate binding and product release: evidence for new reaction cycle intermediates. Biochemistry (0006-2960) 1998 Frazee RW., Orville AM., Dolbeare KB., Yu H., Ohlendorf DH., Lipscomb JD. PDBe - Data obtained from the Protein Data Bank Europe in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Frazee RW., Orville AM., Dolbeare KB., Yu H., Ohlendorf DH., Lipscomb JD. PDBe - Data obtained from the Protein Data Bank Europe Biochemistry (0006-2960) 1998 cy4c_psepu 4-cresol dehydrogenase [hydroxylating] cytochrome c subunit pchC Flavocytochrome c P-cresol methylhydroxylase cytochrome subunit protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MTFPFSGAAVKRMLVTGVVLPFGLLVAAGQAQADSQWGSGKNLYDKVCGHCHKPEVGVGPVLEGRGLPEAYIKDIVRNGFRAMPAFPASYVDDESLTQVAEYLSSLPAPAAQP 568ED7438521C1E1 ndoc_psepu Naphthalene 1,2-dioxygenase system, small oxygenase component Naphthalene 1,2-dioxygenase subunit beta ndoC nahAD Naphthalene 1,2-dioxygenase ISP beta protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MMINIQEDKLVSAHDAEEILRFFNCHDSALQQEATTLLTQEAHLLDIQAYRAWLEHCVGSEVQYQVISRELRAASERRYKLNEAMNVYNENFQQLKVRVEHQLDPQNWGNSPKLRFTRFITNVQAAMDVNDKELLHIRSNVILHRARRGNQVDVFYAAREDKWKRGEGGVRKLVQRFVDYPERILQTHNLMVFL 168D2E1535E66416 pcxb_psepu Protocatechuate 3,4-dioxygenase beta chain 3,4-PCD pcaH protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MPAQDNSRFVIRDRNWHPKALTPDYKTSIARSPRQALVSIPQSISETTGPNFSHLGFGAHDHDLLLNFNNGGLPIGERIIVAGRVVDQYGKPVPNTLVEMWQANAGGRYRHKNDRYLAPLDPNFGGVGRCLTDSDGYYSFRTIKPGPYPWRNGPNDWRPAHIHFGISGPSIATKLITQLYFEGDPLIPMCPIVKSIANPEAVQQLIAKLDMNNANPMDCLAYRFDIVLRGQRKTHFENC 8F8CC293B6E434CE pcxa_psepu Protocatechuate 3,4-dioxygenase alpha chain pcaG 3,4-PCD protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MPIELLPETPSQTAGPYVHIGLALEAAGNPTRDQEIWNRLAKPDAPGEHILLLGQVYDGNGHLVRDSFLEVWQADANGEYQDAYNLENAFNSFGRTATTFDAGEWTLHTVKPGVVNNAAGVPMAPHINISLFARGINIHLHTRLYFDDEAQANAKCPVLNLIEQPQRRETLIAKRCEVDGKTAYRFDIRIQGEGETVFFDF BF95DB892076FBAF dh4c_psepu 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit pchF P-cresol methylhydroxylase protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MSEQNNAVLPKGVTQGEFNKAVQKFRALLGDDNVLVESDQLVPYNKIMMPVENAAHAPSAAVTATTVEQVQGVVKICNEHKIPIWTISTGRNFGYGSAAPVQRGQVILDLKKMNKIIKIDPEMCYALVEPGVTFGQMYDYIQENNLPVMLSFSAPSAIAGPVGNTMDRGVGYTPYGEHFMMQCGMEVVLANGDVYRTGMGGVPGSNTWQIFKWGYGPTLDGMFTQANYGICTKMGFWLMPKPPVFKPFEVIFEDEADIVEIVDALRPLRMSNTIPNSVVIASTLWEAGSAHLTRAQYTTEPGHTPDSVIKQMQKDTGMGAWNLYAALYGTQEQVDVNWKIVTDVFKKLGKGRIVTQEEAGDTQPFKYRAQLMSGVPNLQEFGLYNWRGGGGSMWFAPVSEARGSECKKQAAMAKRVLHKYGLDYVAEFIVAPRDMHHVIDVLYDRTNPEETKRADACFNELLDEFEKEGYAVYRVNTRFQDRVAQSYGPVKRKLEHAIKRAVDPNNILAPGRSGIDLNNDF CFF28ACD77FDC2DE ndob_psepu Naphthalene 1,2-dioxygenase system, large oxygenase component ISP NAP Naphthalene 1,2-dioxygenase subunit alpha ndoB nahA3 nahAC ndoC2 Naphthalene 1,2-dioxygenase ISP alpha protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MNYNNKILVSESGLSQKHLIHGDEELFQHELKTIFARNWLFLTHDSLIPAPGDYVTAKMGIDEVIVSRQNDGSIRAFLNVCRHRGKTLVSVEAGNAKGFVCSYHGWGFGSNGELQSVPFEKDLYGESLNKKCLGLKEVARVESFHGFIYGCFDQEAPPLMDYLGDAAWYLEPMFKHSGGLELVGPPGKVVIKANWKAPAENFVGDAYHVGWTHASSLRSGESIFSSLAGNAALPPEGAGLQMTSKYGSGMGVLWDGYSGVHSADLVPELMAFGGAKQERLNKEIGDVRARIYRSHLNCTVFPNNSMLTCSGVFKVWNPIDANTTEVWTYAIVEKDMPEDLKRRLADSVQRTFGPAGFWESDDNDNMETASQNGKKYQSRDSDLLSNLGFGEDVYGDAVYPGVVGKSAIGETSYRGFYRAYQAHVSSSNWAEFEHASSTWHTELTKTTDR 