{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q53353","uniProtkbId":"LSDX1_SPHPI","entryAudit":{"firstPublicDate":"2012-04-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":74,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Lignostilbene-alpha,beta-dioxygenase isozyme I"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"Reference","id":"Ref.4"}],"value":"LSD-I"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"1.13.11.43"}]}},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1368688"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763879"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21340"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17501"},{"database":"ChEBI","id":"CHEBI:18346"}],"ecNumber":"1.13.11.43","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763879"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763879"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763879"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"1 Fe(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12843670"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14506920"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}],"value":"Activity is high with beta-1 type stilbene and minimal with beta-5 type stilbene. A 4-hydroxyl group and trans-stilbene structure is essential for the binding of substrates to the enzyme. Inhibited by N-benzylideneaniline-hydroxy and -methoxy derivatives and N-(4-hydroxybenzyl)-3-methoxyaniline but not N-benzylideneaniline. Fluorinated olefin (Z)-1-fluoro-1(4-hydroxyphenyl)-2-phenylethylene is also a potent inhibitor. Imine linkage instead of ethylene bridge in the substrate enhances the inhibitory activity"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":11.0,"unit":"uM","substrate":"1,2-bis(4-hydroxy-3-methoxyphenyl)-ethylene","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14506920"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}]},{"constant":110.0,"unit":"uM","substrate":"oxygen","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14506920"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}]},{"constant":8.3,"unit":"uM","substrate":"4-hydroxystilbene","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14506920"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14506920"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"Optimum pH is 8.5. Active from 5.5-10.5."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14506920"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"Optimum temperature is 30 degrees Celsius. Stable at 4 degrees Celsius with minimal loss of activity."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763879"},{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"Homodimer of two alpha subunits"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the carotenoid oxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763879"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":485,"modifier":"EXACT"}},"description":"Lignostilbene-alpha,beta-dioxygenase isozyme I","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}],"featureId":"PRO_0000416940"},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":472,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Helix","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Turn","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Turn","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Turn","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJT"}]},{"type":"Beta strand","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Turn","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJT"}]},{"type":"Beta strand","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Turn","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":437,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Turn","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":449,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":458,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Beta strand","location":{"start":{"value":473,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]},{"type":"Helix","location":{"start":{"value":478,"modifier":"EXACT"},"end":{"value":480,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"6OJR"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0439","category":"Biological process","name":"Lignin degradation"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"7763879","citationType":"journal article","authors":["Kamoda S.","Saburi Y."],"citationCrossReferences":[{"database":"PubMed","id":"7763879"},{"database":"DOI","id":"10.1271/bbb.57.926"}],"title":"Cloning, expression, and sequence analysis of a lignostilbene-alpha,beta-dioxygenase gene from Pseudomonas paucimobilis TMY1009.","publicationDate":"1993","journal":"Biosci. Biotechnol. Biochem.","firstPage":"926","lastPage":"930","volume":"57"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-26","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAC60447.2"}],"value":"TMY1009","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000305"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAC60447.2"}]},{"referenceNumber":2,"citation":{"id":"1368688","citationType":"journal article","authors":["Kamoda S.","Samejima M."],"citationCrossReferences":[{"database":"PubMed","id":"1368688"},{"database":"DOI","id":"10.1271/bbb1961.55.1411"}],"title":"Cloning of a lignostilbene-alpha,beta-dioxygenase gene from Pseudomonas paucimobilis TMY1009.","publicationDate":"1991","journal":"Agric. Biol. Chem.","firstPage":"1411","lastPage":"1412","volume":"55"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"1368688"}],"value":"TMY1009","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000305"}]},{"referenceNumber":3,"citation":{"id":"7763880","citationType":"journal article","authors":["Kamoda S.","Saburi Y."],"citationCrossReferences":[{"database":"PubMed","id":"7763880"},{"database":"DOI","id":"10.1271/bbb.57.931"}],"title":"Structural and enzymatical comparison of lignostilbene-alpha,beta-dioxygenase isozymes, I, II, and III, from Pseudomonas paucimobilis TMY1009.","publicationDate":"1993","journal":"Biosci. Biotechnol. Biochem.","firstPage":"931","lastPage":"934","volume":"57"},"referencePositions":["PROTEIN SEQUENCE OF 2-26","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}],"value":"TMY1009","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000305"}]},{"referenceNumber":4,"citation":{"id":"CI-32HCCGP1IDD82","citationType":"journal article","authors":["Kamoda S.","Habu N.","Samejima M.","Yoshimoto T."],"citationCrossReferences":[{"database":"DOI","id":"10.1271/bbb1961.53.2757"}],"title":"Purification and some properties of lignostilbene-alpha,beta-dioxygenase responsible for the c-alpha-c-beta cleavage of a diarylpropane type lignin model compound from Pseudomonas sp. TMY1009.","publicationDate":"1989","journal":"Agric. Biol. Chem.","firstPage":"2757","lastPage":"2761","volume":"53"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"Reference","id":"Ref.4"}],"value":"TMY1009","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000305"}]},{"referenceNumber":5,"citation":{"id":"12843670","citationType":"journal article","authors":["Kamoda S.","Terada T.","Saburi Y."],"citationCrossReferences":[{"database":"PubMed","id":"12843670"},{"database":"DOI","id":"10.1271/bbb.67.1394"}],"title":"A common structure of substrate shared by lignostilbenedioxygenase isozymes from Sphingomonas paucimobilis TMY1009.","publicationDate":"2003","journal":"Biosci. Biotechnol. Biochem.","firstPage":"1394","lastPage":"1396","volume":"67"},"referencePositions":["ACTIVITY REGULATION"],"evidences":[{"evidenceCode":"ECO:0000305"}]},{"referenceNumber":6,"citation":{"id":"14506920","citationType":"journal article","authors":["Han S.Y.","Inoue H.","Terada T.","Kamoda S.","Saburi Y.","Sekimata K.","Saito T.","Kobayashi M.","Shinozaki K.","Yoshida S.","Asami T."],"citationCrossReferences":[{"database":"PubMed","id":"14506920"},{"database":"DOI","id":"10.1080/1475636031000080207"}],"title":"N-benzylideneaniline and N-benzylaniline are potent inhibitors of lignostilbene-alpha,beta-dioxygenase, a key enzyme in oxidative cleavage of the central double bond of lignostilbene.","publicationDate":"2003","journal":"J. Enzym. Inhib. Med. Chem.","firstPage":"279","lastPage":"283","volume":"18"},"referencePositions":["ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"S65040","properties":[{"key":"ProteinId","value":"AAC60447.2"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JN0595","properties":[{"key":"EntryName","value":"JN0595"}]},{"database":"PDB","id":"6OJR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.30 A"},{"key":"Chains","value":"A/B=2-483"}]},{"database":"PDB","id":"6OJT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.00 A"},{"key":"Chains","value":"A/B=2-482"}]},{"database":"PDB","id":"6OJW","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.60 A"},{"key":"Chains","value":"A/B=2-481"}]},{"database":"AlphaFoldDB","id":"Q53353","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q53353","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-18891","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0010436","properties":[{"key":"GoTerm","value":"F:carotenoid dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}]},{"database":"GO","id":"GO:0050054","properties":[{"key":"GoTerm","value":"F:lignostilbene alpha beta-dioxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7763880"}]},{"database":"GO","id":"GO:0016121","properties":[{"key":"GoTerm","value":"P:carotene catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046274","properties":[{"key":"GoTerm","value":"P:lignin catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7763880"}]},{"database":"InterPro","id":"IPR004294","properties":[{"key":"EntryName","value":"Carotenoid_Oase"}]},{"database":"PANTHER","id":"PTHR10543","properties":[{"key":"EntryName","value":"BETA-CAROTENE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10543:SF89","properties":[{"key":"EntryName","value":"CAROTENOID 9,10(9',10')-CLEAVAGE DIOXYGENASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03055","properties":[{"key":"EntryName","value":"RPE65"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAHFPQTPGFSGTLRPLRIEGDILDIEIEGEVPPQLNGTFHRVHPDAQFPPRFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAYRNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEGYTNFDGKLQSQTFCAHPKIDPVTGNLCAFAYGAKGLMTLDMAYIEISPTGKLLKEIPFQNPYYCMMHDFGVTEDYAVFAVMPLLSSWDRLEQRLPFFGFDTTLPCYLGILPRNGDARDLRWFKTGNCFVGHVMNAFNDGTKVHIDMPVSRNNSFPFFDVHGAPFDPVAGQGFLTRWTVDMASNGDSFEKTERLFDRPDEFPRIDERYATRAYRHGWMLILDTEKPYEAPGGAFYALTNTLGHIDLATGKSSSWWAGPRCAIQEPCFIPRSPDAPEGDGYVIALVDDHVANYSDLAIFDAQHVDQGPIARAKLPVRIRQGLHGNWADASRLAVAA","length":485,"molWeight":54436,"crc64":"71A672E375D29A1C","md5":"72CECE462EFD83B2A433DD9B7DEA467E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Binding site":4,"Helix":12,"Beta strand":36,"Turn":6},"uniParcId":"UPI000004346A"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q93UV0","uniProtkbId":"SPT_SPHPI","entryAudit":{"firstPublicDate":"2022-08-03","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2001-12-01","entryVersion":125,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11279212"}],"value":"Serine palmitoyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11279212"}],"value":"SPT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"value":"2.3.1.50"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17559874"}],"value":"spt"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11279212"}],"value":"SPT1"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"NNG56642.1"}],"value":"HKX06_04505"},{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"QPT08440.1"}],"value":"I6G38_17245"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"value":"Catalyzes the condensation of L-serine with palmitoyl-CoA (hexadecanoyl-CoA) to produce 3-oxosphinganine (PubMed:11279212, PubMed:17557831, PubMed:17559874, PubMed:19376777). Exhibits a broad substrate specificity concerning the chain length and the degree of unsaturation of acyl-CoA (PubMed:11279212, PubMed:19376777)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-serine + hexadecanoyl-CoA + H(+) = 3-oxosphinganine + CO2 + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14761"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57379"},{"database":"ChEBI","id":"CHEBI:58299"}],"ecNumber":"2.3.1.50","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:14762"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"20445930"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23957439"}],"value":"Not inhibited by relatively high concentrations of palmitoyl-CoA (PubMed:11279212). Inhibited by both D-cycloserine (DCS) and L-cycloserine (LCS), which inactivate SPT by transamination to form a free pyridoxamine 5'-phosphate (PMP) and beta-aminooxyacetaldehyde that remain bound at the active site (PubMed:20445930). Inhibition is reversed by incubation with excess pyridoxal phosphate (PubMed:20445930). Inhibited by the fungal natural product myriocin, which acts as a competitive inhibitor for both L-serine and palmitoyl-CoA substrates (PubMed:23957439)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":4.23,"unit":"mM","substrate":"L-serine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"}]},{"constant":4.7,"unit":"mM","substrate":"L-serine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"}]},{"constant":1.4,"unit":"mM","substrate":"L-serine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]},{"constant":0.87,"unit":"mM","substrate":"palmitoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"}]},{"constant":0.69,"unit":"mM","substrate":"palmitoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"}]},{"constant":35.4,"unit":"uM","substrate":"palmitoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]},{"constant":2324.9,"unit":"uM","substrate":"decanoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]},{"constant":822.2,"unit":"uM","substrate":"lauroyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]},{"constant":97.1,"unit":"uM","substrate":"myristoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]},{"constant":13.7,"unit":"uM","substrate":"stearoyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"value":"kcat is 140 min(-1) with palmitoyl-CoA as substrate (PubMed:11279212). kcat is 2.3 sec(-1) with palmitoyl-CoA as substrate (PubMed:17557831). kcat is 1.150 sec(-1) with palmitoyl-CoA as substrate (PubMed:19376777). kcat is 0.045 sec(-1) with decanoyl-CoA as substrate (PubMed:19376777). kcat is 0.262 sec(-1) with lauroyl-CoA as substrate (PubMed:19376777). kcat is 0.601 sec(-1) with myristoyl-CoA as substrate (PubMed:19376777). kcat is 0.898 sec(-1) with stearoyl-CoA as substrate (PubMed:19376777). kcat is 0.327 sec(-1) with arachidoyl-CoA as substrate (PubMed:19376777)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"}],"value":"Optimum pH is 7.5 to 8.0."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"19376777"}],"value":"Lipid metabolism; sphingolipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"}],"value":"Distributed throughout the cytoplasm"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"Serine palmitoyltransferase","featureId":"PRO_0000456080"},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2JG2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8T"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8U"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8V"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2JG2"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2JG2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8T"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8U"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8V"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2JG2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8T"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8U"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8V"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Modified residue","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2JG2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8T"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8U"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8V"}]},{"type":"Mutagenesis","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"23-fold decrease in catalytic efficiency for L-serine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["C"]}},{"type":"Mutagenesis","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"147-fold decrease in catalytic efficiency for L-serine. Affects the chemistry of the pyridoxal phosphate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["W"]}},{"type":"Mutagenesis","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"410-fold decrease in catalytic efficiency for L-serine. Affects the chemistry of the pyridoxal phosphate. Is less able to stabilize a quinonoid intermediate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["Y"]}},{"type":"Mutagenesis","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Loss of activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23957439"}],"alternativeSequence":{"originalSequence":"K","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"40-fold decrease in catalytic efficiency for L-serine. Is less able to stabilize a quinonoid intermediate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"60-fold decrease in catalytic efficiency for L-serine.