{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O52793","uniProtkbId":"EVAA_AMYOR","entryAudit":{"firstPublicDate":"2018-05-23","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-06-01","entryVersion":65,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11035791"}],"value":"dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11035791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"value":"4.2.1.159"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"23473392"}],"value":"2,3-dehydratase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11035791"}],"value":"evaA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11035791"}],"value":"Orf23"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11035791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"value":"Involved in the biosynthesis of the 2,3,6-trideoxysugar L-epivancosamine, the terminal sugar added to the aglycone scaffold of chloroeremomycin, a member of the glycopeptide antibiotics vancomycin family. Catalyzes the removal of the hydroxyl group at position C-2 of the hexose ring of dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose, and the oxidation of the hydroxyl group at position C-3 to form a carbonyl functionality. The product of the reaction, dTDP-2,6-dideoxy-D-glycero-hex-2-enos-4-ulose, is a highly unstable diketosugar, which spontaneously forms dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose = dTDP-3,4-didehydro-2,6-dideoxy-alpha-D-glucose + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47972"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57649"},{"database":"ChEBI","id":"CHEBI:84540"}],"ecNumber":"4.2.1.159","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11035791"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":4.0,"unit":"umol/min/mg","enzyme":"enzyme for dTDP-glucose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}]}],"michaelisConstants":[{"constant":56.0,"unit":"uM","substrate":"dTDP-glucose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}]}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11035791"}],"value":"Antibiotic biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"value":"The mutant Ala-381 is used to improve the quality of the crystals"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"value":"Two binding sites (pockets A and B) for the dTDP-sugar ligands have been identified in each subunit. It seems that pocket A represents the active site and pocket B is a vestige of the gene duplication event"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the hexose 2,3-dehydratase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"dTDP-4-dehydro-6-deoxy-alpha-D-glucopyranose 2,3-dehydratase","featureId":"PRO_0000444212"},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"from pocket A","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"1"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"from pocket A","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"1"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"from pocket B","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7H"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"2"}},{"type":"Binding site","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"from pocket A","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"1"}},{"type":"Binding site","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"from pocket B","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7H"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"2"}},{"type":"Binding site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"from pocket B","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7H"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"2"}},{"type":"Binding site","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"from pocket B","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7H"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"2"}},{"type":"Binding site","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"from pocket B","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7H"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"2"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"from pocket A","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57649"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"}],"ligand":{"name":"dTDP-4-dehydro-6-deoxy-alpha-D-glucose","id":"ChEBI:CHEBI:57649","label":"1"}},{"type":"Disulfide bond","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"Interchain","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7G"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4J7H"}]},{"type":"Mutagenesis","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Loss of dehydratase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Loss of dehydratase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A","Q"]}},{"type":"Mutagenesis","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"Same dehydratase activity compared to the wild type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"The mutation has little effect on the overall catalytic efficiency of the enzyme.