1FD2F42296B4F7A8 pcag-pcah-1 4 8 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain psefl Pseudomonas fluorescens 7 unspecified role unspecified role neutral component neutral component region sufficient to bind sufficient binding region sufficient to bind certain certain sequence position certain certain certain sequence position certain psefl Pseudomonas fluorescens direct interaction direct interaction 24meric, multimeric working 82.00% 2.1A ndob-ndoc-1 2 6 unspecified role unspecified role neutral component neutral component 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) 10 unspecified role unspecified role neutral component neutral component 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 dodecameric, multimeric working 81.00%, free 78.00% 1.6A ndob-ndoc-2 1 6 unspecified role unspecified role neutral component neutral component 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) 10 unspecified role unspecified role neutral component neutral component 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 hexameric, multimeric 1.7A ndob-ndoc-3 1 10 unspecified role unspecified role neutral component neutral component 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 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 hexameric, multimeric 2.2A ndob-ndoc-4 1 10 unspecified role unspecified role neutral component neutral component 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 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 hexameric, multimeric 1.75A ndob-ndoc-5 1 6 unspecified role unspecified role neutral component neutral component 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) 10 unspecified role unspecified role neutral component neutral component 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 hexameric, multimeric 1.4A ndob-ndoc-6 1 10 unspecified role unspecified role neutral component neutral component 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 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 hexameric, multimeric 1.95A ndob-ndoc-7 1 6 unspecified role unspecified role neutral component neutral component 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) 10 unspecified role unspecified role neutral component neutral component 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 hexameric, multimeric 1.9A pchc-pchf-1 3 5 unspecified role unspecified role neutral component neutral component 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) 9 unspecified role unspecified role neutral component neutral component 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 tetrameric, multimeric working 84.100%, free 80.600% 1.85A mpidb The Microbial Protein Interaction Database Characterization of the traD operon of naphthalene-catabolic plasmid NAH7: a host-range modifier in conjugative transfer. Characterization of the traD operon of naphthalene-catabolic plasmid NAH7: a host-range modifier in conjugative transfer. J. Bacteriol. (0021-9193) 2008 imex curation Miyazaki R., Ohtsubo Y., Nagata Y., Tsuda M. 04-Feb-2013: Contacted by IntAct-Help. Only protein-protein interactions ecolx