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["N"]}},{"type":"Helix","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8V"}]},{"type":"Helix","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2XBN"}]},{"type":"Beta strand","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Turn","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Turn","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Turn","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Turn","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8V"}]},{"type":"Beta strand","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8U"}]},{"type":"Beta strand","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Turn","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Beta strand","location":{"start":{"value":387,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]},{"type":"Helix","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":416,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2W8T"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"11279212","citationType":"journal article","authors":["Ikushiro H.","Hayashi H.","Kagamiyama H."],"citationCrossReferences":[{"database":"PubMed","id":"11279212"},{"database":"DOI","id":"10.1074/jbc.m101550200"}],"title":"A water-soluble homodimeric serine palmitoyltransferase from Sphingomonas paucimobilis EY2395T strain. Purification, characterization, cloning, and overproduction.","publicationDate":"2001","journal":"J. Biol. Chem.","firstPage":"18249","lastPage":"18256","volume":"276"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-6","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"],"referenceComments":[{"value":"EY2395","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"CI-CBGLB0GSFKA6B","citationType":"submission","authors":["Bijlani S.","Singh N.K.","Mason C.E.","Wang C.C.","Venkateswaran K."],"title":"Draft Genome Sequences of Sphingomonas sp. Isolated from the International Space Station.","publicationDate":"MAY-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"FKI-L5-BR-P1","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"CI-C8AIJS6VECB27","citationType":"submission","authors":["Sproer C.","Gronow S.","Severitt S.","Schroder I.","Tallon L.","Sadzewicz L.","Zhao X.","Boylan J.","Ott S.","Bowen H.","Vavikolanu K.","Mehta A.","Aluvathingal J.","Nadendla S.","Lowell S.","Myers T.","Yan Y.","Sichtig H."],"title":"FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): Supporting development and validation of Infectious Disease Dx tests.","publicationDate":"DEC-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 10829 / DSM 30198 / FDAARGOS_881","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"17557831","citationType":"journal article","authors":["Ikushiro H.","Islam M.M.","Tojo H.","Hayashi H."],"citationCrossReferences":[{"database":"PubMed","id":"17557831"},{"database":"DOI","id":"10.1128/jb.00194-07"}],"title":"Molecular characterization of membrane-associated soluble serine palmitoyltransferases from Sphingobacterium multivorum and Bdellovibrio stolpii.","publicationDate":"2007","journal":"J. Bacteriol.","firstPage":"5749","lastPage":"5761","volume":"189"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"ATCC 27052","type":"STRAIN"}]},{"referenceNumber":5,"citation":{"id":"17559874","citationType":"journal article","authors":["Yard B.A.","Carter L.G.","Johnson K.A.","Overton I.M.","Dorward M.","Liu H.","McMahon S.A.","Oke M.","Puech D.","Barton G.J.","Naismith J.H.","Campopiano D.J."],"citationCrossReferences":[{"database":"PubMed","id":"17559874"},{"database":"DOI","id":"10.1016/j.jmb.2007.04.086"}],"title":"The structure of serine palmitoyltransferase; gateway to sphingolipid biosynthesis.","publicationDate":"2007","journal":"J. Mol. Biol.","firstPage":"870","lastPage":"886","volume":"370"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH PYRIDOXAL PHOSPHATE","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","SUBUNIT"],"referenceComments":[{"value":"13361","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"2JG2"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2JGT"}]},{"referenceNumber":6,"citation":{"id":"19376777","citationType":"journal article","authors":["Raman M.C.C.","Johnson K.A.","Yard B.A.","Lowther J.","Carter L.G.","Naismith J.H.","Campopiano D.J."],"citationCrossReferences":[{"database":"PubMed","id":"19376777"},{"database":"DOI","id":"10.1074/jbc.m109.008680"}],"title":"The external aldimine form of serine palmitoyltransferase: structural, kinetic, and spectroscopic analysis of the wild-type enzyme and HSAN1 mutant mimics.","publicationDate":"2009","journal":"J. Biol. Chem.","firstPage":"17328","lastPage":"17339","volume":"284"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF WILD-TYPE AND MUTANTS IN COMPLEXES WITH PYRIDOXAL PHOSPHATE AND PLP-BOUND SERINE","FUNCTION","CATALYTIC ACTIVITY","REACTION MECHANISM","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","MUTAGENESIS OF ASN-100 AND ARG-378"],"referenceComments":[{"value":"EY2395","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8J"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8T"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8U"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8V"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"2W8W"}]},{"referenceNumber":7,"citation":{"id":"20445930","citationType":"journal article","authors":["Lowther J.","Yard B.A.","Johnson K.A.","Carter L.G.","Bhat V.T.","Raman M.C.","Clarke D.J.","Ramakers B.","McMahon S.A.","Naismith J.H.","Campopiano D.J."],"citationCrossReferences":[{"database":"PubMed","id":"20445930"},{"database":"DOI","id":"10.1039/c003743e"}],"title":"Inhibition of the PLP-dependent enzyme serine palmitoyltransferase by cycloserine: evidence for a novel decarboxylative mechanism of inactivation.","publicationDate":"2010","journal":"Mol. Biosyst.","firstPage":"1682","lastPage":"1693","volume":"6"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF CYCLOSERINE-INACTIVATED SPT","ACTIVITY REGULATION"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"2XBN"}]},{"referenceNumber":8,"citation":{"id":"23957439","citationType":"journal article","authors":["Wadsworth J.M.","Clarke D.J.","McMahon S.A.","Lowther J.P.","Beattie A.E.","Langridge-Smith P.R.","Broughton H.B.","Dunn T.M.","Naismith J.H.","Campopiano D.J."],"citationCrossReferences":[{"database":"PubMed","id":"23957439"},{"database":"DOI","id":"10.1021/ja4059876"}],"title":"The chemical basis of serine palmitoyltransferase inhibition by myriocin.","publicationDate":"2013","journal":"J. Am. Chem. Soc.","firstPage":"14276","lastPage":"14285","volume":"135"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANT ALA-265 IN COMPLEX WITH PLP-MYRIOCIN ALDIMINE","ACTIVITY REGULATION","MUTAGENESIS OF LYS-265"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"4BMK"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB055142","properties":[{"key":"ProteinId","value":"BAB56013.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"JABEOU010000017","properties":[{"key":"ProteinId","value":"NNG56642.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"CP065713","properties":[{"key":"ProteinId","value":"QPT08440.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_007405449.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP023323.1"}]},{"database":"PDB","id":"2JG2","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.30 A"},{"key":"Chains","value":"A=1-420"}]},{"database":"PDB","id":"2JGT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"3.00 A"},{"key":"Chains","value":"A/B=1-420"}]},{"database":"PDB","id":"2W8J","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.50 A"},{"key":"Chains","value":"A=2-420"}]},{"database":"PDB","id":"2W8T","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.25 A"},{"key":"Chains","value":"A=2-420"}]},{"database":"PDB","id":"2W8U","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.50 A"},{"key":"Chains","value":"A=2-420"}]},{"database":"PDB","id":"2W8V","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.43 A"},{"key":"Chains","value":"A=2-420"}]},{"database":"PDB","id":"2W8W","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.14 A"},{"key":"Chains","value":"A=2-420"}]},{"database":"PDB","id":"2XBN","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A=2-420"}]},{"database":"PDB","id":"4BMK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.62 A"},{"key":"Chains","value":"A/B=2-420"}]},{"database":"AlphaFoldDB","id":"Q93UV0","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"Q93UV0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q93UV0","properties":[{"key":"Description","value":"-"}]},{"database":"ChEMBL","id":"CHEMBL3217400","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"78526496","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9807157at2","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.3.1.50","properties":[{"key":"OrganismId","value":"2280"}]},{"database":"UniPathway","id":"UPA00222","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q93UV0","properties":[{"key":"Description","value":"-"}]},{"database":"PRO","id":"PR:Q93UV0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004758","properties":[{"key":"GoTerm","value":"F:serine C-palmitoyltransferase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11279212"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17557831"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17559874"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19376777"}]},{"database":"GO","id":"GO:0006665","properties":[{"key":"GoTerm","value":"P:sphingolipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd06454","properties":[{"key":"EntryName","value":"KBL_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001917","properties":[{"key":"EntryName","value":"Aminotrans_II_pyridoxalP_BS"}]},{"database":"InterPro","id":"IPR004839","properties":[{"key":"EntryName","value":"Aminotransferase_I/II_large"}]},{"database":"InterPro","id":"IPR050087","properties":[{"key":"EntryName","value":"AON_synthase_class-II"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"NF047603","properties":[{"key":"EntryName","value":"SerpalmtaseAlphaP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF047599","properties":[{"key":"EntryName","value":"SerpalmtaseBetaP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13693","properties":[{"key":"EntryName","value":"CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13693:SF3","properties":[{"key":"EntryName","value":"LD36009P"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00155","properties":[{"key":"EntryName","value":"Aminotran_1_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00599","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTEAAAQPHALPADAPDIAPERDLLSKFDGLIAERQKLLDSGVTDPFAIVMEQVKSPTEAVIRGKDTILLGTYNYMGMTFDPDVIAAGKEALEKFGSGTNGSRMLNGTFHDHMEVEQALRDFYGTTGAIVFSTGYMANLGIISTLAGKGEYVILDADSHASIYDGCQQGNAEIVRFRHNSVEDLDKRLGRLPKEPAKLVVLEGVYSMLGDIAPLKEMVAVAKKHGAMVLVDEAHSMGFFGPNGRGVYEAQGLEGQIDFVVGTFSKSVGTVGGFVVSNHPKFEAVRLACRPYIFTASLPPSVVATATTSIRKLMTAHEKRERLWSNARALHGGLKAMGFRLGTETCDSAIVAVMLEDQEQAAMMWQALLDGGLYVNMARPPATPAGTFLLRCSICAEHTPAQIQTVLGMFQAAGRAVGVIG","length":420,"molWeight":45042,"crc64":"D36B6902D032DE1B","md5":"FC7139C219341796E0EA3C3B5FEDE43E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Binding site":4,"Modified residue":1,"Mutagenesis":6,"Helix":18,"Beta strand":17,"Turn":5},"uniParcId":"UPI00000B883F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q52008","uniProtkbId":"LSDX3_SPHPI","entryAudit":{"firstPublicDate":"2012-04-18","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1996-11-01","entryVersion":56,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAB35856.2"}],"value":"Lignostilbene-alpha,beta-dioxygenase isozyme III"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"8534977"}],"value":"LSD-III"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8534977"}],"value":"1.13.11.43"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAB35856.2"}],"value":"lsdB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8534977"}],"value":"Catalyzes the cleavage of the interphenyl double bond (C alpha-C beta) of lignin-derived polyphenolic diaryl-propane type compounds (Stilbene)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-bis(4-hydroxy-3-methoxyphenyl)ethylene + O2 = 2 vanillin","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21340"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:17501"},{"database":"ChEBI","id":"CHEBI:18346"}],"ecNumber":"1.13.11.43","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8534977"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q53353"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q53353"}],"value":"1 Fe(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}],"value":"Activity is high with beta-5 type stilbene and minimal with beta-1 type stilbene. A 4-hydroxyl group and trans-stilbene structure is essential for the binding of substrates to the enzyme"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}],"value":"Homodimer of two beta subunits"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the carotenoid oxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"Lignostilbene-alpha,beta-dioxygenase isozyme III","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}],"featureId":"PRO_0000416941"},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":477,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}}],"keywords":[{"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0439","category":"Biological process","name":"Lignin degradation"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"8534977","citationType":"journal article","authors":["Kamoda S.","Saburi Y."],"citationCrossReferences":[{"database":"PubMed","id":"8534977"},{"database":"DOI","id":"10.1271/bbb.59.1866"}],"title":"Cloning of a lignostilbene-alpha,beta-dioxygenase isozyme gene from Pseudomonas paucimobilis TMY1009.","publicationDate":"1995","journal":"Biosci. Biotechnol. Biochem.","firstPage":"1866","lastPage":"1868","volume":"59"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAB35856.2"}],"value":"TMY1009","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000305"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAB35856.2"}]},{"referenceNumber":2,"citation":{"id":"7763880","citationType":"journal article","authors":["Kamoda S.","Saburi Y."],"citationCrossReferences":[{"database":"PubMed","id":"7763880"},{"database":"DOI","id":"10.1271/bbb.57.931"}],"title":"Structural and enzymatical comparison of lignostilbene-alpha,beta-dioxygenase isozymes, I, II, and III, from Pseudomonas paucimobilis TMY1009.","publicationDate":"1993","journal":"Biosci. Biotechnol. Biochem.","firstPage":"931","lastPage":"934","volume":"57"},"referencePositions":["PROTEIN SEQUENCE OF 2-26","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","SUBUNIT"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"7763880"}],"value":"TMY1009","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"S80637","properties":[{"key":"ProteinId","value":"AAB35856.2"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JC4324","properties":[{"key":"EntryName","value":"JC4324"}]},{"database":"AlphaFoldDB","id":"Q52008","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q52008","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ag:AAB35856","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-18892","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0010436","properties":[{"key":"GoTerm","value":"F:carotenoid dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0050054","properties":[{"key":"GoTerm","value":"F:lignostilbene alpha beta-dioxygenase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7763880"}]},{"database":"GO","id":"GO:0016121","properties":[{"key":"GoTerm","value":"P:carotene catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046274","properties":[{"key":"GoTerm","value":"P:lignin catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"7763880"}]},{"database":"InterPro","id":"IPR004294","properties":[{"key":"EntryName","value":"Carotenoid_Oase"}]},{"database":"PANTHER","id":"PTHR10543","properties":[{"key":"EntryName","value":"BETA-CAROTENE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10543:SF89","properties":[{"key":"EntryName","value":"CAROTENOID 9,10(9',10')-CLEAVAGE DIOXYGENASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03055","properties":[{"key":"EntryName","value":"RPE65"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAHFPDTSGMTGVLRPLRIEGDILDLEVEGEIPAQLDGTFHRVHPDAQFPPRFEDDQFFNGDGMVSLFRFHDGKIDFRQRYAQTDKWKVERKAGKSLFGAYRNPLTDDASVQGMIRGTANTNVMVHAGKLYAMKEDSPCLIMDPLTLETEGYTNFDGKLKNQTFSAHAKIDPVTGNFCNFGYAATGLLTTDCSYFEIDPAGNLLFETEFQVPYYCMMHDYGLTEHYAIFHIVPCSPNWDRLKAGLPHFGFDTTLPVWLGVVPRGPGVTNKDVRWFKAPKTIFASHVMNAFEEGSKIHFDTPQAENNAFPFFPDIHGAPFDPVAARPYLHRWTVDLGSNSEDFAEVRQLTSWIDEFPRVDARYVGQPYRHGWGLVMDPEMEMEFARGRASGFKMNRIGHWDHATGKEDSWWCGPQSIIQEPCFVPRMADSAEGDGYIIALVDNLITNYSDLVVLDALNLKDGPIGRAKLPIRLRSGLHGNWADASKLPIAA","length":490,"molWeight":55126,"crc64":"32EC3A4E03A52DA9","md5":"36EF89B5622C57358F554777EC9E9D20"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Binding site":4},"uniParcId":"UPI00000B890E"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P47243","uniProtkbId":"DBFB_SPHPI","entryAudit":{"firstPublicDate":"1996-02-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2007-01-23","entryVersion":81,"sequenceVersion":4},"annotationScore":4.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"2,2',3-trihydroxybiphenyl dioxygenase"},"ecNumbers":[{"value":"1.13.11.-"}]}},"genes":[{"geneName":{"value":"dbfB"}}],"comments":[{"texts":[{"value":"Responsible for meta-cleavage of the first aromatic ring of 2,2',3-trihydroxybiphenyl and 2,3-dihydroxybiphenyl. 2,2',3-trihydroxydiphenyl ether, catechol, 3-methylcatechol, and 4-methylcatechol are oxidized less efficiently and 3,4-dihydroxybiphenyl is oxidized considerably less efficiently"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"value":"Xenobiotic degradation; dibenzo-p-dioxin degradation; 2-hydroxymuconate and catechol from dibenzo-p-dioxin: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"value":"Xenobiotic degradation; dibenzofuran degradation; 2-hydroxy-2,4-pentadienoate and salicylate from dibenzofuran: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the extradiol ring-cleavage dioxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"8226678"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"2,2',3-trihydroxybiphenyl dioxygenase","featureId":"PRO_0000085041"},{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"VOC 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Domain","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"VOC 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}}],"keywords":[{"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"8226678","citationType":"journal article","authors":["Happe B.","Eltis L.D.","Poth H.","Hedderich R.","Timmis K.N."],"citationCrossReferences":[{"database":"PubMed","id":"8226678"},{"database":"DOI","id":"10.1128/jb.175.22.7313-7320.1993"}],"title":"Characterization of 2,2',3-trihydroxybiphenyl dioxygenase, an extradiol dioxygenase from the dibenzofuran- and dibenzo-p-dioxin-degrading bacterium Sphingomonas sp. strain RW1.","publicationDate":"1993","journal":"J. Bacteriol.","firstPage":"7313","lastPage":"7320","volume":"175"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-64"],"referenceComments":[{"value":"RW1","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"CI-E0U6N0M8NDTPI","citationType":"submission","authors":["Armengaud J."],"publicationDate":"DEC-1998","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["SEQUENCE REVISION"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X72850","properties":[{"key":"ProteinId","value":"CAA51364.