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"R","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Loss of dehydratase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Loss of dehydratase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A","Q"]}},{"type":"Mutagenesis","location":{"start":{"value":452,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"Loss of dehydratase activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":452,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"Same dehydratase activity compared to the wild type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23473392"}],"alternativeSequence":{"originalSequence":"E","alternativeSequences":["Q"]}},{"type":"Helix","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Turn","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Turn","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Turn","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Beta strand","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]},{"type":"Helix","location":{"start":{"value":451,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4J7H"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"}],"references":[{"referenceNumber":1,"citation":{"id":"9545426","citationType":"journal article","authors":["van Wageningen A.","Kirkpatrick P.","Williams D.","Harris B.","Kershaw J.","Lennard N.","Jones M.","Jones S.","Solenberg P."],"citationCrossReferences":[{"database":"PubMed","id":"9545426"},{"database":"DOI","id":"10.1016/s1074-5521(98)90060-6"}],"title":"Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic.","publicationDate":"1998","journal":"Chem. Biol.","firstPage":"155","lastPage":"162","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"11035791","citationType":"journal article","authors":["Chen H.","Thomas M.G.","Hubbard B.K.","Losey H.C.","Walsh C.T.","Burkart M.D."],"citationCrossReferences":[{"database":"PubMed","id":"11035791"},{"database":"DOI","id":"10.1073/pnas.210395097"}],"title":"Deoxysugars in glycopeptide antibiotics: enzymatic synthesis of TDP-L-epivancosamine in chloroeremomycin biosynthesis.","publicationDate":"2000","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"11942","lastPage":"11947","volume":"97"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","PATHWAY"]},{"referenceNumber":3,"citation":{"id":"23473392","citationType":"journal article","authors":["Kubiak R.L.","Thoden J.B.","Holden H.M."],"citationCrossReferences":[{"database":"PubMed","id":"23473392"},{"database":"DOI","id":"10.1021/bi400176n"}],"title":"Structure of EvaA: a paradigm for sugar 2,3-dehydratases.","publicationDate":"2013","journal":"Biochemistry","firstPage":"2078","lastPage":"2088","volume":"52"},"referencePositions":["X-RAY CRYSTALLOGRAPHY OF MUTANT ALA-381 IN COMPLEX WITH SUBSTRATE ANALOGS","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","MUTAGENESIS OF GLU-139; GLU-190; ASP-353; ARG-381; GLU-404; GLU-405 AND GLU-452","DISULFIDE BONDS","SUBUNIT","REACTION MECHANISM"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ223998","properties":[{"key":"ProteinId","value":"CAA11763.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T17472","properties":[{"key":"EntryName","value":"T17472"}]},{"database":"PDB","id":"4J7G","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A/B=1-471"}]},{"database":"PDB","id":"4J7H","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.69 A"},{"key":"Chains","value":"A/B=1-471"}]},{"database":"AlphaFoldDB","id":"O52793","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O52793","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33630","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-18438","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.2.1.159","properties":[{"key":"OrganismId","value":"315"}]},{"database":"EvolutionaryTrace","id":"O52793","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016829","properties":[{"key":"GoTerm","value":"F:lyase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.79.40","properties":[{"key":"EntryName","value":"EvaA sugar 2,3-dehydratase subunit"},{"key":"MatchStatus","value":"3"}]},{"database":"InterPro","id":"IPR005212","properties":[{"key":"EntryName","value":"EvaA-like"}]},{"database":"InterPro","id":"IPR038153","properties":[{"key":"EntryName","value":"EvaA-like_sf"}]},{"database":"Pfam","id":"PF03559","properties":[{"key":"EntryName","value":"Hexose_dehydrat"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSSFVVPSLTAVRPRDHHDYADRIALSAATTDGVQMRTEDVRAWIAERRDANVFHVERIPFADLDQWWFEGVTGNLVHRSGRFFTIEGLHVIEHDGPHGDGPYREWQQPVIRQPEVGILGILAKEFDGVLHFLMQAKMEPGNPNLVQLSPTVQATRSNYTKAHGGTNVKLIEYFAPPDPERVIVDVLQAEQGSWFFRKSNRNMIVETVDDVPLWDDFCWLTLGQIAELMHEDETINMNSRSVLSCLPYQDITPRALFSDVQLLSWFTNERSRHDVRVRRIPLADVCGWKQGAEEIEHEDGRYFKVLAVAVKGSNREKISWTQPLVESVDLGVVAFLVRKIDGVPHVLVQARVDGGFLDTVELAPTVQCTPLNYAHLPAEERPPFLDLVQNAPRSRIRYEAIHSEEGGRFLGVRARYLVIDADEAIDPPPGYAWVTPAQLTALTRHGHYVNVEARTLLACINAAAAQPRGGA","length":471,"molWeight":53023,"crc64":"9D8ED63C2C98CA51","md5":"C8CDF02419CDB5A5D003E35EF2E519CF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":2,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":9,"Disulfide bond":1,"Mutagenesis":8,"Helix":16,"Beta strand":26,"Turn":3},"uniParcId":"UPI00000B41C6"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q56F26","uniProtkbId":"EBDG_AMYOR","entryAudit":{"firstPublicDate":"2010-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2006-03-21","entryVersion":96,"sequenceVersion":2},"annotationScore":5.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAX62629.2"}],"value":"Exo-beta-D-glucosaminidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16316314"}],"value":"GlcNase"}],"ecNumbers":[{"value":"3.2.1.165"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"16316314"}],"value":"Exochitinase"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAX62629.2"}],"value":"csxA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2351651"}],"value":"Hydrolyzes chitosan and chitooligosaccharides with retention of anomeric configuration. Has maximum activity on chitotetraose, chitopentaose and their corresponding alcohols, with a slight decrease in the rate of hydrolysis on longer chains. Has no activity against beta-D-glucopyranoside, beta-D-xylopyranoside, beta-D-mannoside, beta-D-glucuronide, beta-D-galactoside, beta-D-N-acetylgalactosamide, beta-D-N-acetylglucosaminide and alpha-D-N-acetylglucosaminide"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of chitosan or chitosan oligosaccharides to remove successive D-glucosamine residues from the non-reducing termini.","ecNumber":"3.2.1.165","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2351651"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2351651"}],"value":"Optimum pH is 5.5 with chitotriitol as substrate, and 5.3 with (GlcN)2 as substrate. Activity is lost below pH 3.5 and above pH 8.0."