Escherichia coli adenylate cyclase adenylate cyclase complementation bacterial two-hybrid bacterial two-hybrid adenylate cyclase predetermined predetermined participant predetermined Miyazaki R., Ohtsubo Y., Nagata Y., Tsuda M. Accepted 2013-JAN-28 by ORCHARD 04-Feb-2013: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2008 Only protein-protein interactions imex curation An antirepressor, SrpR, is involved in transcriptional regulation of the SrpABC solvent tolerance efflux pump of Pseudomonas putida S12. An antirepressor, SrpR, is involved in transcriptional regulation of the SrpABC solvent tolerance efflux pump of Pseudomonas putida S12. J. Bacteriol. (0021-9193) 2011 imex curation Sun X., Zahir Z., Lynch K.H., Dennis J.J. 18-Dec-2012: Contacted by IntAct-Help. Only protein-protein interactions in vitro In vitro pull down pull down anti tag western anti tag western blot anti tag western Sun X., Zahir Z., Lynch K.H., Dennis J.J. Accepted 2012-DEC-11 by ORCHARD 18-Dec-2012: Contacted by IntAct-Help. J. Bacteriol. (0021-9193) 2011 Only protein-protein interactions imex curation q1xgm8_psepu traB protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MHKREVDSAVMTAGFGLPIAGWAAGVYFAQMPLTPFPAAFKETLHNGWHNPIVLGATIATSAVAASLVYYLYEYCDDGFRGEQYQEFLRGSEIKNWHTVKAKVRRRNEKTNRERKKWGLAKSEPIMIGKLPMPLHLEDRNTMICASIGAGKSVTMEGMIASALKRGDRLAVVDPNGTFYSKFSFKGDSILNPFDERSVGWTIFNEIRGIHDFNRMAKSIIPPQVDPSDEQWCAYARDVLSDTMRKLKETNNPDQDTLVNLLVREDGDTIRAFLANTDSEGYFRDNAEKAIASIQFMMNKYIRPLRYMSKGEFSIYKWVNDPNAGNLFITWREDMRDTMKPLVATWIDTICATILSSEPMTGKRLWLFLDELQSLGKLESFVPAATKGRKHGLRMVGSLQDWSQLNASYGRDDAETLLSCFRNYVILAAANAKNAGMASEILGSHDVKRWRKSYTAGKLTRTEEVTRDEPVVQASEISNLPDLVAYVKFGEDFPITKVKTPYIDYKERAQAIMLTGQAAA 9F7461B3F1287F27 q1xgm7_psepu traC protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MFNVTSIKGSNQYAAAGYYTAADDYYAKESPGEWQGIGAELLGLAGPIDQKELAKLFDGKLPNGEVMPKTFDKETGNRRMGLDLTFSAPKSVSMQALIAGDKDVVAAHDRAVTKAMEHVEKLAQARRKEHGKSMLERTGNLIIGKFRHELSRAKDPQLHTHAVVMNATRREDGKWRAIHNDDIFKIQPQIDAMYKGELAKELRELGYEIRVLDKDGNFELAHISRDQIEAFSSRAKVIEEALAKDGKTRSNATALEKQIIAMATRPRKDERDRHLVKEYWVTKARDLGIEFGGRSQLDNQEYGRRSESIHAEHNLPEGITAGQAVVQYAINHLTEREQVVGESDLRTAALRRAVGLASPSEVDDEIKRLVKQGTLIESPPTYRMATGKDGAALSPAGWRALLKEQKGWSEKEAQQYVKMAINRGSLVEAEKRYTTQRALKREKAILAIERSGRGQVAPLLSKEQVAKALESSTLSAGQYQAVEVIVSTSNRFVGIQGDAGTGKTYSVDRAVKLIESVNNAMTERSTTTDAVFRVVALAPYGNQVTALKNEGLDAHTLASFFHTKDKKLDERTIVVLDEAGVVGARQMEQLMRIIEQSGARLVQLGDTKQTEAIEAGKPFAQLQQNGMQTARIKEIQRQKNQELKIAVQHAADGNPGKSLEHVNHVEELREPGQRHQAIVRDYMSLTPQERKEVLIVAGTNKDRKQINAMTRESLGLVGNGKELPTLNRVDTTQAERRYAPSYKKGMIVQPEKDYIRAGLSRGELYTVDQALPGNVLVVKDKNGNRVEFNPRKLTKLSVYNLEKPEFSVGDLVRITRNDQKLDLTNGDRMRVVGNANGVIELASLKEKDGTPERVVALPTNRPLHLEHAYSATVHSAQGLTNDRVMISINTKSLTTSQNLWYVAISRARHEARIYTDSIAGLPAAIANRYDKTTALSLQQARERQRNESIKPRTVLDGKELERKQRSALDGAGLGKSGV 6ED0AC2D227E8B5C q1xgi2_psepu mpfH protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MAKEPNNPIDQPAAKTREEEMAEWNESQSNSMLKAGSGGKRSGVLMIGAAVVACGFVYWLKHDNGETAAPEKTDEIVAAERRKVQDPTPKREAAKVKPVTNDGEPGAPADTPRSTAERQTQQEGLSEAERQRQALEFQEEVARKKMLAARQRSAIFATAKDDGFAQGRDDQDPAQQPTGGSLLGGNSGNSGRVSRNANENFASSTYSSGVPVAKARALENLQFKVLQGAVIEATLQPRAQSQLPGQICVSVAQDVYAAEGRRVLIPWGSSVCGSYNASLAPGQERLFTVWNWLRMPKLSGRRAMEIPLDSAGSDQLGSAGQGGVVDNHWAQIFGVAAAVSIIGAGASNSGVSSGDQDNSASQYRTQVQEAAAESSQTILSRYANIQPTVTVPHGSRVVIYLQRDLDFTEQFAEEAKEADNGGVKFIN