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"P47243","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"P47243","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P47243","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00808","properties":[{"key":"RectionId","value":"UER00777"}]},{"database":"UniPathway","id":"UPA00809","properties":[{"key":"RectionId","value":"UER00780"}]},{"database":"GO","id":"GO:0003824","properties":[{"key":"GoTerm","value":"F:catalytic activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008198","properties":[{"key":"GoTerm","value":"F:ferrous iron binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019341","properties":[{"key":"GoTerm","value":"P:dibenzo-p-dioxin catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0019340","properties":[{"key":"GoTerm","value":"P:dibenzofuran catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd07237","properties":[{"key":"EntryName","value":"BphC1-RGP6_C_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07252","properties":[{"key":"EntryName","value":"BphC1-RGP6_N_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR051332","properties":[{"key":"EntryName","value":"Fosfomycin_Res_Enzymes"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR004360","properties":[{"key":"EntryName","value":"Glyas_Fos-R_dOase_dom"}]},{"database":"InterPro","id":"IPR037523","properties":[{"key":"EntryName","value":"VOC_core"}]},{"database":"InterPro","id":"IPR000486","properties":[{"key":"EntryName","value":"Xdiol_ring_cleave_dOase_1/2"}]},{"database":"PANTHER","id":"PTHR36113","properties":[{"key":"EntryName","value":"LYASE, PUTATIVE-RELATED-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36113:SF3","properties":[{"key":"EntryName","value":"SLL5075 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00903","properties":[{"key":"EntryName","value":"Glyoxalase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54593","properties":[{"key":"EntryName","value":"Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00082","properties":[{"key":"EntryName","value":"EXTRADIOL_DIOXYGENAS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51819","properties":[{"key":"EntryName","value":"VOC"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSVKQLGYLIFECRADVLEQMVVVYQDIIGAVVERDEGGRALVRLDGRPFRIRLDPGPANRLAAIGWNVDPSDLAAIAEQVEKACYSVVTADAELAADRAAAQVRQFADNDGFTHELYVESSFPTDPVLESLFVCGEEANGIFGLGHLVVIVADRAKTQSFFTDVLGFGLSDRVTWPEADIFFLHCNQRHHTVALSAPALGLKPGMVHHLMLEAKSKEQVDRAFAAVKRLGYDVLMTIGQHSNDKVYSFYMMAPAGFAVELGFGGQVIGDLESWHVGFYDAPSIWGHELQLPAH","length":294,"molWeight":32278,"crc64":"9315F5B922E1BF8D","md5":"47AE9B2D683E722934CF3F935E48B0FC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Domain":2,"Binding site":3},"uniParcId":"UPI00001701D0"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P11122","uniProtkbId":"BPHC_SPHPI","entryAudit":{"firstPublicDate":"1989-07-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1989-07-01","entryVersion":102,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Biphenyl-2,3-diol 1,2-dioxygenase"},"ecNumbers":[{"value":"1.13.11.39"}]},"alternativeNames":[{"fullName":{"value":"2,3-dihydroxybiphenyl dioxygenase"},"shortNames":[{"value":"DHBD"}]},{"fullName":{"value":"23OHBP oxygenase"}}]},"genes":[{"geneName":{"value":"bphC"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"biphenyl-2,3-diol + O2 = 2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14413"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16205"},{"database":"ChEBI","id":"CHEBI:58284"}],"ecNumber":"1.13.11.39"}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"value":"Xenobiotic degradation; biphenyl degradation; 2-hydroxy-2,4-pentadienoate and benzoate from biphenyl: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"value":"Homooctamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the extradiol ring-cleavage dioxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"Biphenyl-2,3-diol 1,2-dioxygenase","featureId":"PRO_0000085036"},{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"VOC 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Domain","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"VOC 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}}],"keywords":[{"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"3137968","citationType":"journal article","authors":["Taira K.","Hayase N.","Arimura N.","Yamashita S.","Miyazaki T.","Furukawa K."],"citationCrossReferences":[{"database":"PubMed","id":"3137968"},{"database":"DOI","id":"10.1021/bi00411a015"}],"title":"Cloning and nucleotide sequence of the 2,3-dihydroxybiphenyl dioxygenase gene from the PCB-degrading strain of Pseudomonas paucimobilis Q1.","publicationDate":"1988","journal":"Biochemistry","firstPage":"3990","lastPage":"3996","volume":"27"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"Q1","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"M20640","properties":[{"key":"ProteinId","value":"AAA25678.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A28718","properties":[{"key":"EntryName","value":"A28718"}]},{"database":"AlphaFoldDB","id":"P11122","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P11122","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"13689.BV96_03597","properties":[{"key":"Description","value":"-"}]},{"database":"PaxDb","id":"13689-BV96_03597","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0346","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00155","properties":[{"key":"RectionId","value":"UER00252"}]},{"database":"GO","id":"GO:0018583","properties":[{"key":"GoTerm","value":"F:biphenyl-2,3-diol 1,2-dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008198","properties":[{"key":"GoTerm","value":"F:ferrous iron binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:1901170","properties":[{"key":"GoTerm","value":"P:naphthalene catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0042178","properties":[{"key":"GoTerm","value":"P:xenobiotic catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07237","properties":[{"key":"EntryName","value":"BphC1-RGP6_C_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07252","properties":[{"key":"EntryName","value":"BphC1-RGP6_N_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.180.10:FF:000027","properties":[{"key":"EntryName","value":"1,2-dihydroxynaphthalene dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR017626","properties":[{"key":"EntryName","value":"DiOHbiphenyl_dOase"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR004360","properties":[{"key":"EntryName","value":"Glyas_Fos-R_dOase_dom"}]},{"database":"InterPro","id":"IPR037523","properties":[{"key":"EntryName","value":"VOC_core"}]},{"database":"InterPro","id":"IPR000486","properties":[{"key":"EntryName","value":"Xdiol_ring_cleave_dOase_1/2"}]},{"database":"NCBIfam","id":"TIGR03213","properties":[{"key":"EntryName","value":"23dbph12diox"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21366:SF14","properties":[{"key":"EntryName","value":"GLYOXALASE DOMAIN-CONTAINING PROTEIN 5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21366","properties":[{"key":"EntryName","value":"GLYOXALASE FAMILY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22632","properties":[{"key":"EntryName","value":"BphC_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00903","properties":[{"key":"EntryName","value":"Glyoxalase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54593","properties":[{"key":"EntryName","value":"Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00082","properties":[{"key":"EntryName","value":"EXTRADIOL_DIOXYGENAS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51819","properties":[{"key":"EntryName","value":"VOC"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MVAVTELGYLGLTVTNLDAWRSYAAEVAGMEIVDEGEGDRLYLRMDQWHHRIVLHASDSDDLAYLGWRVADPVEFDAMVAKLTAAGISLTVASEAEARERRVLGLAKLADPGGNPTEIFYGPQVDTHKPFHPGRPMYGKFVTGSEGIGHCILRQDDVPAAAAFYGLLGLRGSVEYHLQLPNGMVAQPYFMHCNERQHSVAFGLGPMEKRINHLMFEYTDLDDLGLAHDIVRARKIDVALQLGKHANDQALTFYCANPSGWLWEFGWGARKAPSQQEYYTRDIFGHGNEAAGYGMDIPLG","length":299,"molWeight":33095,"crc64":"29746CAB79D6FC7B","md5":"F94A16C430FCDD89D0EC2C5E300DFD50"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Binding site":3},"uniParcId":"UPI000000055D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQX7","uniProtkbId":"Q6VQX7_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":92,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05974.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Bifunctional protein PutA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Proline dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"1.5.5.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Proline oxidase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"1-pyrroline-5-carboxylate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"P5C dehydrogenase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"1.2.1.88"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"L-glutamate gamma-semialdehyde dehydrogenase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05974.1"}],"value":"orfV"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Oxidizes proline to glutamate for use as a carbon and nitrogen source"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamate 5-semialdehyde + NAD(+) + H2O = L-glutamate + NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30235"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58066"}],"ecNumber":"1.2.1.88","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048142"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23784"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17388"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:60039"},{"database":"ChEBI","id":"CHEBI:132124"}],"ecNumber":"1.5.5.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048779"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004739"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004786"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060911"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"In the C-terminal section; belongs to the aldehyde dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060889"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"In the N-terminal section; belongs to the proline dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Proline utilization A proline dehydrogenase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18327"}]},{"type":"Domain","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Proline dehydrogenase PutA","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14850"}]},{"type":"Domain","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"Proline dehydrogenase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01619"}]},{"type":"Domain","location":{"start":{"value":574,"modifier":"EXACT"},"end":{"value":1007,"modifier":"EXACT"}},"description":"Aldehyde dehydrogenase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00171"}]},{"type":"Active site","location":{"start":{"value":792,"modifier":"EXACT"},"end":{"value":792,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000197-1"}]},{"type":"Active site","location":{"start":{"value":826,"modifier":"EXACT"},"end":{"value":826,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000197-1"}]},{"type":"Active site","location":{"start":{"value":826,"modifier":"EXACT"},"end":{"value":826,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10008"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023062"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0642","category":"Biological process","name":"Proline metabolism"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05974.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05974.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05974.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQX7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00261","properties":[{"key":"RectionId","value":"UER00373"}]},{"database":"GO","id":"GO:0009898","properties":[{"key":"GoTerm","value":"C:cytoplasmic side of plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003700","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003842","properties":[{"key":"GoTerm","value":"F:L-glutamate gamma-semialdehyde dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004657","properties":[{"key":"GoTerm","value":"F:proline dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0055129","properties":[{"key":"GoTerm","value":"P:L-proline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006562","properties":[{"key":"GoTerm","value":"P:L-proline catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07125","properties":[{"key":"EntryName","value":"ALDH_PutA-P5CDH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.309.10:FF:000005","properties":[{"key":"EntryName","value":"1-pyrroline-5-carboxylate dehydrogenase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.460:FF:000001","properties":[{"key":"EntryName","value":"Bifunctional protein PutA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.220:FF:000004","properties":[{"key":"EntryName","value":"Bifunctional protein PutA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.220","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.605.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.309.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.460","properties":[{"key":"EntryName","value":"Single helix bin"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.550","properties":[{"key":"EntryName","value":"Single Helix bin"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016161","properties":[{"key":"EntryName","value":"Ald_DH/histidinol_DH"}]},{"database":"InterPro","id":"IPR016163","properties":[{"key":"EntryName","value":"Ald_DH_C"}]},{"database":"InterPro","id":"IPR016160","properties":[{"key":"EntryName","value":"Ald_DH_CS_CYS"}]},{"database":"InterPro","id":"IPR016162","properties":[{"key":"EntryName","value":"Ald_DH_N"}]},{"database":"InterPro","id":"IPR015590","properties":[{"key":"EntryName","value":"Aldehyde_DH_dom"}]},{"database":"InterPro","id":"IPR025703","properties":[{"key":"EntryName","value":"Bifunct_PutA"}]},{"database":"InterPro","id":"IPR029041","properties":[{"key":"EntryName","value":"FAD-linked_oxidoreductase-like"}]},{"database":"InterPro","id":"IPR041349","properties":[{"key":"EntryName","value":"PRODH"}]},{"database":"InterPro","id":"IPR024090","properties":[{"key":"EntryName","value":"PRODH_PutA_dom_I"}]},{"database":"InterPro","id":"IPR024089","properties":[{"key":"EntryName","value":"PRODH_PutA_dom_I/II"}]},{"database":"InterPro","id":"IPR024082","properties":[{"key":"EntryName","value":"PRODH_PutA_dom_II"}]},{"database":"InterPro","id":"IPR002872","properties":[{"key":"EntryName","value":"Proline_DH_dom"}]},{"database":"InterPro","id":"IPR050485","properties":[{"key":"EntryName","value":"Proline_metab_enzyme"}]},{"database":"InterPro","id":"IPR005933","properties":[{"key":"EntryName","value":"PutA_C"}]},{"database":"NCBIfam","id":"TIGR01238","properties":[{"key":"EntryName","value":"D1pyr5carbox3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008772","properties":[{"key":"EntryName","value":"putA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008869","properties":[{"key":"EntryName","value":"putA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42862","properties":[{"key":"EntryName","value":"DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42862:SF1","properties":[{"key":"EntryName","value":"DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00171","properties":[{"key":"EntryName","value":"Aldedh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01619","properties":[{"key":"EntryName","value":"Pro_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14850","properties":[{"key":"EntryName","value":"Pro_dh-DNA_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18327","properties":[{"key":"EntryName","value":"PRODH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000197","properties":[{"key":"EntryName","value":"Bifunct_PutA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53720","properties":[{"key":"EntryName","value":"ALDH-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51730","properties":[{"key":"EntryName","value":"FAD-linked oxidoreductase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81935","properties":[{"key":"EntryName","value":"N-terminal domain of bifunctional PutA protein"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00070","properties":[{"key":"EntryName","value":"ALDEHYDE_DEHYDR_CYS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTNPPPFTDFAPVIRPQSPLRQAITAAYRRDEAECMAPLLEAAALPDAMRRGVRDMARRLVTTLRANGKGSGVEALVQEYSLSSQEGVALMCLAEALLRIPDDATRDALIRDKIADGDWGGHLGGGRSLFVNAATWGLVVTGKLVGSVDDRGLGAALTRLVARLGEPVIRRGVDLAMRMMGEQFVTGETIGEALKRARAQEAKGFQYSYDMLGEAAATAADAARYLEDYRQAIHAIGRASAGRGVYAGPGISIKLSALHPRYSRAQAERVMGELLPRVKELALLARGYDIGLNIDAEEADRLELSLDLLESLALDPELAGWNGLGFVVQAYGKRCPFVIDWIVDLAGRAGRRIMVRLVKGAYWDAEIKRAQVDGLADFPVYTRKVHTDVAYIACARKLLAARDRVFPQFATHNAQTLATVHHLAGHDFTLGDYEYQCLHGMGEPLYEQVVGKGDLDRPCRIYAPVGTHETLLAYLVRRLLENGANSSFVHRIADPAVPVEEMIADPVEQVRAMPHPGARHADIALPSGLYPDRRNSDGIDLSDENALAMLTRALAESAQIGWTARPEGGEGAARPVLNPADRRDVVGTVFEASTDFARAAVARADGSGWARAPVTERAAILERAADAMQARMPILLGLIVREAGKSLPNAIAEVREAIDFLRYYAAQARSTFGPAQEPLGPVVCISPWNFPLAIFTGQVAAALVAGNAVLAKPAEETPLIAAEAVRLLHEAGVPGDALQLVPGAGEIGAALVAAPQTAGVLFTGSTEVARLIQRQLASRLSASGRPIPLVAETGGQNAMIVDSSALAEQVVADVIASAFDSAGQRCSALRILCLQEDVADRTLAMLKGALRELRIGRTDRLAVDIGPVITDEAQEGIGRHIEAMRALRCAVEQQPLPEESAHGSFVPPTIIEIDDIAQLRREVFGPVLHVIRFPRAGLDALVDAINATGYGLTFGLHTRLDDTVAQVTGRVKAGNLYVNRNVIGAIVGVQPFGGRGLSGTGPKAGGPLYLGRLVRVPPAFAGRAGSFPSALADFADWLAAEGEAEASAMARRCGDASALGVEMALPGPVGERNLYALHPRGWIGMRPATRQGLLGQMAAVLATGNRGVLQDMALPRGLPPHIAAHFASRPEGPLGAVLVEGDAGRIGAAVRDVAGLPGPVVSVHAAGADGMYPLHWLLEEVSTSINTTAAGGNASLMMIG","length":1200,"molWeight":127237,"crc64":"9651154C721A84CE","md5":"136F12125A3C1F8BC29BD7F9D133E2A9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":2},"countByFeatureType":{"Domain":4,"Active site":3},"uniParcId":"UPI0000351E15"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQY3","uniProtkbId":"Q6VQY3_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-07-05","entryVersion":84,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05968.