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2351651"}],"value":"Optimum temperature is 60 degrees Celsius. Stable below 50 degrees Celsius, inactive above 60 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18976664"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2351651"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2351651"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Belongs to the glycosyl hydrolase 2 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Propeptide","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"}],"featureId":"PRO_0000399046"},{"type":"Chain","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":1032,"modifier":"EXACT"}},"description":"Exo-beta-D-glucosaminidase","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"}],"featureId":"PRO_5000095799"},{"type":"Domain","location":{"start":{"value":909,"modifier":"EXACT"},"end":{"value":1032,"modifier":"EXACT"}},"description":"CBM6","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00523"}]},{"type":"Region","location":{"start":{"value":883,"modifier":"EXACT"},"end":{"value":908,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":469,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18976664"}]},{"type":"Active site","location":{"start":{"value":541,"modifier":"EXACT"},"end":{"value":541,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18976664"}]},{"type":"Sequence conflict","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"in Ref. 1; AA sequence","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["VN"]}},{"type":"Beta strand","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X09"}]},{"type":"Beta strand","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":416,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":437,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X09"}]},{"type":"Helix","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":486,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":499,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":503,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":521,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":542,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":551,"modifier":"EXACT"},"end":{"value":557,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":560,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":577,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZU"}]},{"type":"Beta strand","location":{"start":{"value":579,"modifier":"EXACT"},"end":{"value":581,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":587,"modifier":"EXACT"},"end":{"value":597,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":603,"modifier":"EXACT"},"end":{"value":628,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":632,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":636,"modifier":"EXACT"},"end":{"value":642,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":647,"modifier":"EXACT"},"end":{"value":649,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":651,"modifier":"EXACT"},"end":{"value":653,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":664,"modifier":"EXACT"},"end":{"value":672,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":675,"modifier":"EXACT"},"end":{"value":680,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":682,"modifier":"EXACT"},"end":{"value":684,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":691,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":693,"modifier":"EXACT"},"end":{"value":695,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":697,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":713,"modifier":"EXACT"},"end":{"value":724,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":726,"modifier":"EXACT"},"end":{"value":728,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZV"}]},{"type":"Beta strand","location":{"start":{"value":729,"modifier":"EXACT"},"end":{"value":735,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":744,"modifier":"EXACT"},"end":{"value":753,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":759,"modifier":"EXACT"},"end":{"value":770,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":776,"modifier":"EXACT"},"end":{"value":778,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":786,"modifier":"EXACT"},"end":{"value":788,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":793,"modifier":"EXACT"},"end":{"value":797,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":803,"modifier":"EXACT"},"end":{"value":811,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":815,"modifier":"EXACT"},"end":{"value":825,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":828,"modifier":"EXACT"},"end":{"value":830,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":841,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":852,"modifier":"EXACT"},"end":{"value":855,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":857,"modifier":"EXACT"},"end":{"value":860,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":865,"modifier":"EXACT"},"end":{"value":873,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Helix","location":{"start":{"value":874,"modifier":"EXACT"},"end":{"value":877,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":883,"modifier":"EXACT"},"end":{"value":888,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Turn","location":{"start":{"value":889,"modifier":"EXACT"},"end":{"value":891,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":892,"modifier":"EXACT"},"end":{"value":897,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZS"}]},{"type":"Beta