F53BFF9D7B7F0D62 q49kf1_psepu traE protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MSRADKNEAITKADMAVFQEERQNLETDLLDEVLKSRRVAWWVATGLGALAGVALAVTGFTMYRYSQPVPAHMLVMNSDGTIQQVSLLTPQSSYGDVADTYWVSTFIRHYESYEFNTAQADYDAIGLMAGPDVAEDYQKRYKWGTKEAMDKTVGDRKSVKVKVSSVILDRETGIATVRFSTTEKYRTRGADEAPQFWIATLSYRYDNMELTAAQRYINPAGFRVYSYRVNAESVASVGGR 1D7DE1775BF10CFD srps_psepu HTH-type transcriptional regulator SrpS srpS Solvent efflux pump srpABC operon corepressor protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MNQSDENVGKAGGIQVIARAASIMRALGSHPHGLSLAAIAQLVGLPRSTVQRIINALEEEFLVEALGPAGGFRLGPALGQLINQAQSDILSLVKPYLRSLAEELEESVCLASLAGDKIYVLDRIVSERELRVVFPIGINVPAAATAAGKVLLAALPDETLQAALGEQLPVFTSNTLRRKALVKQLSEVRQSGFASDLDEHIDGVCSFATLLDTYLGYYSLAVVMPSSRASKQSDLIKKALLQSKQNIERAIGRASKKAP 322E1DF03842C211 srpr_psepu HTH-type transcriptional regulator SrpR srpR Solvent efflux pump srpABC operon corepressor protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MARKTAAEAEETRQRIIDAALEVFVAQGVSDATLDQIARKAGVTRGAVYWHFNGKLEVLQAVLASRQHPLELDFTPDLGIERSWEAVVVAMLDAVHSPQSKQFSEILIYQGLDESGLIHNRMVQASDRFLQYIHQVLRHAVTQGELPINLDLQTSIGVFKGLITGLLYEGLRSKDQQAQIIKVALGSFWALLREPPRFLLCEEAQIKQVKSFE 2201B522EC4B1813 trac-trae 1 4 unspecified role unspecified role bait bait 6 unspecified role unspecified role prey prey physical association physical association Table 2 trab-trae 1 6 unspecified role unspecified role prey prey 3 unspecified role unspecified role bait bait physical association physical association Table 2 trae-trae 1 6 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait physical association physical association Table 2 mpfh-mpfh 1 5 unspecified role unspecified role prey prey 5 unspecified role unspecified role bait bait physical association physical association Table 2 trac-mpfh 1 4 unspecified role unspecified role bait bait 5 unspecified role unspecified role prey prey physical association physical association Table 2 trab-mpfh 1 3 unspecified role unspecified role bait bait 5 unspecified role unspecified role prey prey physical association physical association Table 1 trae-mpfh 1 5 unspecified role unspecified role prey prey 6 unspecified role unspecified role bait bait physical association physical association Table 2 trac-trab 1 3 unspecified role unspecified role prey prey 4 unspecified role unspecified role bait bait physical association physical association Table 2 srpr-srps 2 7 unspecified role unspecified role prey prey q9r9u0-- Q9R9U0-- his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli 8 unspecified role unspecified role bait bait q9r9t9-- Q9R9T9-- gst tag glutathione s tranferase tag glutathione S-tranferase tag glutathione S-tranferase tag gst tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined ecolx Escherichia coli physical association physical association figure 5 MINT MINT, Dpt of Biology, University of Rome Tor Vergata MINT http://mint.bio.uniroma2.it/mint url>http://mint.bio.uniroma2.it/mint/ https://mint.bio.uniroma2.it MINT-[0-9]+ https://mint.bio.uniroma2.it/index.php/results-interactions/?id=${ac} The Molecular INTeraction database (MINT) is a relational database designed to store interactions between biological