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"}],"value":"cytochrome-c oxidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012949"}],"value":"7.1.1.9"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05968.1"}],"value":"orfP"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 Fe(II)-[cytochrome c] + O2 + 8 H(+)(in) = 4 Fe(III)-[cytochrome c] + 2 H2O + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11436"},{"database":"Rhea","id":"RHEA-COMP:10350"},{"database":"Rhea","id":"RHEA-COMP:14399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"7.1.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047816"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Cu(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29036"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"value":"Binds 1 copper ion per subunit, denoted as copper B."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001970"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"value":"Binds 2 heme groups per subunit, denoted as high- and low-spin."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009578"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000370"}],"value":"Belongs to the heme-copper respiratory oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":449,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":549,"modifier":"EXACT"}},"description":"Cytochrome oxidase subunit I profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50855"}]},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"1; low-spin"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:23378"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"ligand":{"name":"Cu cation","id":"ChEBI:CHEBI:23378","label":"B"}},{"type":"Binding site","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:23378"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"ligand":{"name":"Cu cation","id":"ChEBI:CHEBI:23378","label":"B"}},{"type":"Binding site","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:23378"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"ligand":{"name":"Cu cation","id":"ChEBI:CHEBI:23378","label":"B"}},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"2; high-spin"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"1; low-spin"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023008"}],"id":"KW-0186","category":"Ligand","name":"Copper"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000370"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604677-50"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000370"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000370"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000370"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05968.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05968.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05968.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQY3","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00705","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004129","properties":[{"key":"GoTerm","value":"F:cytochrome-c oxidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006119","properties":[{"key":"GoTerm","value":"P:oxidative phosphorylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0022904","properties":[{"key":"GoTerm","value":"P:respiratory electron transport chain"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01661","properties":[{"key":"EntryName","value":"cbb3_Oxidase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.210.10:FF:000005","properties":[{"key":"EntryName","value":"Cytochrome c oxidase, cbb3-type, subunit I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.210.10","properties":[{"key":"EntryName","value":"Cytochrome c oxidase-like, subunit I domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023616","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_dom"}]},{"database":"InterPro","id":"IPR036927","properties":[{"key":"EntryName","value":"Cyt_c_oxase-like_su1_sf"}]},{"database":"InterPro","id":"IPR000883","properties":[{"key":"EntryName","value":"Cyt_C_Oxase_1"}]},{"database":"InterPro","id":"IPR023615","properties":[{"key":"EntryName","value":"Cyt_c_Oxase_su1_BS"}]},{"database":"InterPro","id":"IPR004677","properties":[{"key":"EntryName","value":"Cyt_c_oxidase_cbb3_su1"}]},{"database":"NCBIfam","id":"TIGR00780","properties":[{"key":"EntryName","value":"ccoN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10422","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10422:SF29","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE SUBUNIT 1 HOMOLOG, BACTEROID"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00115","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81442","properties":[{"key":"EntryName","value":"Cytochrome c oxidase subunit I-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50855","properties":[{"key":"EntryName","value":"COX1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00077","properties":[{"key":"EntryName","value":"COX1_CUB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEQLVWKTGGWFALATLAFLAALAAADFGFAVHMGIVCAAALAVAVLTMRHADYEAITRGLLKMPASQGRYDDDPIRWGVIATVFWGLAGFLAGLYIALQLAFPALNLGLEYTSFGRLRPLHTSAVIFAFGGNALIATSFYVVQRTCRARLAFPALARFVFWGYQLFIVLAATGYLLGITEGKEYAEPEWYVDLWLTIVWVAYLVVFGGTILRRSEPHIYVANWFYLSFILTIAMLHIVNNLSMPVSWLGSKSYSAFAGVQDALTQWWYGHNAVGFFLTAGFLAMMYYFVPKQAERPVYSYRLSIIHFWSLIFLYIWAGPHHLHYTALPDWAQTLGMVFSVMLWMPSWGGMINGLMTLNGAWDRIRTDPIIRMMVMALAFYGMSTFEGPMMSVKAVNSLSHYTDWTIGHVHSGALGWNGLITFACLYYLTPRLWKRERLYSLRLVNWHFWLATVGIVLYAASMWVAGIMQGLMWREYGSDGYLVYAFSEVVSAMFPMYLIRAAGGLLYLSGAIVMAWNIGRTIAGSPLRVEKPMNDAAYDAEADRPIVAQPA","length":552,"molWeight":61993,"crc64":"7C7878A90AAE2EB9","md5":"7DED9218A88F1C46BE5B77E4AA4C355E"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":3,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":13,"Domain":1,"Binding site":6},"uniParcId":"UPI0000351E0F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q2HXE0","uniProtkbId":"Q2HXE0_SPHPI","entryAudit":{"firstPublicDate":"2006-03-21","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2006-03-21","entryVersion":78,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAE79507.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00362"}],"value":"Chromosomal replication initiator protein DnaA"}},"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAE79507.1"}],"value":"dnaA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004227"}],"value":"Belongs to the DnaA family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"Chromosomal replication initiator DnaA C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00760"}]},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAE79507.1"}]},{"type":"Non-terminal residue","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAE79507.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022705"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004227"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023121"}],"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"16487327","citationType":"journal article","authors":["Nagata Y.","Kamakura M.","Endo R.","Miyazaki R.","Ohtsubo Y.","Tsuda M."],"citationCrossReferences":[{"database":"PubMed","id":"16487327"},{"database":"DOI","id":"10.1111/j.1574-6968.2005.00096.x"}],"title":"Distribution of gamma-hexachlorocyclohexane-degrading genes on three replicons in Sphingobium japonicum UT26.","publicationDate":"2006","journal":"FEMS Microbiol. Lett.","firstPage":"112","lastPage":"118","volume":"256"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAE79507.1"}],"value":"UT26","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAE79507.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB218823","properties":[{"key":"ProteinId","value":"BAE79507.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q2HXE0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003688","properties":[{"key":"GoTerm","value":"F:DNA replication origin binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006270","properties":[{"key":"GoTerm","value":"P:DNA replication initiation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006275","properties":[{"key":"GoTerm","value":"P:regulation of DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00009","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd06571","properties":[{"key":"EntryName","value":"Bac_DnaA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1750.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001957","properties":[{"key":"EntryName","value":"Chromosome_initiator_DnaA"}]},{"database":"InterPro","id":"IPR020591","properties":[{"key":"EntryName","value":"Chromosome_initiator_DnaA-like"}]},{"database":"InterPro","id":"IPR013159","properties":[{"key":"EntryName","value":"DnaA_C"}]},{"database":"InterPro","id":"IPR013317","properties":[{"key":"EntryName","value":"DnaA_dom"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR010921","properties":[{"key":"EntryName","value":"Trp_repressor/repl_initiator"}]},{"database":"NCBIfam","id":"TIGR00362","properties":[{"key":"EntryName","value":"DnaA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30050","properties":[{"key":"EntryName","value":"CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30050:SF2","properties":[{"key":"EntryName","value":"CHROMOSOMAL REPLICATION INITIATOR PROTEIN DNAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00308","properties":[{"key":"EntryName","value":"Bac_DnaA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08299","properties":[{"key":"EntryName","value":"Bac_DnaA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00051","properties":[{"key":"EntryName","value":"DNAA"}]},{"database":"SMART","id":"SM00760","properties":[{"key":"EntryName","value":"Bac_DnaA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48295","properties":[{"key":"EntryName","value":"TrpR-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"GLGKTHLLHAIARLFSSHSPSAPVLYMSAERFMMEFVNAMRANETMMFKARLRAARLLLIDDIQFIAGKGSTQEEFLHTINDLIDSGARIVVTADRAPQMLDAIDARILSRLAGGLVADIRPAGLDLRLAILEAKRAIAGDPPVPDAVVDFLARSIRSNVRELEGAFNKLIAYGQLTGRSIDLEFAQAMLADAVRANARRITVDEIQKACAAHYKIDAAEMRSKRRARAVARPRQVAMYLAKKMTPRSLPEIGRIFGGRDHTT","length":263,"molWeight":28973,"crc64":"12CC82A2ADB92218","md5":"D41AFE63B53431A5D81D1A47C11314EE"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Non-terminal residue":2},"uniParcId":"UPI0000697618"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q5QKZ2","uniProtkbId":"Q5QKZ2_SPHPI","entryAudit":{"firstPublicDate":"2005-01-04","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2005-01-04","entryVersion":75,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAV73945.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"long-chain-acyl-CoA dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"1.3.8.8"}]},"flag":"Fragment"},"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17721"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83721"},{"database":"ChEBI","id":"CHEBI:83727"}],"ecNumber":"1.3.8.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047434"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17722"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047434"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005005"}],"value":"Lipid metabolism; fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]},{"type":"Non-terminal residue","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAV73945.1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"12450824","citationType":"journal article","authors":["Kumari R.","Subudhi S.","Suar M.","Dhingra G.","Raina V.","Dogra C.","Lal S.","Van Der Meer J.R.","Holliger C.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"12450824"},{"database":"DOI","id":"10.1128/AEM.68.12.6021-6028.2002"}],"title":"Cloning and characterization of lin genes responsible for the degradation of hexachlorocyclohexane isomers by Sphingomonas paucimobilis strain B90.","publicationDate":"2002","journal":"Appl. Environ. Microbiol.","firstPage":"6021","lastPage":"6028","volume":"68"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAV73945.1"}],"value":"B90","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAV73945.1"}]},{"referenceNumber":2,"citation":{"id":"CI-ELVT3JC147SNL","citationType":"submission","authors":["Lal R.","Kumari R.","Subudhi S.","Suar M.","Dhingra G.","Raina V.","Dogra C.","Lal S."],"publicationDate":"NOV-2004","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAV73945.1"}],"value":"B90","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAV73945.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY150580","properties":[{"key":"ProteinId","value":"AAV73945.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q5QKZ2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004466","properties":[{"key":"GoTerm","value":"F:long-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0033539","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation using acyl-CoA dehydrogenase"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"2.40.110.10:FF:000002","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase fadE12"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"PANTHER","id":"PTHR48083:SF13","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE FAMILY MEMBER 11"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48083","properties":[{"key":"EntryName","value":"MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNFTMSPAETMWRDRVRNFMNDVVRPHDETYAAQQASGERWKTLPIIEELKERAKADGIWNLFMPPLAGHNPVDSSFEFVAPGLTNLEYASCAEEMGRIEWASEVFNCSAPDTGNMEVLHRYGTREHKERWLRPLMEGKIRSVFLMTEPRVASSDATNIETSIVCDGDHYVINGRKWWSSGIGDPRCSVGILMGKTDPDAPRHAQQSMILLPLDTPGVKVLRMLPVFGYDDAPHGHGEVELKDVRVPVENMLLGEGRGFEIAQGRLGPGRIHHCMRTIGLAEEILKKMVERLLSRTAFGKRLAEHSIWEQRIAEARTSLEMTRLLCLKAADVM","length":333,"molWeight":37624,"crc64":"22BCE0A48954C938","md5":"5AED0997C657E4D12B5BA79A35DD6878"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3,"Non-terminal residue":1},"uniParcId":"UPI000048E0A6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQX3","uniProtkbId":"Q6VQX3_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2004-07-05","entryVersion":58,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05978.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012065"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}],"value":"Haloalkane dehalogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012065"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}],"value":"3.8.1.5"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05978.1"}],"value":"linB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}],"value":"dhaA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}],"value":"Catalyzes hydrolytic cleavage of carbon-halogen bonds in halogenated aliphatic compounds, leading to the formation of the corresponding primary alcohols, halide ions and protons"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-haloalkane + H2O = a halide anion + a primary alcohol + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19081"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15734"},{"database":"ChEBI","id":"CHEBI:16042"},{"database":"ChEBI","id":"CHEBI:18060"}],"ecNumber":"3.8.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007213"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}],"value":"Belongs to the haloalkane dehalogenase family. Type 2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00561"}]},{"type":"Active site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}]},{"type":"Active site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}]},{"type":"Active site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01231"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05978.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05978.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY331259","properties":[{"key":"ProteinId","value":"AAR05978.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQX3","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q6VQX3","properties":[{"key":"Description","value":"-"}]},{"database":"ESTHER","id":"sphpi-linb","properties":[{"key":"FamilyName","value":"Haloalkane_dehalogenase-HLD2"}]},{"database":"GO","id":"GO:0018786","properties":[{"key":"GoTerm","value":"F:haloalkane dehalogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.1820","properties":[{"key":"EntryName","value":"alpha/beta hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01231","properties":[{"key":"EntryName","value":"Haloalk_dehal_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000073","properties":[{"key":"EntryName","value":"AB_hydrolase_1"}]},{"database":"InterPro","id":"IPR029058","properties":[{"key":"EntryName","value":"AB_hydrolase_fold"}]},{"database":"InterPro","id":"IPR000639","properties":[{"key":"EntryName","value":"Epox_hydrolase-like"}]},{"database":"InterPro","id":"IPR023594","properties":[{"key":"EntryName","value":"Haloalkane_dehalogenase_2"}]},{"database":"NCBIfam","id":"NF002938","properties":[{"key":"EntryName","value":"PRK03592.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43329","properties":[{"key":"EntryName","value":"EPOXIDE HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00561","properties":[{"key":"EntryName","value":"Abhydrolase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00412","properties":[{"key":"EntryName","value":"EPOXHYDRLASE"}]},{"database":"SUPFAM","id":"SSF53474","properties":[{"key":"EntryName","value":"alpha/beta-Hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSLGAKPFGEKKFIEIKGRRMAYIDEGTGDPILFQHGNPTSSYLWRNIMPHCAGLGRLIACDLIGMGDSDKLDPSGPERYTYAEHRDYLDALWEALDLGDRVVLVVHDWGSVLGFDWARRHRERVQGIAYMEAVTMPLEWADFPEQDRDLFQAFRSQAGEELVLQDNVFVEQVLPGLILRPLSEAEMAAYREPFLAAGEARRPTLSWPRQIPIAGTPADVVAIARDYAGWLSESPIPKLFINAEPGHLTTGRIRDFCRTWPNQTEITVAGAHFIQEDSPDEIGAAIAAFVRRLRPA","length":296,"molWeight":33230,"crc64":"B14249854546F602","md5":"D3EBDC3C6201E3A3DD962176A4E0FA7D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":3},"uniParcId":"UPI000016E5D1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQX8","uniProtkbId":"Q6VQX8_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":112,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05973.