strand","location":{"start":{"value":910,"modifier":"EXACT"},"end":{"value":912,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Helix","location":{"start":{"value":913,"modifier":"EXACT"},"end":{"value":915,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":916,"modifier":"EXACT"},"end":{"value":924,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":935,"modifier":"EXACT"},"end":{"value":938,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":945,"modifier":"EXACT"},"end":{"value":965,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":968,"modifier":"EXACT"},"end":{"value":970,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":974,"modifier":"EXACT"},"end":{"value":978,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":981,"modifier":"EXACT"},"end":{"value":987,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":999,"modifier":"EXACT"},"end":{"value":1007,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":1009,"modifier":"EXACT"},"end":{"value":1018,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]},{"type":"Beta strand","location":{"start":{"value":1026,"modifier":"EXACT"},"end":{"value":1031,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2VZP"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"id":"KW-0146","category":"Biological process","name":"Chitin degradation"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"16316314","citationType":"journal article","authors":["Cote N.","Fleury A.","Dumont-Blanchette E.","Fukamizo T.","Mitsutomi M.","Brzezinski R."],"citationCrossReferences":[{"database":"PubMed","id":"16316314"},{"database":"DOI","id":"10.1042/bj20051436"}],"title":"Two exo-beta-D-glucosaminidases/exochitosanases from actinomycetes define a new subfamily within family 2 of glycoside hydrolases.","publicationDate":"2006","journal":"Biochem. J.","firstPage":"675","lastPage":"686","volume":"394"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 47-60 AND 610-619","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","SUBCELLULAR LOCATION"],"referenceComments":[{"value":"ATCC 19795 / DSM 40040 / CBS 547.68 / JCM 4235 / KCTC 9412 / NBRC 12806 / NCIMB 12945 / M43-05865","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000305"},{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAX62629.2"}]},{"referenceNumber":2,"citation":{"id":"2351651","citationType":"journal article","authors":["Nanjo F.","Katsumi R.","Sakai K."],"citationCrossReferences":[{"database":"PubMed","id":"2351651"},{"database":"DOI","id":"10.1016/s0021-9258(19)38783-6"}],"title":"Purification and characterization of an exo-beta-D-glucosaminidase, a novel type of enzyme, from Nocardia orientalis.","publicationDate":"1990","journal":"J. Biol. Chem.","firstPage":"10088","lastPage":"10094","volume":"265"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","SUBCELLULAR LOCATION"],"evidences":[{"evidenceCode":"ECO:0000305"}]},{"referenceNumber":3,"citation":{"id":"18976664","citationType":"journal article","authors":["van Bueren A.L.","Ghinet M.G.","Gregg K.","Fleury A.","Brzezinski R.","Boraston A.B."],"citationCrossReferences":[{"database":"PubMed","id":"18976664"},{"database":"DOI","id":"10.1016/j.jmb.2008.10.031"}],"title":"The structural basis of substrate recognition in an exo-beta-D-glucosaminidase involved in chitosan hydrolysis.","publicationDate":"2009","journal":"J. Mol. Biol.","firstPage":"131","lastPage":"139","volume":"385"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH BETA-1,4-D-GLUCOSAMINE TETRASACCHARIDE","ACTIVE SITES"],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AY962188","properties":[{"key":"ProteinId","value":"AAX62629.2"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"2VZO","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.24 A"},{"key":"Chains","value":"A/B=1-1032"}]},{"database":"PDB","id":"2VZP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.05 A"},{"key":"Chains","value":"A/B=906-1032"}]},{"database":"PDB","id":"2VZQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A/B=906-1032"}]},{"database":"PDB","id":"2VZR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A/B=906-1032"}]},{"database":"PDB","id":"2VZS","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.85 A"},{"key":"Chains","value":"A/B=1-1032"}]},{"database":"PDB","id":"2VZT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A/B=1-1032"}]},{"database":"PDB","id":"2VZU","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.10 A"},{"key":"Chains","value":"A/B=1-1032"}]},{"database":"PDB","id":"2VZV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.70 A"},{"key":"Chains","value":"A/B=1-1032"}]},{"database":"PDB","id":"2X05","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.30 A"},{"key":"Chains","value":"A/B=1-1032"}]},{"database":"PDB","id":"2X09","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A/B=1-1032"}]},{"database":"AlphaFoldDB","id":"Q56F26","properties":[{"key":"Description","value":"-"}]},{"database":"MDposit","id":"Q56F26","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q56F26","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_25235","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"CBM35","properties":[{"key":"FamilyName","value":"Carbohydrate-Binding Module Family 35"}]},{"database":"CAZy","id":"GH2","properties":[{"key":"FamilyName","value":"Glycoside Hydrolase Family 2"}]},{"database":"KEGG","id":"ag:AAX62629","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG3250","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"BRENDA","id":"3.2.1.165","properties":[{"key":"OrganismId","value":"315"}]},{"database":"EvolutionaryTrace","id":"Q56F26","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"2351651"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0052761","properties":[{"key":"GoTerm","value":"F:exo-1,4-beta-D-glucosaminidase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"16316314"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2351651"}]},{"database":"GO","id":"GO:0004553","properties":[{"key":"GoTerm","value":"F:hydrolase activity, hydrolyzing O-glycosyl compounds"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"2351651"}]},{"database":"GO","id":"GO:0000272","properties":[{"key":"GoTerm","value":"P:polysaccharide