molecules. http://mint.bio.uniroma2.it Kinetics of hydrolysis and mutational analysis of N,N-diethyl-m-toluamide hydrolase from Pseudomonas putida DTB. Kinetics of hydrolysis and mutational analysis of N,N-diethyl-m-toluamide hydrolase from Pseudomonas putida DTB. FEBS J. (1742-464X) 2012 Rivera-Cancel G., Sanders JM., Hay AG. in vitro In vitro molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Rivera-Cancel G., Sanders JM., Hay AG. FEBS J. (1742-464X) 2012 a3r4e0_psepu protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MTQNHNNPAGHPDGASESAFDNSIATRSLAALPAPRKDRSVVEPFWAERLTGYLRTRDGEELRYSALLPKGDGPFPTLLHFSGYAPSAMGGKSYLNGRDYYPRSIDKQFLDAGYAIIGVNRRATGCSTGNMFDVHHPLYGQDGYDSVEFAAAQPWSTGAVGMYSWSWAGMSQLWTAIAQPPHLKAIAPGLVIADQRADSYAPGGVPQPAMLSNWPLSYVPMFWENIRDDAVAENDVRGLYQLEKNLKTLEEGSPGRLVLRHPNKDAYLEARAPARLAHKIQVPTLSLTAYQDEATTSRGGYYQWEVDPQLMWMIDTNGGHEMYMAETYRRQMLRFFDHFLKGAANGFENTPRLQIWQEAWLNPATERSTSICEDAFETAEPNFIVSRPTITPATEDVVFTLTSGGILSENGAPSTGSESFAYPVPSPSILAPEGWGPLDPRWREGSLAFTTPPLDRDLIPFGPASADLWICPDTATEADLQVTVTALLPDGQEMYIQRGWLRLSNRAIDPERSTSSRPVLLDDPEHYSPMIPGRPELARVEVNRFSTILRKGTRLRIWIETPGDTGMYKFSYSPVPTKLTIWHDASRISRFVMAVLTDEATEALPEKPQAILNQPCRKDPLTGC mint F36C8CCB1E95175C a3r4e0 1 DthA 2 predetermined predetermined participant predetermined predetermined predetermined participant predetermined unspecified role unspecified role neutral component neutral component purified purified his tag his tag his tag Hexa-His-tag 6-His-tag Histidine-tag Hexa-His-tag Histidine-tag 6-His-tag undetermined undetermined sequence position undetermined undetermined undetermined sequence position undetermined Stoichiometry: 4.0 direct interaction direct interaction sf2 mint DthA eluted at approximately 334 kDa on a size exclusion chromatography column (Fig. S2). This is between the expected native mass for a tetramer or pentamer of DthA, 280 kDa and 350 kDa, respectively Pseudomonas putida (strain DTB) DIP Database of Interacting Proteins 611 Young Drive East; Los Angeles CA 90095; USA http://dip.doe-mbi.ucla.edu/ dip@mbi.ucla.edu Structural basis for effector control and redox partner recognition in cytochrome P450. Structural basis for effector control and redox partner recognition in cytochrome P450. Science (New York, N.Y.) 2013 imex curation Tripathi S., Li H., Poulos TL. Only protein-protein interactions in vitro In vitro x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Tripathi S., Li H., Poulos TL. DIP original experiment: DIP-264982X Science (New York, N.Y.) 2013 IMEx Structural basis for effector control and redox partner recognition in cytochrome P450. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. Nature structural biology 1999 imex curation Aevarsson A., Seger K., Turley S., Sokatch JR., Hol WG. Only protein-protein interactions psepu Pseudomonas putida Arthrobacter siderocapsulatus x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Aevarsson A., Seger K., Turley S., Sokatch JR., Hol WG. DIP original experiment: DIP-262985X Nature structural biology 1999 IMEx Crystal structure of 2-oxoisovalerate and dehydrogenase and the architecture of 2-oxo acid dehydrogenase multienzyme complexes. 