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05973.1"}],"value":"ORFU"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05973.1"}],"value":"orfU"}}],"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"value":"Cell membrane","id":"SL-0039"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006024"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"value":"Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IB subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Transmembrane","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Transmembrane","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Transmembrane","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Transmembrane","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Transmembrane","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Transmembrane","location":{"start":{"value":663,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Transmembrane","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":703,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}]},{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"HMA","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50846"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362081"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05973.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05973.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05973.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQX8","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005507","properties":[{"key":"GoTerm","value":"F:copper ion binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043682","properties":[{"key":"GoTerm","value":"F:P-type divalent copper transporter activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0055070","properties":[{"key":"GoTerm","value":"P:copper ion homeostasis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00371","properties":[{"key":"EntryName","value":"HMA"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02092","properties":[{"key":"EntryName","value":"P-type_ATPase_FixI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1110.10","properties":[{"key":"EntryName","value":"Calcium-transporting ATPase, cytoplasmic domain N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.70.150.10","properties":[{"key":"EntryName","value":"Calcium-transporting ATPase, cytoplasmic transduction domain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1000","properties":[{"key":"EntryName","value":"HAD superfamily/HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023299","properties":[{"key":"EntryName","value":"ATPase_P-typ_cyto_dom_N"}]},{"database":"InterPro","id":"IPR018303","properties":[{"key":"EntryName","value":"ATPase_P-typ_P_site"}]},{"database":"InterPro","id":"IPR023298","properties":[{"key":"EntryName","value":"ATPase_P-typ_TM_dom_sf"}]},{"database":"InterPro","id":"IPR008250","properties":[{"key":"EntryName","value":"ATPase_P-typ_transduc_dom_A_sf"}]},{"database":"InterPro","id":"IPR059000","properties":[{"key":"EntryName","value":"ATPase_P-type_domA"}]},{"database":"InterPro","id":"IPR036412","properties":[{"key":"EntryName","value":"HAD-like_sf"}]},{"database":"InterPro","id":"IPR023214","properties":[{"key":"EntryName","value":"HAD_sf"}]},{"database":"InterPro","id":"IPR006121","properties":[{"key":"EntryName","value":"HMA_dom"}]},{"database":"InterPro","id":"IPR036163","properties":[{"key":"EntryName","value":"HMA_dom_sf"}]},{"database":"InterPro","id":"IPR027256","properties":[{"key":"EntryName","value":"P-typ_ATPase_IB"}]},{"database":"InterPro","id":"IPR001757","properties":[{"key":"EntryName","value":"P_typ_ATPase"}]},{"database":"NCBIfam","id":"TIGR01511","properties":[{"key":"EntryName","value":"ATPase-IB1_Cu"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01512","properties":[{"key":"EntryName","value":"ATPase-IB2_Cd"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01525","properties":[{"key":"EntryName","value":"ATPase-IB_hvy"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01494","properties":[{"key":"EntryName","value":"ATPase_P-type"},{"key":"MatchStatus","value":"2"}]},{"database":"PANTHER","id":"PTHR43520","properties":[{"key":"EntryName","value":"ATP7, ISOFORM B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43520:SF5","properties":[{"key":"EntryName","value":"CATION-TRANSPORTING P-TYPE ATPASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00122","properties":[{"key":"EntryName","value":"E1-E2_ATPase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00403","properties":[{"key":"EntryName","value":"HMA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00702","properties":[{"key":"EntryName","value":"Hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00119","properties":[{"key":"EntryName","value":"CATATPASE"}]},{"database":"PRINTS","id":"PR00943","properties":[{"key":"EntryName","value":"CUATPASE"}]},{"database":"SUPFAM","id":"SSF81653","properties":[{"key":"EntryName","value":"Calcium ATPase, transduction domain A"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81665","properties":[{"key":"EntryName","value":"Calcium ATPase, transmembrane domain M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56784","properties":[{"key":"EntryName","value":"HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55008","properties":[{"key":"EntryName","value":"HMA, heavy metal-associated domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00154","properties":[{"key":"EntryName","value":"ATPASE_E1_E2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50846","properties":[{"key":"EntryName","value":"HMA_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATKALIADPVAEEAVESLFAVPGIHCVSCIAKIEEGLPRQPGIISARVNMGAKRVAIRHDPALTPPDLRATIAALGFEAEPLADAGLDVAAAESRRLTRALVVAGFAAMNIMLLSVSVWSGAAGATRGMFHWLSALIALPTVAYAGQPFFRSAWAAVRHGRTNMDVPISIGVLLTTGMSLYETVTGGAHAWFDGAVMLLFFLLAGRALDSMMRGRARAGVAALLKQTAPGALVLEADGGSRWTRADALRPGMTILVAAGERLAADGRVTEGESGLDIAFLTGESAPVRVHPGDAVQAGALNVDGPIRVEVTAAGADTVIADIARLMEEAAQGKSRYVRLADRAARLYAPCVHLLAALSFAGWMIAGAGVHQALLIAVAVLLITCPCALGLAVPAAQIVACGALMRRGVLVKDGSALERLAEVSEAVFDKTGTLTLGRPVPQGLRRLWRDDRAILLALSRASRHPLSVALRQALEARGVAPAVLDNVREVAGEGVFGDYQGVAVSLARPRSLVNLFGLAAEYRRGDQATLLGFADALRPDAAETLDALRGMGTKVLIASGDRPEALEEIARTTGATAIGHLRPADKLALIGRLKARGEKVLMVGDGLNDGPALAAGHASMAPASASDASQLAADAVFLGDRLAPVALAVHAARRTVAVVKQNFALAIGYNLLAVPLAMAGKVTPLVAAVAMSTSSLIVIANALRLKGVAK","length":710,"molWeight":73469,"crc64":"CD3B7894EA1EA7A9","md5":"62F204792D147E91DEAC532454D3F2E2"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":8,"Domain":1},"uniParcId":"UPI0000351E14"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQY1","uniProtkbId":"Q6VQY1_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-07-05","entryVersion":94,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05970.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"value":"Cbb3-type cytochrome c oxidase subunit"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05970.1"}],"value":"orfR"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"value":"C-type cytochrome. Part of the cbb3-type cytochrome c oxidase complex"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme c","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:61717"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-2"}],"value":"Binds 2 heme C groups per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004673"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"value":"Energy metabolism; oxidative phosphorylation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"value":"Component of the cbb3-type cytochrome c oxidase"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004533"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"value":"Cell inner membrane","id":"SL-0037"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006113"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"value":"Belongs to the CcoP / FixP family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Cytochrome c","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51007"}]},{"type":"Domain","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"Cytochrome c","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51007"}]},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-2"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"1"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-2"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"1"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-1"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"1"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-1"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"2"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-2"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"2"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"covalent","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-2"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"2"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-1"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"2"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61717"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000006-1"}],"ligand":{"name":"heme c","id":"ChEBI:CHEBI:61717","label":"1"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022519"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022781"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023065"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022660"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000006"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05970.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05970.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05970.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQY1","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00705","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006119","properties":[{"key":"GoTerm","value":"P:oxidative phosphorylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"Gene3D","id":"6.10.280.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.760.10","properties":[{"key":"EntryName","value":"Cytochrome c-like domain"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR032858","properties":[{"key":"EntryName","value":"CcoP_N"}]},{"database":"InterPro","id":"IPR038414","properties":[{"key":"EntryName","value":"CcoP_N_sf"}]},{"database":"InterPro","id":"IPR009056","properties":[{"key":"EntryName","value":"Cyt_c-like_dom"}]},{"database":"InterPro","id":"IPR036909","properties":[{"key":"EntryName","value":"Cyt_c-like_dom_sf"}]},{"database":"InterPro","id":"IPR008168","properties":[{"key":"EntryName","value":"Cyt_C_IC"}]},{"database":"InterPro","id":"IPR004678","properties":[{"key":"EntryName","value":"Cyt_c_oxidase_cbb3_su3"}]},{"database":"InterPro","id":"IPR050597","properties":[{"key":"EntryName","value":"Cytochrome_c_Oxidase_Subunit"}]},{"database":"NCBIfam","id":"TIGR00782","properties":[{"key":"EntryName","value":"ccoP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33751","properties":[{"key":"EntryName","value":"CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33751:SF1","properties":[{"key":"EntryName","value":"CBB3-TYPE CYTOCHROME C OXIDASE SUBUNIT FIXP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13442","properties":[{"key":"EntryName","value":"Cytochrome_CBB3"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF14715","properties":[{"key":"EntryName","value":"FixP_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000006","properties":[{"key":"EntryName","value":"Cbb3-Cox_fixP"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00605","properties":[{"key":"EntryName","value":"CYTCHROMECIC"}]},{"database":"SUPFAM","id":"SSF46626","properties":[{"key":"EntryName","value":"Cytochrome c"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51007","properties":[{"key":"EntryName","value":"CYTC"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MADDKRIDPATGTEIKHHEWDGIQELDTPLPRWWLWTFYATILFAVGYMIAYPAIPMIDRATGGILGWSSRGALDRELAARERQIAPIRKAIADTPITALPGRPELMQQAVEGGRAAFRVHCVQCHGSGAAGSKGYPNLNDDDWLWGGDLAAIEKTITDGVRNPGHDATRQSLMPAFGKDQLLTAAQVDDVVAHVRAISGQDRPGAASRRGDRVFADNCAVCHGPAGKGNRALGAPDLTDAIWLYGGDAGTIRETVWNSRHGVMPRWDDKLDKATIRMLAAYVHSLGGGEGDAGR","length":295,"molWeight":31895,"crc64":"F27AC686A8A8E96D","md5":"9F5B96C7A948CC587C982ED414DD89C0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":1,"Domain":2,"Binding site":8},"uniParcId":"UPI0000351E11"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQZ1","uniProtkbId":"Q6VQZ1_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":69,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05960.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05960.1"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05979.1"}],"value":"TnpA"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05963.1"}],"value":"TnpA2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05965.1"}],"value":"TnpA3"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAQ96757.1"}],"value":"TnpA4"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAX07228.1"}],"value":"Transposase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05960.1"}],"value":"tnpA1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05979.1"}],"value":"tnpA"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05963.1"}],"value":"tnpA2"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05965.1"}],"value":"tnpA3"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAQ96757.1"}],"value":"tnpA4"}]}],"features":[{"type":"Domain","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Integrase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50994"}]},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0229","category":"Biological process","name":"DNA integration"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00457"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022578"}],"id":"KW-0815","category":"Biological process","name":"Transposition"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05960.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05960.1"}]},{"referenceNumber":2,"citation":{"id":"CI-DFQ1O6052753","citationType":"submission","authors":["Lal R.","Pal R.","Sharma P.","Malhotra S.","Kumari R.","Raina V.","Dogra C."],"publicationDate":"JAN-2005","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAX07228.1"}],"value":"Sp+","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAX07228.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY334273","properties":[{"key":"ProteinId","value":"AAQ96757.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05960.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05963.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05965.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AY331259","properties":[{"key":"ProteinId","value":"AAR05979.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AY903216","properties":[{"key":"ProteinId","value":"AAX07228.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AY903217","properties":[{"key":"ProteinId","value":"AAX07230.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQZ1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004519","properties":[{"key":"GoTerm","value":"F:endonuclease activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015074","properties":[{"key":"GoTerm","value":"P:DNA integration"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006313","properties":[{"key":"GoTerm","value":"P:DNA transposition"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"InterPro","id":"IPR032874","properties":[{"key":"EntryName","value":"DDE_dom"}]},{"database":"InterPro","id":"IPR001584","properties":[{"key":"EntryName","value":"Integrase_cat-core"}]},{"database":"InterPro","id":"IPR052183","properties":[{"key":"EntryName","value":"IS_Transposase"}]},{"database":"InterPro","id":"IPR012337","properties":[{"key":"EntryName","value":"RNaseH-like_sf"}]},{"database":"InterPro","id":"IPR047930","properties":[{"key":"EntryName","value":"Transpos_IS6"}]},{"database":"NCBIfam","id":"NF033587","properties":[{"key":"EntryName","value":"transpos_IS6"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR35528","properties":[{"key":"EntryName","value":"BLL1675 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR35528:SF3","properties":[{"key":"EntryName","value":"BLL1675 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13610","properties":[{"key":"EntryName","value":"DDE_Tnp_IS240"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53098","properties":[{"key":"EntryName","value":"Ribonuclease H-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50994","properties":[{"key":"EntryName","value":"INTEGRASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLGGDWTDGTMTDFKWRHFQGDVILWAVRWYCRYPISYRDLEEMLAERGISVDHTTIYRWVQCYAPEMEKRLRWFWRRGFDPSWRLDETYVKVRGKWTYLYRAVDKRGDTIDFYLSPTRSAKAAKRFLGKALRGLKHWEKPATLNTDKAPSYGAAITELKREGKLDRETAHRQVKYLNNVIEADHGKLKILIKPVRGFKSIPTAYATIKGFEVMRALRKGQARPWCLQPGIRGEVRLVERAFGIGPSALTEAMGMLNHHFAAAA","length":264,"molWeight":30717,"crc64":"8FF031657C4298B5","md5":"0C49DDC2C6D9A864B86B8A768AD71E64"},"extraAttributes":{"countByFeatureType":{"Domain":1,"Binding site":2},"uniParcId":"UPI000005E804"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQZ5","uniProtkbId":"Q6VQZ5_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-07-05","entryVersion":73,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05956.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"long-chain-acyl-CoA dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"1.3.8.8"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05956.1"}],"value":"orfH"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17721"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83721"},{"database":"ChEBI","id":"CHEBI:83727"}],"ecNumber":"1.3.8.