catabolic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"2351651"}]},{"database":"CDD","id":"cd04082","properties":[{"key":"EntryName","value":"CBM35_pectate_lyase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.120.260:FF:000182","properties":[{"key":"EntryName","value":"Exo-beta-D-glucosaminidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.10:FF:001725","properties":[{"key":"EntryName","value":"Exo-beta-D-glucosaminidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.10:FF:002523","properties":[{"key":"EntryName","value":"Exo-beta-D-glucosaminidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.80:FF:000166","properties":[{"key":"EntryName","value":"Exo-beta-D-glucosaminidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.260","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"3"}]},{"database":"InterPro","id":"IPR036156","properties":[{"key":"EntryName","value":"Beta-gal/glucu_dom_sf"}]},{"database":"InterPro","id":"IPR054593","properties":[{"key":"EntryName","value":"Beta-mannosidase-like_N2"}]},{"database":"InterPro","id":"IPR005084","properties":[{"key":"EntryName","value":"CBM6"}]},{"database":"InterPro","id":"IPR043534","properties":[{"key":"EntryName","value":"EBDG/EBM"}]},{"database":"InterPro","id":"IPR008979","properties":[{"key":"EntryName","value":"Galactose-bd-like_sf"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"InterPro","id":"IPR006102","properties":[{"key":"EntryName","value":"Ig-like_GH2"}]},{"database":"InterPro","id":"IPR041351","properties":[{"key":"EntryName","value":"Ig_GlcNase"}]},{"database":"PANTHER","id":"PTHR43536","properties":[{"key":"EntryName","value":"MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43536:SF1","properties":[{"key":"EntryName","value":"MANNOSYLGLYCOPROTEIN ENDO-BETA-MANNOSIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16990","properties":[{"key":"EntryName","value":"CBM_35"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00703","properties":[{"key":"EntryName","value":"Glyco_hydro_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22666","properties":[{"key":"EntryName","value":"Glyco_hydro_2_N2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18368","properties":[{"key":"EntryName","value":"Ig_GlcNase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF49303","properties":[{"key":"EntryName","value":"beta-Galactosidase/glucuronidase domain"},{"key":"MatchStatus","value":"3"}]},{"database":"SUPFAM","id":"SSF49785","properties":[{"key":"EntryName","value":"Galactose-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51175","properties":[{"key":"EntryName","value":"CBM6"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFRQKRTRIPLLAMTVTALAAAVCGVTTAPAATGAEVAVPLSVGAAAGNATPIPGYVIQSSAQVSDDSAVSKPGFPTSGWYPVSSRSTVYAGLLQNGKYADPFYSTNMQNVPAAQFSVPWWYRTDLNVDDTSSRTYLDFSGVLSKADVWVNGTKVATKDQVNGAYTRHDLDITAQVHTGVNSVAFKVYPNDPNRDLSMGWIDWAQTPPDQNMGIVRDVLVRRSGAVALRSAHVIQKLNSALDHADLTVKADVRNDSANAVQTTVAGTVAGKPISQTVSLAAKERKTVTFPLVGLDRPNVWWPAGMGGQHRYDLDLTASVGGTPSDAAKSKFGVRDVKATLNSSGGRQYSVNGKPLLIRGGGYTPDLFLRWNETAAADKLKYVLNLGLNTVRLEGHIEPDEFFDIADDLGVLTMPGWECCDKWEGQVNGEEKGEPWVESDYPIAKASMFSEAERLRDHPSVISFHIGSDFAPDRRIEQGYLDAMKAADFLLPVIPAASARPSPITGASGMKMNGPYDYVPPVYWYDKSQKDRGGAWSFNSETSAGVDIPTMDTLKRMMSASELDTMWKNPSAKQYHRSSSDTFGNLKLFGDALTKRYGASANLNDFVRKAQLSQYENVRAEFESHSRNYTDSTNPSTGLIYWMLNSPWTSLHWQLFDAYMDQNGAYYGAKKANEPLHIQYSHDNRSVVVINQTSNAVSGLTATTKLYNLDGTEKYSNTKTGLSVGALGAKATAVTVPAVSGLSTTYLAKWVLTDSSGKEVSRNVYWLSTKADTLNWGGSDWYYTPQSAFADLSGLNNLGQSAVGATANSVAGADGTTTTTVTLKNTSGGRLPAFYVDSKVVDSAGKPVLPVEWNDNAVSLWPGETTTLTAKYRTADLKGSKPSVRISGWNTGTQTVPADGSGPGPSDPVDYQAEDATIVQGAVESNHAGYTGTGFVNYDNVAGSSVEWTVTVPSAGTYDVVVRYANGTTTSRPLDFSVNGSISASGVAFGSTGTWPAWTTKTVRVTLAAGVNKIKAVATTANGGPNVDKITL","length":1032,"molWeight":110633,"crc64":"150778589094F223","md5":"A39F528DEFD2077F63FD0CDC9BAC1E6C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Propeptide":1,"Chain":1,"Domain":1,"Region":1,"Active site":2,"Sequence conflict":1,"Beta strand":67,"Helix":21,"Turn":11},"uniParcId":"UPI000069A9F3"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O52792","uniProtkbId":"HMO_AMYOR","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-06-01","entryVersion":101,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"4-hydroxymandelate oxidase"},"ecNumbers":[{"value":"1.1.3.46"}]}},"genes":[{"geneName":{"value":"hmo"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12240298"}],"value":"Catalyzes the oxidation of p-hydroxymandelate to p-hydroxybenzoylformate in the biosynthesis of L-(4-hydroxyphenyl)glycine and L-(3,5-dihydroxyphenyl)glycine, 2 non-proteinogenic amino acids occurring in the vancomycin group of antibiotics"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-4-hydroxymandelate + O2 = 4-hydroxyphenylglyoxylate + H2O2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41227"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17210"},{"database":"ChEBI","id":"CHEBI:58586"}],"ecNumber":"1.1.3.46","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12240298"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12240298"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9545426"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"value":"Belongs to the FMN-dependent alpha-hydroxy acid dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"4-hydroxymandelate oxidase","featureId":"PRO_0000430441"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"FMN hydroxy acid dehydrogenase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}]},{"type":"Active site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}]},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:35179"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"a 2-oxocarboxylate","id":"ChEBI:CHEBI:35179"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:35179"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"a 2-oxocarboxylate","id":"ChEBI:CHEBI:35179"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:35179"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"a 