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. Structure (London, England : 1993) 2005 imex curation Martins BM., Svetlitchnaia T., Dobbek H. Only protein-protein interactions psepu Pseudomonas putida Arthrobacter siderocapsulatus molecular sieving molecular sieving Gel Filtration Size Exclusion Chromatography Size Exclusion Chromatography Gel Filtration Sizing column predetermined predetermined participant predetermined Martins BM., Svetlitchnaia T., Dobbek H. DIP original experiment: DIP-132771X Structure (London, England : 1993) 2005 IMEx 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. Structural basis for effector control and redox partner recognition in cytochrome P450. Structural basis for effector control and redox partner recognition in cytochrome P450. Science (New York, N.Y.) 2013 imex curation Tripathi S., Li H., Poulos TL. Only protein-protein interactions in vitro In vitro crosslink cross-linking study crosslink predetermined predetermined participant predetermined Tripathi S., Li H., Poulos TL. DIP original experiment: DIP-264983X Science (New York, N.Y.) 2013 IMEx Structural basis for effector control and redox partner recognition in cytochrome P450. 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. Structure (London, England : 1993) 2005 imex curation Martins BM., Svetlitchnaia T., Dobbek H. Only protein-protein interactions psepu Pseudomonas putida Arthrobacter siderocapsulatus x-ray diffraction x-ray crystallography X-ray X-ray x-ray diffraction predetermined predetermined participant predetermined Martins BM., Svetlitchnaia T., Dobbek H. DIP original experiment: DIP-132770X Structure (London, England : 1993) 2005 IMEx 2-Oxoquinoline 8-monooxygenase oxygenase component: active site modulation by Rieske-[2Fe-2S] center oxidation/reduction. A functional proline switch in cytochrome P450cam. A functional proline switch in cytochrome P450cam. Structure (London, England : 1993) 2008 imex curation OuYang B., Pochapsky SS., Dang M., Pochapsky TC. Only protein-protein interactions in vitro In vitro nmr nuclear magnetic resonance NMR NMR nmr predetermined predetermined participant predetermined OuYang B., Pochapsky SS., Dang M., Pochapsky TC. DIP original experiment: DIP-68474X Structure (London, England : 1993) 2008 IMEx A functional proline switch in cytochrome P450cam. o05935_psepu KF715C_ch5870 oxoO protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MSDQPIIRRRQVKTGISDARANNAKTQSQYQPYKDAAWGFINHWYPALFTHELEEDQVQGIQICGVPIVLRRVNGKVFALKDQCLHRGVRLSEKPTCFTKSTISCWYHGFTFDLETGKLVTIVANPEDKLIGTTGVTTYPVHEVNGMIFVFVREDDFPDEDVPPLAHDLPFRFPERSEQFPHPLWPSSPSVLDDNAVVHGMHRTGFGNWRIACENGFDNAHILVHKDNTIVHAMDWVLPLGLLPTSDDCIAVVEDDDGPKGMMQWLFTDKWAPVLENQELGLKVEGLKGRHYRTSVVLPGVLMVENWPEEHVVQYEWYVPITDDTHEYWEILVRVCPTDEDRKKFQYRYDHMYKPLCLHGFNDSDLYAREAMQNFYYDGTGWDDEQLVATDISPITWRKLASRWNRGIAKPGRGVAGAVKDTSLIFKQTADGKRPGYKVEQIKEDH DIP protein O05935 original sequence version: 44 putx_psepu Putidaredoxin camB protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MSKVVYVSHDGTRRELDVADGVSLMQAAVSNGIYDIVGDCGGSASCATCHVYVNEAFTDKVPAANEREIGMLECVTAELKPNSRLCCQIIMTPELDGIVVDVPDRQW DIP protein P00259 original sequence version: 81 DIP protein P00259 original sequence version: 109 cpxa_psepu Camphor 5-monooxygenase camC cyp101 Cytochrome P450-cam protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MTTETIQSNANLAPLPPHVPEHLVFDFDMYNPSNLSAGVQEAWAVLQESNVPDLVWTRCNGGHWIATRGQLIREAYEDYRHFSSECPFIPREAGEAYDFIPTSMDPPEQRQFRALANQVVGMPVVDKLENRIQELACSLIESLRPQGQCNFTEDYAEPFPIRIFMLLAGLPEEDIPHLKYLTDQMTRPDGSMTFAEAKEALYDYLIPIIEQRRQKPGTDAISIVANGQVNGRPITSDEAKRMCGLLLVGGLDTVVNFLSFSMEFLAKSPEHRQELIERPERIPAACEELLRRFSLVADGRILTSDYEFHGVQLKKGDQILLPQMLSGLDERENACPMHVDFSRQKVSHTTFGHGSHLCLGQHLARREIIVTLKEWLTRIPDFSIAPGAQIQHKSGIVSGVQALPLVWDPATTKAV DIP protein P00183 original sequence version: 93 DIP protein P00183 original sequence version: 137 odbb_psepu 2-oxoisovalerate dehydrogenase subunit beta bkdA2 Branched-chain alpha-keto acid dehydrogenase E1 component beta chain protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MATTTMTMIQALRSAMDVMLERDDNVVVYGQDVGYFGGVFRCTEGLQTKYGKSRVFDAPISESGIVGTAVGMGAYGLRPVVEIQFADYFYPASDQIVSEMARLRYRSAGEFIAPLTLRMPCGGGIYGGQTHSQSPEAMFTQVCGLRTVMPSNPYDAKGLLIASIECDDPVIFLEPKRLYNGPFDGHHDRPVTPWSKHPHSAVPDGYYTVPLDKAAITRPGNDVSVLTYGTTVYVAQVAAEESGVDAEVIDLRSLWPLDLDTIVESVKKTGRCVVVHEATRTCGFGAELVSLVQEHCFHHLEAPIERVTGWDTPYPHAQEWAYFPGPSRVGAALKKVMEV DIP protein P09061 original sequence version: 90 318FE1E403B2AEA5 odba_psepu 2-oxoisovalerate dehydrogenase subunit alpha bkdA1 Branched-chain alpha-keto acid dehydrogenase E1 component alpha chain protein protein psepu Pseudomonas putida Arthrobacter siderocapsulatus MNEYAPLRLHVPEPTGRPGCQTDFSYLRLNDAGQARKPPVDVDAADTADLSYSLVRVLDEQGDAQGPWAEDIDPQILRQGMRAMLKTRIFDSRMVVAQRQKKMSFYMQSLGEEAIGSGQALALNRTDMCFPTYRQQSILMARDVSLVEMICQLLSNERDPLKGRQLPIMYSVREAGFFTISGNLATQFVQAVGWAMASAIKGDTKIASAWIGDGATAESDFHTALTFAHVYRAPVILNVVNNQWAISTFQAIAGGESTTFAGRGVGCGIASLRVDGNDFVAVYAASRWAAERARRGLGPSLIEWVTYRAGPHSTSDDPSKYRPADDWSHFPLGDPIARLKQHLIKIGHWSEEEHQATTAEFEAAVIAAQKEAEQYGTLANGHIPSAASMFEDVYKEMPDHLRRQRQELGV DIP protein P09060 original sequence version: 86 0C998460CCFB9CF4 bkda1-bkda2-1 2 10 unspecified role unspecified role unspecified role unspecified role 2-339 binding region 2-339 binding region binding region binding-associated region binding region predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain psepu Pseudomonas putida Arthrobacter siderocapsulatus 11 unspecified role unspecified role unspecified role unspecified role 2-408 binding region 2-408 binding region binding region binding-associated region binding region predetermined featur predetermined feature predetermined featur certain certain sequence position certain certain certain sequence position certain psepu Pseudomonas putida Arthrobacter siderocapsulatus direct interaction direct interaction oxoo-1 5 7 unspecified role unspecified role unspecified role unspecified role psepu Pseudomonas putida Arthrobacter siderocapsulatus direct interaction direct interaction oxoo-2 3 7 unspecified role unspecified role unspecified role unspecified role psepu Pseudomonas putida Arthrobacter siderocapsulatus direct interaction direct interaction camb-camc-1 6 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction camb-camc-2 1 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction camb-camc-3 4 9 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli 8 unspecified role unspecified role unspecified role unspecified role ecolx Escherichia coli direct interaction direct interaction