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047434"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:17722"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047434"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005005"}],"value":"Lipid metabolism; fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05956.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05956.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05956.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQZ5","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004466","properties":[{"key":"GoTerm","value":"F:long-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0033539","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation using acyl-CoA dehydrogenase"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"2.40.110.10:FF:000002","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase fadE12"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"PANTHER","id":"PTHR48083:SF13","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE FAMILY MEMBER 11"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48083","properties":[{"key":"EntryName","value":"MEDIUM-CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNFTMSPAETMWRDRVRNFMNDVVRPHDETYAAQQASGERWKTLPIIEELKERAKADGIWNLFMPPLAGHNPVDSSFEFVAPGLTNLEYASCAEEMGRIEWASEVFNCSAPDTGNMEVLHRYGTREHKERWLRPLMEGKIRSVFLMTEPRVASSDATNIETSIVCDGDHYVINGRKWWSSGIGDPRCSVGILMGKTDPDAPRHAQQSMILLPLDTPGVKVLRMLPVFGYDDAPHGHGEVELKDVRVPVENMLLGEGRGFEIAQGRLGPGRIHHCMRTIGLAEEILKKMVERLLSRTAFGKRLAEHSIWEQRIAEARTSLEMTRLLCLKAADVMDKLGAKAAQAEIAMIKVAGPHMALKIADDAIQAHGGAGVADDFGLARAYAHLRTMRLVDGPDEVHNRAIARLEMRRYRQ","length":412,"molWeight":46169,"crc64":"79DCA8A61A01CFCB","md5":"6C829CF027BF5340F1FBE9951B7C94B1"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0000351E08"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q6VQZ6","uniProtkbId":"Q6VQZ6_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":99,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05955.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05955.1"}],"value":"ORFG"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05955.1"}],"value":"orfG"}}],"comments":[{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"value":"Binds 1 FAD per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007532"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"value":"Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"FAD/NAD(P)-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07992"}]},{"type":"Domain","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"Pyridine nucleotide-disulphide oxidoreductase dimerisation","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02852"}]},{"type":"Active site","location":{"start":{"value":437,"modifier":"EXACT"},"end":{"value":437,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-2"}]},{"type":"Binding site","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Disulfide bond","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-4"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023284"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"id":"KW-0676","category":"Domain","name":"Redox-active center"}],"references":[{"referenceNumber":1,"citation":{"id":"15060023","citationType":"journal article","authors":["Dogra C.","Raina V.","Pal R.","Suar M.","Lal S.","Gartemann K.H.","Holliger C.","van der Meer J.R.","Lal R."],"citationCrossReferences":[{"database":"PubMed","id":"15060023"},{"database":"DOI","id":"10.1128/JB.186.8.2225-2235.2004"}],"title":"Organization of lin genes and IS6100 among different strains of hexachlorocyclohexane-degrading Sphingomonas paucimobilis: evidence for horizontal gene transfer.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"2225","lastPage":"2235","volume":"186"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05955.1"}],"value":"B90A","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAR05955.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY331258","properties":[{"key":"ProteinId","value":"AAR05955.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q6VQZ6","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004362","properties":[{"key":"GoTerm","value":"F:glutathione-disulfide reductase (NADPH) activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045454","properties":[{"key":"GoTerm","value":"P:cell redox homeostasis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0034599","properties":[{"key":"GoTerm","value":"P:cellular response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006749","properties":[{"key":"GoTerm","value":"P:glutathione metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.30.390.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR023753","properties":[{"key":"EntryName","value":"FAD/NAD-binding_dom"}]},{"database":"InterPro","id":"IPR016156","properties":[{"key":"EntryName","value":"FAD/NAD-linked_Rdtase_dimer_sf"}]},{"database":"InterPro","id":"IPR046952","properties":[{"key":"EntryName","value":"GSHR/TRXR-like"}]},{"database":"InterPro","id":"IPR001100","properties":[{"key":"EntryName","value":"Pyr_nuc-diS_OxRdtase"}]},{"database":"InterPro","id":"IPR004099","properties":[{"key":"EntryName","value":"Pyr_nucl-diS_OxRdtase_dimer"}]},{"database":"InterPro","id":"IPR012999","properties":[{"key":"EntryName","value":"Pyr_OxRdtase_I_AS"}]},{"database":"NCBIfam","id":"NF004776","properties":[{"key":"EntryName","value":"gorA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42737","properties":[{"key":"EntryName","value":"GLUTATHIONE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42737:SF2","properties":[{"key":"EntryName","value":"GLUTATHIONE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07992","properties":[{"key":"EntryName","value":"Pyr_redox_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02852","properties":[{"key":"EntryName","value":"Pyr_redox_dim"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000350","properties":[{"key":"EntryName","value":"Mercury_reductase_MerA"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00368","properties":[{"key":"EntryName","value":"FADPNR"}]},{"database":"PRINTS","id":"PR00411","properties":[{"key":"EntryName","value":"PNDRDTASEI"}]},{"database":"SUPFAM","id":"SSF51905","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55424","properties":[{"key":"EntryName","value":"FAD/NAD-linked reductases, dimerisation (C-terminal) domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00076","properties":[{"key":"EntryName","value":"PYRIDINE_REDOX_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLTYDYDLFVIGAGSGGVRAARVSAAYGARVAVAEEHRVGGTCVIRGCVPKKLLVYGSHFAEDLQDARRFGWKVPDCEFDWSALRDNVLAEVSRLEGLYTETLGNNKVEIIRERATVAGPHEVLLGSGQTITAGKILIATGAWPIVPHFPGAEHGITSNEVFHLDTFPKRVVIAGAGYIANEFAGIFHQFGAHVTLVNRTDVILRGYDEQIRDRLLQISMTKGIEFKFHVAFEKVDKQPDGSLLVHMTGHEPIPADMLLFATGRRPHTENLGLETADVALDAKGAIKVDDDNRSSCASIYAVGDVTNRVQLTPVAIREGQAFADTVFGNNPRRVDYGCIPSAVFSHPPMAGVGMTEAEARNKLGEVKVYTSDFRAMKNVLADRHERALYKLVVHPETDVVVGIHMIGPDAPEILQAAAIAVKARLTKAQFDDTVALHPSMAEELVLMR","length":448,"molWeight":48829,"crc64":"EE394413E23CBD6B","md5":"9CFB1B2A7C9CF2948E111DF874433CBC"},"extraAttributes":{"countByCommentType":{"COFACTOR":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":4,"Disulfide bond":1},"uniParcId":"UPI0000351E07"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q7BRG2","uniProtkbId":"Q7BRG2_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":39,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017053"}],"value":"Mercuric transport protein MerT"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030934"}],"value":"Mercury ion transport protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}],"value":"merT"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045720"}],"value":"Involved in mercury resistance. Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004429"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004429"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008224"}],"value":"Belongs to the MerT family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022519"}],"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022466"}],"id":"KW-0475","category":"Biological process","name":"Mercuric resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022914"}],"id":"KW-0476","category":"Ligand","name":"Mercury"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"9055422","citationType":"journal article","authors":["Liebert C.A.","Wireman J.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9055422"}],"title":"Phylogeny of mercury resistance (mer) operons of gram-negative bacteria isolated from the fecal flora of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"1066","lastPage":"1076","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23825.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}]},{"referenceNumber":2,"citation":{"id":"9361435","citationType":"journal article","authors":["Wireman J.","Liebert C.A.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9361435"}],"title":"Association of mercury resistance with antibiotic resistance in the gram-negative fecal bacteria of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"4494","lastPage":"4503","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23825.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}]},{"referenceNumber":3,"citation":{"id":"11116334","citationType":"journal article","authors":["Liebert C.A.","Watson A.L.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"11116334"}],"title":"The quality of merC, a module of the mer mosaic.","publicationDate":"2000","journal":"J. Mol. Evol.","firstPage":"607","lastPage":"622","volume":"51"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23825.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23822.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF120976","properties":[{"key":"ProteinId","value":"AAD23822.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AF120977","properties":[{"key":"ProteinId","value":"AAD23825.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q7BRG2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0015097","properties":[{"key":"GoTerm","value":"F:mercury ion transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.10.287.910","properties":[{"key":"EntryName","value":"bacterial mercury transporter, merf"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003457","properties":[{"key":"EntryName","value":"Transprt_MerT"}]},{"database":"NCBIfam","id":"NF010314","properties":[{"key":"EntryName","value":"merT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02411","properties":[{"key":"EntryName","value":"MerT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEPSNGRAPLVAGGLAAILASACCLGPLVLIALGFSGAWIGNLTVLEPYRPIFIGAALVALFFAWRRIVRPTAACKPGEVCAIPQVRTTYKLIFWFVAVLVLVALGFPYVMPFFY","length":116,"molWeight":12461,"crc64":"E963ACF8C3997B72","md5":"084BD7413C9E465CA77F922BFF7BD2CF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":3},"uniParcId":"UPI00000B9E45"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q7BRH0","uniProtkbId":"Q7BRH0_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2025-04-02","lastSequenceUpdateDate":"2004-07-05","entryVersion":80,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"value":"Periplasmic mercury ion-binding protein"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}],"value":"merP"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045344"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"value":"Involved in mercury resistance. Acts as a mercury scavenger that specifically binds to a mercuric ion in the periplasm and probably passes it to the cytoplasmic mercuric reductase MerA via the mercuric transport protein MerT"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004418"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"value":"Periplasm","id":"SL-0200"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005938"}],"value":"Belongs to the MerP family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Periplasmic mercury ion-binding protein","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5007710499"},{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"HMA","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50846"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022466"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0475","category":"Biological process","name":"Mercuric resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022914"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0476","category":"Ligand","name":"Mercury"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022764"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0574","category":"Cellular component","name":"Periplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"9055422","citationType":"journal article","authors":["Liebert C.A.","Wireman J.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9055422"}],"title":"Phylogeny of mercury resistance (mer) operons of gram-negative bacteria isolated from the fecal flora of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"1066","lastPage":"1076","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23810.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}]},{"referenceNumber":2,"citation":{"id":"9361435","citationType":"journal article","authors":["Wireman J.","Liebert C.A.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9361435"}],"title":"Association of mercury resistance with antibiotic resistance in the gram-negative fecal bacteria of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"4494","lastPage":"4503","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23810.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}]},{"referenceNumber":3,"citation":{"id":"11116334","citationType":"journal article","authors":["Liebert C.A.","Watson A.L.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"11116334"}],"title":"The quality of merC, a module of the mer mosaic.","publicationDate":"2000","journal":"J. Mol. Evol.","firstPage":"607","lastPage":"622","volume":"51"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23810.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23805.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF120972","properties":[{"key":"ProteinId","value":"AAD23805.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AF120973","properties":[{"key":"ProteinId","value":"AAD23810.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q7BRH0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q7BRH0","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0042597","properties":[{"key":"GoTerm","value":"C:periplasmic space"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0045340","properties":[{"key":"GoTerm","value":"F:mercury ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015097","properties":[{"key":"GoTerm","value":"F:mercury ion transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00371","properties":[{"key":"EntryName","value":"HMA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.100:FF:000005","properties":[{"key":"EntryName","value":"Copper-exporting P-type ATPase A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017969","properties":[{"key":"EntryName","value":"Heavy-metal-associated_CS"}]},{"database":"InterPro","id":"IPR006121","properties":[{"key":"EntryName","value":"HMA_dom"}]},{"database":"InterPro","id":"IPR036163","properties":[{"key":"EntryName","value":"HMA_dom_sf"}]},{"database":"InterPro","id":"IPR011795","properties":[{"key":"EntryName","value":"MerP"}]},{"database":"InterPro","id":"IPR001802","properties":[{"key":"EntryName","value":"MerP/CopZ"}]},{"database":"NCBIfam","id":"TIGR02052","properties":[{"key":"EntryName","value":"MerP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46594","properties":[{"key":"EntryName","value":"P-TYPE CATION-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46594:SF4","properties":[{"key":"EntryName","value":"P-TYPE CATION-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00403","properties":[{"key":"EntryName","value":"HMA"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00946","properties":[{"key":"EntryName","value":"HGSCAVENGER"}]},{"database":"SUPFAM","id":"SSF55008","properties":[{"key":"EntryName","value":"HMA, heavy metal-associated domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01047","properties":[{"key":"EntryName","value":"HMA_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50846","properties":[{"key":"EntryName","value":"HMA_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRKLLASLALASLVATPVWAATQTVTLAVPGMTCAACPITVKTALTKVDGVTKAEVSFENREAIVTFDDTKTNALALTKATEDAGYPSSVKQ","length":92,"molWeight":9585,"crc64":"CA42FABEC7AC884C","md5":"81DBA5069BD392441128A183B19086DA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1},"uniParcId":"UPI00000BB691"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q7BRH1","uniProtkbId":"Q7BRH1_SPHPI","entryAudit":{"firstPublicDate":"2004-07-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2004-07-05","entryVersion":37,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017053"}],"value":"Mercuric transport protein MerT"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030934"}],"value":"Mercury ion transport protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}],"value":"merT"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045720"}],"value":"Involved in mercury resistance. Probably transfers a mercuric ion from the periplasmic Hg(2+)-binding protein MerP to the cytoplasmic mercuric reductase MerA"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004429"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004429"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008224"}],"value":"Belongs to the MerT family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022519"}],"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022466"}],"id":"KW-0475","category":"Biological process","name":"Mercuric resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022914"}],"id":"KW-0476","category":"Ligand","name":"Mercury"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"9055422","citationType":"journal article","authors":["Liebert C.A.","Wireman J.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9055422"}],"title":"Phylogeny of mercury resistance (mer) operons of gram-negative bacteria isolated from the fecal flora of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"1066","lastPage":"1076","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23811.