2-oxocarboxylate","id":"ChEBI:CHEBI:35179"}},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00683"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Helix","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZQ"}]},{"type":"Helix","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Turn","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZQ"}]},{"type":"Helix","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZQ"}]},{"type":"Helix","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Helix","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]},{"type":"Beta strand","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5ZZR"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0288","category":"Ligand","name":"FMN"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"9545426","citationType":"journal article","authors":["van Wageningen A.","Kirkpatrick P.","Williams D.","Harris B.","Kershaw J.","Lennard N.","Jones M.","Jones S.","Solenberg P."],"citationCrossReferences":[{"database":"PubMed","id":"9545426"},{"database":"DOI","id":"10.1016/s1074-5521(98)90060-6"}],"title":"Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic.","publicationDate":"1998","journal":"Chem. Biol.","firstPage":"155","lastPage":"162","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PATHWAY"]},{"referenceNumber":2,"citation":{"id":"11137816","citationType":"journal article","authors":["Hubbard B.K.","Thomas M.G.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11137816"},{"database":"DOI","id":"10.1016/s1074-5521(00)00043-0"}],"title":"Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics.","publicationDate":"2000","journal":"Chem. Biol.","firstPage":"931","lastPage":"942","volume":"7"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR"]},{"referenceNumber":3,"citation":{"id":"12240298","citationType":"journal article","authors":["Li T.L.","Choroba O.W.","Charles E.H.","Sandercock A.M.","Williams D.H.","Spencer J.B."],"citationCrossReferences":[{"database":"PubMed","id":"12240298"},{"database":"DOI","id":"10.1039/b103548g"}],"title":"Characterisation of a hydroxymandelate oxidase involved in the biosynthesis of two unusual amino acids occurring in the vancomycin group of antibiotics.","publicationDate":"2001","journal":"Chem. Commun. (Camb.)","firstPage":"1752","lastPage":"1753","volume":"18"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ223998","properties":[{"key":"ProteinId","value":"CAA11762.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T17471","properties":[{"key":"EntryName","value":"T17471"}]},{"database":"PDB","id":"5ZZP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.39 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"5ZZQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.32 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"5ZZR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.31 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"5ZZS","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"5ZZT","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.35 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"5ZZX","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.49 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"5ZZY","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.50 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"5ZZZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.45 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A00","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.59 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A01","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.87 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A08","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A0B","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.65 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A0D","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.65 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A0G","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A0M","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.75 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A0O","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A0V","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.39 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A0Y","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A11","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.45 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A13","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A19","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1A","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.35 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1B","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.47 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1H","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.36 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1L","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.40 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1M","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.55 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1N","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.42 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1P","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.51 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1R","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.65 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A1W","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A21","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.50 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A23","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.65 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A24","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.39 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A36","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.44 