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}]},{"referenceNumber":2,"citation":{"id":"9361435","citationType":"journal article","authors":["Wireman J.","Liebert C.A.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9361435"}],"title":"Association of mercury resistance with antibiotic resistance in the gram-negative fecal bacteria of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"4494","lastPage":"4503","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23811.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}]},{"referenceNumber":3,"citation":{"id":"11116334","citationType":"journal article","authors":["Liebert C.A.","Watson A.L.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"11116334"}],"title":"The quality of merC, a module of the mer mosaic.","publicationDate":"2000","journal":"J. Mol. Evol.","firstPage":"607","lastPage":"622","volume":"51"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23811.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23806.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF120972","properties":[{"key":"ProteinId","value":"AAD23806.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AF120973","properties":[{"key":"ProteinId","value":"AAD23811.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q7BRH1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0015097","properties":[{"key":"GoTerm","value":"F:mercury ion transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.10.287.910","properties":[{"key":"EntryName","value":"bacterial mercury transporter, merf"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003457","properties":[{"key":"EntryName","value":"Transprt_MerT"}]},{"database":"NCBIfam","id":"NF010314","properties":[{"key":"EntryName","value":"merT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02411","properties":[{"key":"EntryName","value":"MerT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEPQNGRGALFTGGLAAILASACCLGPLVLIALGFSGAWIGNLTVLEPYRPLFIGAALVALFFAYRRIFRPAQACAPGEVCAIPQVRTSYKLLYWLVAALVLVALGFPYILPLFY","length":116,"molWeight":12437,"crc64":"5C926A63C211FE6B","md5":"C364B0F2D59DF387B0DFE1935E7F7781"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":3},"uniParcId":"UPI00000B0DA1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q8RQW2","uniProtkbId":"Q8RQW2_SPHPI","entryAudit":{"firstPublicDate":"2002-06-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2002-06-01","entryVersion":54,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364048"}],"value":"Dioxygenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364048"}],"value":"1.13.11.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}],"value":"lsdA"}}],"comments":[{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364048"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364048"}],"value":"Binds 1 Fe(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006787"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364048"}],"value":"Belongs to the carotenoid oxygenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":476,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364048"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604294-1"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364048"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"2185230","citationType":"journal article","authors":["Noda Y.","Nishikawa S.","Shiozuka K.","Kadokura H.","Nakajima H.","Yoda K.","Katayama Y.","Morohoshi N.","Haraguchi T.","Yamasaki M."],"citationCrossReferences":[{"database":"PubMed","id":"2185230"}],"title":"Molecular cloning of the protocatechuate 4,5-dioxygenase genes of Pseudomonas paucimobilis.","publicationDate":"1990","journal":"J. Bacteriol.","firstPage":"2704","lastPage":"2709","volume":"172"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}]},{"referenceNumber":2,"citation":{"id":"9864312","citationType":"journal article","authors":["Masai E.","Shinohara S.","Hara H.","Nishikawa S.","Katayama Y.","Fukuda M."],"citationCrossReferences":[{"database":"PubMed","id":"9864312"}],"title":"Genetic and biochemical characterization of a 2-pyrone-4, 6-dicarboxylic acid hydrolase involved in the protocatechuate 4, 5-cleavage pathway of Sphingomonas paucimobilis SYK-6.","publicationDate":"1999","journal":"J. Bacteriol.","firstPage":"55","lastPage":"62","volume":"181"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}]},{"referenceNumber":3,"citation":{"id":"11073908","citationType":"journal article","authors":["Masai E.","Momose K.","Hara H.","Nishikawa S.","Katayama Y.","Fukuda M."],"citationCrossReferences":[{"database":"PubMed","id":"11073908"},{"database":"DOI","id":"10.1128/JB.182.23.6651-6658.2000"}],"title":"Genetic and biochemical characterization of 4-carboxy-2-hydroxymuconate-6-semialdehyde dehydrogenase and its role in the protocatechuate 4,5-cleavage pathway in Sphingomonas paucimobilis SYK-6.","publicationDate":"2000","journal":"J. Bacteriol.","firstPage":"6651","lastPage":"6658","volume":"182"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}]},{"referenceNumber":4,"citation":{"id":"11092855","citationType":"journal article","authors":["Hara H.","Masai E.","Katayama Y.","Fukuda M."],"citationCrossReferences":[{"database":"PubMed","id":"11092855"},{"database":"DOI","id":"10.1128/JB.182.24.6950-6957.2000"}],"title":"The 4-oxalomesaconate hydratase gene, involved in the protocatechuate 4,5-cleavage pathway, is essential to vanillate and syringate degradation in Sphingomonas paucimobilis SYK-6.","publicationDate":"2000","journal":"J. Bacteriol.","firstPage":"6950","lastPage":"6957","volume":"182"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}]},{"referenceNumber":5,"citation":{"id":"12486039","citationType":"journal article","authors":["Hara H.","Masai E.","Miyauchi K.","Katayama Y.","Fukuda M."],"citationCrossReferences":[{"database":"PubMed","id":"12486039"},{"database":"DOI","id":"10.1128/JB.185.1.41-50.2003"}],"title":"Characterization of the 4-carboxy-4-hydroxy-2-oxoadipate aldolase gene and operon structure of the protocatechuate 4,5-cleavage pathway genes in Sphingomonas paucimobilis SYK-6.","publicationDate":"2003","journal":"J. Bacteriol.","firstPage":"41","lastPage":"50","volume":"185"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB88735.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB073227","properties":[{"key":"ProteinId","value":"BAB88735.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q8RQW2","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8RQW2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0010436","properties":[{"key":"GoTerm","value":"F:carotenoid dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016121","properties":[{"key":"GoTerm","value":"P:carotene catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"InterPro","id":"IPR004294","properties":[{"key":"EntryName","value":"Carotenoid_Oase"}]},{"database":"PANTHER","id":"PTHR10543","properties":[{"key":"EntryName","value":"BETA-CAROTENE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10543:SF89","properties":[{"key":"EntryName","value":"CAROTENOID 9,10(9',10')-CLEAVAGE DIOXYGENASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03055","properties":[{"key":"EntryName","value":"RPE65"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFPATPDYTGLNKPVGQEVSIKGLKASEGTIPADVRGAFFRAVPDPQFPPFFHPDTALSDDGMISRVLFNADGTVDYDIRYVQTPRWKAERAAGKRLFGRYRNPYTNDPSAFDLEGTVSNTTPVWHAGKLIMTKEDGPGHQVDPHTLETIGAYDFGGVLRSKTMTAHVRVDPETKEMFVYGYEADGLCSKTMAYWWTDRDGKLVKEQWFEAPFCSLVHDFVITENYAIFPLQPTTADLERVKGKGAHWVHQQDLDYHVGIMPRYGDVSQIRWFKGPKGMSSFHMMNAFETDDGKVHMDHHVTDTIAFPHIQADSGINVPPQMLGGGFQRWIMDMKGDGESVAVTPLGPPGDMPRIADADQGRPYRRGWYCSMNPQPMGPPVMGGVVGVMFSALLRKDFETGEIVGYNLPPAHGMSETVHVPASEPGHEGWLIAVVDHQLGPDTFEHALWIWNAGDLPAGPVAKVPVPTRMRPQVHGWWVPMADYEAARAA","length":491,"molWeight":54536,"crc64":"46FEA625A0BE2FEA","md5":"F64EBBBEB0A5550F74B07A743AAD31AD"},"extraAttributes":{"countByCommentType":{"COFACTOR":1,"SIMILARITY":1},"countByFeatureType":{"Binding site":4},"uniParcId":"UPI00000BA120"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q8RTG2","uniProtkbId":"Q8RTG2_SPHPI","entryAudit":{"firstPublicDate":"2002-06-01","lastAnnotationUpdateDate":"2025-10-08","lastSequenceUpdateDate":"2002-06-01","entryVersion":54,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAL79535.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019048"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361259"}],"value":"UTP--glucose-1-phosphate uridylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012415"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361259"}],"value":"2.7.7.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361259"}],"value":"UDP-glucose pyrophosphorylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAL79535.1"}],"value":"ugpG"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 1-phosphate + UTP + H(+) = UDP-alpha-D-glucose + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19889"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58601"},{"database":"ChEBI","id":"CHEBI:58885"}],"ecNumber":"2.7.7.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048128"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361259"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006890"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361259"}],"value":"Belongs to the UDPGP type 2 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361259"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361259"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"12655408","citationType":"journal article","authors":["Marques A.R.","Ferreira P.B.","Sa-Correia I.","Fialho A.M."],"citationCrossReferences":[{"database":"PubMed","id":"12655408"}],"title":"Characterization of the ugpG gene encoding a UDP-glucose pyrophosphorylase from the gellan gum producer Sphingomonas paucimobilis ATCC 31461.","publicationDate":"2003","journal":"Mol. Genet. Genomics","firstPage":"816","lastPage":"824","volume":"268"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAL79535.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF461178","properties":[{"key":"ProteinId","value":"AAL79535.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q8RTG2","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8RTG2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003983","properties":[{"key":"GoTerm","value":"F:UTP:glucose-1-phosphate uridylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006011","properties":[{"key":"GoTerm","value":"P:UDP-alpha-D-glucose metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02541","properties":[{"key":"EntryName","value":"UGPase_prokaryotic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005771","properties":[{"key":"EntryName","value":"GalU_uridylyltTrfase_bac/arc"}]},{"database":"InterPro","id":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"NCBIfam","id":"TIGR01099","properties":[{"key":"EntryName","value":"galU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43197","properties":[{"key":"EntryName","value":"UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43197:SF1","properties":[{"key":"EntryName","value":"UTP--GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTIKPLRKAVFPVAGLGTRFLPATKAMPKEMLPVVDRPLIQYAVDEAVEAGIEQMIFVTGRGKSALEDHFDIAYELEATMAARGKSLDVLDGTRLKPGNIAYVRQQEPMGLGHAVWCARDIVGDEPFAVLLPDDFMFGQPGCLKQMVDAYNKVGGNLICAEEVPDDQTHRYGIITPGTQDGVLTEVKGLVEKPAPGTAPSNLSVIGRYILQPEVMRILENQGKGAGGEIQLTDAMQRMIGDQPFHGVTFQGTRYDCGDKAGFIQANLAVALSRPDLEPAVRAFAVKALG","length":289,"molWeight":31208,"crc64":"9DDD8B4D29BA369A","md5":"780366558D2ED95C885E42F904BB89D7"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI000005D2A3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q9KWI1","uniProtkbId":"Q9KWI1_SPHPI","entryAudit":{"firstPublicDate":"2000-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2000-10-01","entryVersion":84,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07893.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022190"}],"value":"Metapyrocatechase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013117"}],"value":"1.13.11.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031146"}],"value":"CatO2ase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030369"}],"value":"Catechol 2,3-dioxygenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07893.1"}],"value":"catA"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"catechol + O2 = (2Z,4E)-2-hydroxy-6-oxohexa-2,4-dienoate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17337"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:18135"},{"database":"ChEBI","id":"CHEBI:71198"}],"ecNumber":"1.13.11.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000163"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001954"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008784"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"value":"Belongs to the extradiol ring-cleavage dioxygenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"VOC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51819"}]},{"type":"Domain","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"VOC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51819"}]},{"type":"Active site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Active site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022797"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-L6BIDRFSF6BG","citationType":"submission","authors":["Nomura N.","Lu J.","Nakahara T.","Nakajima-Kambe T."],"title":"Catechol 2,3-dioxygenase.","publicationDate":"DEC-1999","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB12679.1"}],"value":"TZS-7","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB12679.1"}]},{"referenceNumber":2,"citation":{"id":"10899588","citationType":"journal article","authors":["Lu J.","Nomura N.","Nakajima-Kambe T.","Nakahara T."],"citationCrossReferences":[{"database":"PubMed","id":"10899588"},{"database":"DOI","id":"10.1016/S0167-4781(00)00115-9"}],"title":"Cloning and expression of genes encoding meta-cleavage enzymes from 4,6-dimethyldibenzothiophene-degrading Sphingomonas strain TZS-7.","publicationDate":"2000","journal":"Biochim. Biophys. Acta","firstPage":"493","lastPage":"498","volume":"1492"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07893.1"}],"value":"TZS-7","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07893.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB035678","properties":[{"key":"ProteinId","value":"BAB07893.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AB035539","properties":[{"key":"ProteinId","value":"BAB12679.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9KWI1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0018577","properties":[{"key":"GoTerm","value":"F:catechol 2,3-dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008198","properties":[{"key":"GoTerm","value":"F:ferrous iron binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07243","properties":[{"key":"EntryName","value":"2_3_CTD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR017624","properties":[{"key":"EntryName","value":"Catechol_2-3_dOase"}]},{"database":"InterPro","id":"IPR051332","properties":[{"key":"EntryName","value":"Fosfomycin_Res_Enzymes"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR004360","properties":[{"key":"EntryName","value":"Glyas_Fos-R_dOase_dom"}]},{"database":"InterPro","id":"IPR037523","properties":[{"key":"EntryName","value":"VOC_core"}]},{"database":"InterPro","id":"IPR000486","properties":[{"key":"EntryName","value":"Xdiol_ring_cleave_dOase_1/2"}]},{"database":"InterPro","id":"IPR054560","properties":[{"key":"EntryName","value":"XylE-like_N"}]},{"database":"NCBIfam","id":"TIGR03211","properties":[{"key":"EntryName","value":"catechol_2_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36113:SF1","properties":[{"key":"EntryName","value":"GLYOXALASE_BLEOMYCIN RESISTANCE PROTEIN_DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36113","properties":[{"key":"EntryName","value":"LYASE, PUTATIVE-RELATED-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22247","properties":[{"key":"EntryName","value":"Diox-like_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00903","properties":[{"key":"EntryName","value":"Glyoxalase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54593","properties":[{"key":"EntryName","value":"Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00082","properties":[{"key":"EntryName","value":"EXTRADIOL_DIOXYGENAS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51819","properties":[{"key":"EntryName","value":"VOC"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MALTGVIRPGYVQLRVLDLDEAMTHYRDRIGLNFVNRDGDRAFFQAFDEFDRHSIILREADQAGMDVMGFKVAKDADLDHFAERLLDIGVHVDVIPAGSDPGVGRKIRFNTPTQHVFELYAEMELSATGPAVKNPDVWVVEPRGMRATRFDHCALNGVDISATAKIFVDALDFAVTEELVDEGSGTRLGIFLSCSNKAHDVAFLGYPEDGKIHHTSFNLESWHDVGHAADIISRYDISLDIGPTRHGITRGQTIYFFDPSGNRNETFSGGYIYYPDNPQRMWQAESAGKAIFYYEKALNDRFMTVNT","length":307,"molWeight":34434,"crc64":"B20C51D6EEE7235B","md5":"E5EEFAE8F451D50311BFB1BBE4DA3059"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":2},"uniParcId":"UPI00000B4878"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q9KWI2","uniProtkbId":"Q9KWI2_SPHPI","entryAudit":{"firstPublicDate":"2000-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2000-10-01","entryVersion":77,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07894.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07894.1"}],"value":"2,3-dihydroxybiphenyl 1,2-dioxygenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07894.1"}],"value":"dmdC"}}],"comments":[{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001954"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011823"}],"value":"Homooctamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008784"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"value":"Belongs to the extradiol ring-cleavage dioxygenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"VOC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51819"}]},{"type":"Domain","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"VOC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51819"}]},{"type":"Active site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Active site","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022797"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000683"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"10899588","citationType":"journal article","authors":["Lu J.","Nomura N.","Nakajima-Kambe T.","Nakahara T."],"citationCrossReferences":[{"database":"PubMed","id":"10899588"},{"database":"DOI","id":"10.1016/S0167-4781(00)00115-9"}],"title":"Cloning and expression of genes encoding meta-cleavage enzymes from 4,6-dimethyldibenzothiophene-degrading Sphingomonas strain TZS-7.","publicationDate":"2000","journal":"Biochim. Biophys. Acta","firstPage":"493","lastPage":"498","volume":"1492"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07894.1"}],"value":"TZS-7","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAB07894.