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A39","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.89 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A3D","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.92 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A3T","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.51 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A4G","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.04 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6A4H","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.99 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"6AI7","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.07 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"PDB","id":"7BSR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.89 A"},{"key":"Chains","value":"A=1-357"}]},{"database":"AlphaFoldDB","id":"O52792","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O52792","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33640","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ag:CAA11762","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.1.3.46","properties":[{"key":"OrganismId","value":"315"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0003973","properties":[{"key":"GoTerm","value":"F:(S)-2-hydroxy-acid oxidase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11137816"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"12240298"}]},{"database":"GO","id":"GO:0016899","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-OH group of donors, oxygen as acceptor"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11137816"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"12240298"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11137816"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"12240298"}]},{"database":"CDD","id":"cd02809","properties":[{"key":"EntryName","value":"alpha_hydroxyacid_oxid_FMN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000029","properties":[{"key":"EntryName","value":"L-lactate dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR012133","properties":[{"key":"EntryName","value":"Alpha-hydoxy_acid_DH_FMN"}]},{"database":"InterPro","id":"IPR000262","properties":[{"key":"EntryName","value":"FMN-dep_DH"}]},{"database":"InterPro","id":"IPR037396","properties":[{"key":"EntryName","value":"FMN_HAD"}]},{"database":"InterPro","id":"IPR008259","properties":[{"key":"EntryName","value":"FMN_hydac_DH_AS"}]},{"database":"PANTHER","id":"PTHR10578:SF107","properties":[{"key":"EntryName","value":"2-HYDROXYACID OXIDASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10578","properties":[{"key":"EntryName","value":"S -2-HYDROXY-ACID OXIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01070","properties":[{"key":"EntryName","value":"FMN_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000138","properties":[{"key":"EntryName","value":"Al-hdrx_acd_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00557","properties":[{"key":"EntryName","value":"FMN_HYDROXY_ACID_DH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51349","properties":[{"key":"EntryName","value":"FMN_HYDROXY_ACID_DH_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTYVSLADLERAARDVLPGEIFDFLAGGSGTEASLVANRTALERVFVIPRMLRDLTDVTTEIDIFGRRAALPMAVAPVAYQRLFHPEGELAVARAARDAGVPYTICTLSSVSLEEIAAVGGRPWFQLYWLRDEKRSLDLVRRAEDAGCEAIVFTVDVPWMGRRLRDMRNGFALPEWVTAANFDAGTAAHRRTQGVSAVADHTAREFAPATWESVEAVRAHTDLPVVLKGILAVEDARRAVDAGAGGIVVSNHGGRQLDGAVPGIEMLGEIVAAVSGGCEVLVDGGIRSGGDVLKATALGASAVLVGRPVMWALAAAGQDGVRQLLELLAEEVRDAMGLAGCESVGAARRLNTKLGVV","length":357,"molWeight":37832,"crc64":"15EBFFEA0CA946C0","md5":"46D2EA1E201A933DDF5A6987CDFD0A30"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Active site":1,"Binding site":8,"Helix":16,"Beta strand":12,"Turn":1},"uniParcId":"UPI00000B8F3F"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9AFC7","uniProtkbId":"GTFD_AMYOR","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2001-06-01","entryVersion":83,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Devancosaminyl-vancomycin vancosaminetransferase"},"ecNumbers":[{"value":"2.4.1.322"}]},"alternativeNames":[{"fullName":{"value":"Devancosamine-vancomycin TDP-vancosaminyltransferase"}},{"fullName":{"value":"Glycosyltransferase GtfD"}}]},"genes":[{"geneName":{"value":"gtfD"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"value":"Catalyzes the attachment of L-vancosamine to a monoglucosylated heptapeptide intermediate during the final stage of glycopeptide antibiotic vancomycin biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dTDP-beta-L-vancosamine + devancoaminyl-vancomycin = vancomycin + dTDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:39891"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58369"},{"database":"ChEBI","id":"CHEBI:75953"},{"database":"ChEBI","id":"CHEBI:76839"},{"database":"ChEBI","id":"CHEBI:76842"}],"ecNumber":"2.4.1.322","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":16.3,"unit":"uM","substrate":"devancoaminyl-vancomycin","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}]},{"constant":2.0,"unit":"mM","substrate":"UDP-L-epivancosamine","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}]}],"note":{"texts":[{"value":"kcat is 67.6 min(-1)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"value":"In A.orientalis different glycosyltransferases are involved in biosynthesis of the vancomycin group of antibiotics. GtfA (AC P96558), GtfB (AC P96559) and GtfC (AC P96560) are involved in biosynthesis of antibiotic chloroeremomycin, while GtfD and GtfE (AC G4V4R9) are involved in biosynthesis of vancomycin"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyltransferase 28 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Devancosaminyl-vancomycin