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB035677","properties":[{"key":"ProteinId","value":"BAB07894.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9KWI2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0008198","properties":[{"key":"GoTerm","value":"F:ferrous iron binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016702","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on single donors with incorporation of molecular oxygen, incorporation of two atoms of oxygen"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:1901170","properties":[{"key":"GoTerm","value":"P:naphthalene catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0042178","properties":[{"key":"GoTerm","value":"P:xenobiotic catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07237","properties":[{"key":"EntryName","value":"BphC1-RGP6_C_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07252","properties":[{"key":"EntryName","value":"BphC1-RGP6_N_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.180.10:FF:000027","properties":[{"key":"EntryName","value":"1,2-dihydroxynaphthalene dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR017626","properties":[{"key":"EntryName","value":"DiOHbiphenyl_dOase"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR004360","properties":[{"key":"EntryName","value":"Glyas_Fos-R_dOase_dom"}]},{"database":"InterPro","id":"IPR037523","properties":[{"key":"EntryName","value":"VOC_core"}]},{"database":"InterPro","id":"IPR000486","properties":[{"key":"EntryName","value":"Xdiol_ring_cleave_dOase_1/2"}]},{"database":"NCBIfam","id":"TIGR03213","properties":[{"key":"EntryName","value":"23dbph12diox"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21366:SF14","properties":[{"key":"EntryName","value":"GLYOXALASE DOMAIN-CONTAINING PROTEIN 5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21366","properties":[{"key":"EntryName","value":"GLYOXALASE FAMILY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22632","properties":[{"key":"EntryName","value":"BphC_D1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00903","properties":[{"key":"EntryName","value":"Glyoxalase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54593","properties":[{"key":"EntryName","value":"Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00082","properties":[{"key":"EntryName","value":"EXTRADIOL_DIOXYGENAS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51819","properties":[{"key":"EntryName","value":"VOC"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSVVTELGYLGLSVSDLAAWRAYAAEVAGMEVVDEGEGDRLYLRMDLWHHRIVLHADGSDDLAYMGWRVAGPQEFAAMQEKLSAAGIPFTVGSEAEARERRVLGLLKLADPGGNPTEIFFGPQVDTHKPFHPGRPMFGKFLTDSQGVGHCILRQDDVEAAARFYELLGLRGSVEYHLQLPNGMVAQPYFMHCNERQHSVAFGLGPMEKRINHLMFEYTELDDLGMAHDIVREKKIDVALQLGKHANDQALTFYCANPSGWLWEFGWGARPAPAQQEYYIRDIFGHGNEAAGYGMDIPLL","length":299,"molWeight":33353,"crc64":"DE2570BD5BDDD1BC","md5":"1E7DA605AEB283C039587E6DBB292898"},"extraAttributes":{"countByCommentType":{"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":2},"uniParcId":"UPI00000B1CA7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"Q9WW07","uniProtkbId":"Q9WW07_SPHPI","entryAudit":{"firstPublicDate":"1999-11-01","lastAnnotationUpdateDate":"2025-04-02","lastSequenceUpdateDate":"1999-11-01","entryVersion":88,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"value":"Periplasmic mercury ion-binding protein"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}],"value":"merP"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045344"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"value":"Involved in mercury resistance. Acts as a mercury scavenger that specifically binds to a mercuric ion in the periplasm and probably passes it to the cytoplasmic mercuric reductase MerA via the mercuric transport protein MerT"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004418"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"value":"Periplasm","id":"SL-0200"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005938"}],"value":"Belongs to the MerP family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Periplasmic mercury ion-binding protein","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5007719029"},{"type":"Domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"HMA","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50846"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022466"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0475","category":"Biological process","name":"Mercuric resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022914"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0476","category":"Ligand","name":"Mercury"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022764"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361212"}],"id":"KW-0574","category":"Cellular component","name":"Periplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"9055422","citationType":"journal article","authors":["Liebert C.A.","Wireman J.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9055422"}],"title":"Phylogeny of mercury resistance (mer) operons of gram-negative bacteria isolated from the fecal flora of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"1066","lastPage":"1076","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23821.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}]},{"referenceNumber":2,"citation":{"id":"9361435","citationType":"journal article","authors":["Wireman J.","Liebert C.A.","Smith T.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"9361435"}],"title":"Association of mercury resistance with antibiotic resistance in the gram-negative fecal bacteria of primates.","publicationDate":"1997","journal":"Appl. Environ. Microbiol.","firstPage":"4494","lastPage":"4503","volume":"63"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23821.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}]},{"referenceNumber":3,"citation":{"id":"11116334","citationType":"journal article","authors":["Liebert C.A.","Watson A.L.","Summers A.O."],"citationCrossReferences":[{"database":"PubMed","id":"11116334"}],"title":"The quality of merC, a module of the mer mosaic.","publicationDate":"2000","journal":"J. Mol. Evol.","firstPage":"607","lastPage":"622","volume":"51"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}],"value":"660H","type":"STRAIN"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23821.1"}],"value":"661H","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"AAD23826.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF120976","properties":[{"key":"ProteinId","value":"AAD23821.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AF120977","properties":[{"key":"ProteinId","value":"AAD23826.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9WW07","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9WW07","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0042597","properties":[{"key":"GoTerm","value":"C:periplasmic space"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0045340","properties":[{"key":"GoTerm","value":"F:mercury ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015097","properties":[{"key":"GoTerm","value":"F:mercury ion transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00371","properties":[{"key":"EntryName","value":"HMA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.100:FF:000005","properties":[{"key":"EntryName","value":"Copper-exporting P-type ATPase A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017969","properties":[{"key":"EntryName","value":"Heavy-metal-associated_CS"}]},{"database":"InterPro","id":"IPR006121","properties":[{"key":"EntryName","value":"HMA_dom"}]},{"database":"InterPro","id":"IPR036163","properties":[{"key":"EntryName","value":"HMA_dom_sf"}]},{"database":"InterPro","id":"IPR011795","properties":[{"key":"EntryName","value":"MerP"}]},{"database":"InterPro","id":"IPR001802","properties":[{"key":"EntryName","value":"MerP/CopZ"}]},{"database":"NCBIfam","id":"TIGR02052","properties":[{"key":"EntryName","value":"MerP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46594","properties":[{"key":"EntryName","value":"P-TYPE CATION-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46594:SF4","properties":[{"key":"EntryName","value":"P-TYPE CATION-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00403","properties":[{"key":"EntryName","value":"HMA"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00946","properties":[{"key":"EntryName","value":"HGSCAVENGER"}]},{"database":"SUPFAM","id":"SSF55008","properties":[{"key":"EntryName","value":"HMA, heavy metal-associated domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01047","properties":[{"key":"EntryName","value":"HMA_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50846","properties":[{"key":"EntryName","value":"HMA_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKKLFASLALAAFVAPVFAATQTVTLSVPGMTCSTCPITVKKAISKVEGVSKVNVTFETREAVVTFDDAKTSVQKLTKATEDAGYPSSVKK","length":91,"molWeight":9587,"crc64":"43F017C85FC9579D","md5":"9C46633AEDE2824ED01A18E4A6C27C3D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1},"uniParcId":"UPI00000B63E8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A411LJN5","uniProtkbId":"A0A411LJN5_SPHPI","entryAudit":{"firstPublicDate":"2019-05-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-05-08","entryVersion":31,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NNG59570.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NNG59570.1"}],"value":"Bacteriorhodopsin"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NNG59570.1"}],"value":"HKX06_19670"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QPT09066.1"}],"value":"I6G38_01705"}]}],"comments":[{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008130"}],"value":"Belongs to the archaeal/bacterial/fungal opsin family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"8ANQ"}],"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022991"}],"id":"KW-0157","category":"Ligand","name":"Chromophore"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022543"}],"id":"KW-0600","category":"Molecular function","name":"Photoreceptor protein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023170"}],"id":"KW-0675","category":"Molecular function","name":"Receptor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022925"}],"id":"KW-0681","category":"Molecular function","name":"Retinal protein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022606"}],"id":"KW-0716","category":"Biological process","name":"Sensory transduction"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CBGLB0GSFKA6B","citationType":"submission","authors":["Bijlani S.","Singh N.K.","Mason C.E.","Wang C.C.","Venkateswaran K."],"title":"Draft Genome Sequences of Sphingomonas sp. Isolated from the International Space Station.","publicationDate":"MAY-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NNG59570.1"}],"value":"FKI-L5-BR-P1","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NNG59570.1"}]},{"referenceNumber":2,"citation":{"id":"CI-C8AIJS6VECB27","citationType":"submission","authors":["Sproer C.","Gronow S.","Severitt S.","Schroder I.","Tallon L.","Sadzewicz L.","Zhao X.","Boylan J.","Ott S.","Bowen H.","Vavikolanu K.","Mehta A.","Aluvathingal J.","Nadendla S.","Lowell S.","Myers T.","Yan Y.","Sichtig H."],"title":"FDA dAtabase for Regulatory Grade micrObial Sequences (FDA-ARGOS): Supporting development and validation of Infectious Disease Dx tests.","publicationDate":"DEC-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QPT09066.1"}],"value":"FDAARGOS_881","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"QPT09066.1"}]},{"referenceNumber":3,"citation":{"id":"37130895","citationType":"journal article","authors":["Okhrimenko I.S.","Kovalev K.","Petrovskaya L.E.","Ilyinsky N.S.","Alekseev A.A.","Marin E.","Rokitskaya T.I.","Antonenko Y.N.","Siletsky S.A.","Popov P.A.","Zagryadskaya Y.A.","Soloviov D.V.","Chizhov I.V.","Zabelskii D.V.","Ryzhykau Y.L.","Vlasov A.V.","Kuklin A.I.","Bogorodskiy A.O.","Mikhailov A.E.","Sidorov D.V.","Bukhalovich S.","Tsybrov F.","Bukhdruker S.","Vlasova A.D.","Borshchevskiy V.I.","Dolgikh D.A.","Kirpichnikov M.P.","Bamberg E.","Gordeliy V.I."],"citationCrossReferences":[{"database":"PubMed","id":"37130895"},{"database":"DOI","id":"10.1038/s42004-023-00884-8"}],"title":"Mirror proteorhodopsins.","publicationDate":"2023","journal":"Commun. Chem.","firstPage":"88","lastPage":"88","volume":"6"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (2.80 ANGSTROMS)"],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"8ANQ"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JABEOU010000057","properties":[{"key":"ProteinId","value":"NNG59570.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"CP065713","properties":[{"key":"ProteinId","value":"QPT09066.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"8ANQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.80 A"},{"key":"Chains","value":"A/B/C/P/T/Y=1-237"}]},{"database":"AlphaFoldDB","id":"A0A411LJN5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A0A411LJN5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"70408at2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005216","properties":[{"key":"GoTerm","value":"F:monoatomic ion channel activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.20.1070.10","properties":[{"key":"EntryName","value":"Rhodopsin 7-helix transmembrane proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001425","properties":[{"key":"EntryName","value":"Arc/bac/fun_rhodopsins"}]},{"database":"InterPro","id":"IPR018229","properties":[{"key":"EntryName","value":"Rhodopsin_retinal_BS"}]},{"database":"PANTHER","id":"PTHR28286","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR28286:SF2","properties":[{"key":"EntryName","value":"BACTERIORHODOPSIN _OPSIN, NOPA (EUROFUNG)"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01036","properties":[{"key":"EntryName","value":"Bac_rhodopsin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00251","properties":[{"key":"EntryName","value":"BACTRLOPSIN"}]},{"database":"SMART","id":"SM01021","properties":[{"key":"EntryName","value":"Bac_rhodopsin"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81321","properties":[{"key":"EntryName","value":"Family A G protein-coupled receptor-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00950","properties":[{"key":"EntryName","value":"BACTERIAL_OPSIN_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDWMAFLIGFTIMSLASLAIYAKGSKTSPALHHTLLHAAVPFIAATAYLAMTFGIGTLVNFNGSVTYLARYADWSVTTPILLASLVLLAFHERGRTGEVGGYLTAIIVLDVLMIVTGLISSLAVVPALKWVWYLWSCAAFLGVLYLLWVPLRAMAVERGEALGTAYQKNVAFLTVIWFLYPIVFLIGPEGLKIISDPTSVWAILIMDVLAKVVYAFYAAANLETALRHHDVRHDDRF","length":237,"molWeight":26083,"crc64":"2497F3DA15673D59","md5":"4306AA7E8E7BB41CC8DE4D91BF2B6237"},"extraAttributes":{"countByCommentType":{"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":7},"uniParcId":"UPI0002F3BE5E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A2PZP1","uniProtkbId":"A2PZP1_SPHPI","entryAudit":{"firstPublicDate":"2007-03-06","lastAnnotationUpdateDate":"2025-04-02","lastSequenceUpdateDate":"2007-03-06","entryVersion":27,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Sphingomonas paucimobilis","commonName":"Pseudomonas paucimobilis","taxonId":13689,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF45813.1"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Sphingomonadales","Sphingomonadaceae","Sphingomonas"]},"proteinExistence":"4: Predicted","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF45813.1"}],"value":"Uncharacterized protein"}}],"flag":"Fragment"},"features":[{"type":"Non-terminal residue","location":{"start":{"value":402,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF45813.1"}]}],"references":[{"referenceNumber":1,"citation":{"id":"17928721","citationType":"journal article","authors":["Masai E.","Yamamoto Y.","Inoue T.","Takamura K.","Hara H.","Kasai D.","Katayama Y.","Fukuda M."],"citationCrossReferences":[{"database":"PubMed","id":"17928721"},{"database":"DOI","id":"10.1271/bbb.70267"}],"title":"Characterization of ligV essential for catabolism of vanillin by Sphingomonas paucimobilis SYK-6.","publicationDate":"2007","journal":"Biosci. Biotechnol. Biochem.","firstPage":"2487","lastPage":"2492","volume":"71"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF45813.1"}],"value":"SYK-6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BAF45813.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB287332","properties":[{"key":"ProteinId","value":"BAF45813.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A2PZP1","properties":[{"key":"Description","value":"-"}]},{"database":"InterPro","id":"IPR046880","properties":[{"key":"EntryName","value":"TPR-S"}]},{"database":"Pfam","id":"PF20308","properties":[{"key":"EntryName","value":"TPR-S"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFEAAGWLNSDEADALSLRGRLLKDRALRSAGEDRTRYFDEAEAAYMRAAGNRRATYPLINAATIAFLNGKPERAQMLAQQTLAVLESGDYEPETAYWLGATRAEALLLLGDIPGGVTALEAAVARAPQAWEDHAATIRQLQLILQQANAANDLFDHLRPPVCLHFSGIIHLPVQEEGIRDVVEAMLDQIRPGFAFGALAAGSDILIGEMVLARGARLHVVLPGPVDLFRESSVIPFGDQWARRFDTLIEAADAVETLGGITRLSDAAVTLAEEMAMGLAIRHAHSLASKAVALRLRRSTDQVKASEAVWRRRGLPVYDLAIDRESPASMLATLDTGRRRAILASTEAFPADLERTSGNRPRFVQDVWLMDFDDLGHAIEIATTFLRSAPENSLGLVYHVVD","length":402,"molWeight":43910,"crc64":"3A5A052049C5D3FB","md5":"338E6530AE98968C92826F210A67A0C2"},"extraAttributes":{"countByFeatureType":{"Non-terminal residue":1},"uniParcId":"UPI0000EFD93D"}}]}