vancosaminetransferase","featureId":"PRO_0000430439"},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58369"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"dTDP","id":"ChEBI:CHEBI:58369"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15903"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"beta-D-glucose","id":"ChEBI:CHEBI:15903"}},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75953"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"devancoaminyl-vancomycin","id":"ChEBI:CHEBI:75953"}},{"type":"Binding site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75953"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"devancoaminyl-vancomycin","id":"ChEBI:CHEBI:75953"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15903"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"beta-D-glucose","id":"ChEBI:CHEBI:15903"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58369"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"dTDP","id":"ChEBI:CHEBI:58369"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58369"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"dTDP","id":"ChEBI:CHEBI:58369"}},{"type":"Binding site","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58369"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"ligand":{"name":"dTDP","id":"ChEBI:CHEBI:58369"}},{"type":"Mutagenesis","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"Strongly decreased activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"alternativeSequence":{"originalSequence":"T","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Abolishes catalytic activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15122882"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Turn","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Turn","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Turn","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Beta strand","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Turn","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]},{"type":"Helix","location":{"start":{"value":387,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1RRV"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"11294642","citationType":"journal article","authors":["Losey H.C.","Peczuh M.W.","Chen Z.","Eggert U.S.","Dong S.D.","Pelczer I.","Kahne D.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11294642"},{"database":"DOI","id":"10.1021/bi010050w"}],"title":"Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides.","publicationDate":"2001","journal":"Biochemistry","firstPage":"4745","lastPage":"4755","volume":"40"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","PATHWAY"],"referenceComments":[{"value":"ATCC 19795 / DSM 40040 / CBS 547.68 / JCM 4235 / KCTC 9412 / NBRC 12806 / NCIMB 12945 / M43-05865","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"15122882","citationType":"journal article","authors":["Mulichak A.M.","Lu W.","Losey H.C.","Walsh C.T.","Garavito R.M."],"citationCrossReferences":[{"database":"PubMed","id":"15122882"},{"database":"DOI","id":"10.1021/bi036130c"}],"title":"Crystal structure of vancosaminyltransferase GtfD from the vancomycin biosynthetic pathway: interactions with acceptor and nucleotide ligands.","publicationDate":"2004","journal":"Biochemistry","firstPage":"5170","lastPage":"5180","volume":"43"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH DTDP; DEVANCOAMINYL-VANCOMYCIN AND BETA-D-GLUCOSE","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","MUTAGENESIS OF THR-10 AND ASP-13"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF351621","properties":[{"key":"ProteinId","value":"AAK31352.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"1RRV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A/B=1-408"}]},{"database":"AlphaFoldDB","id":"Q9AFC7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9AFC7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33690","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB04529","properties":[{"key":"GenericName","value":"Desvancosaminyl vancomycin"}]},{"database":"CAZy","id":"GT1","properties":[{"key":"FamilyName","value":"Glycosyltransferase Family 1"}]},{"database":"KEGG","id":"ag:AAK31352","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1819","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-18443","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.4.1.322","properties":[{"key":"OrganismId","value":"315"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q9AFC7","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016758","properties":[{"key":"GoTerm","value":"F:hexosyltransferase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15122882"}]},{"database":"GO","id":"GO:0008194","properties":[{"key":"GoTerm","value":"F:UDP-glycosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15122882"}]},{"database":"CDD","id":"cd03784","properties":[{"key":"EntryName","value":"GT1_Gtf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000292","properties":[{"key":"EntryName","value":"Glycosyltransferase GtfE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000009","properties":[{"key":"EntryName","value":"Sterol 3-beta-glucosyltransferase UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR010610","properties":[{"key":"EntryName","value":"EryCIII-like_C"}]},{"database":"InterPro","id":"IPR050426","properties":[{"key":"EntryName","value":"Glycosyltransferase_28"}]},{"database":"InterPro","id":"IPR004276","properties":[{"key":"EntryName","value":"GlycoTrans_28_N"}]},{"database":"InterPro","id":"IPR002213","properties":[{"key":"EntryName","value":"UDP_glucos_trans"}]},{"database":"PANTHER","id":"PTHR48050","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48050:SF13","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06722","properties":[{"key":"EntryName","value":"EryCIII-like_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03033","properties":[{"key":"EntryName","value":"Glyco_transf_28"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVLLSVCGTRGDVEIGVALADRLKALGVQTRMCAPPAAEERLAEVGVPHVPVGLPQHMMLQEGMPPPPPEEEQRLAAMTVEMQFDAVPGAAEGCAAVVAVGDLAAATGVRSVAEKLGLPFFYSVPSPVYLASPHLPPAYDEPTTPGVTDIRVLWEERAARFADRYGPTLNRRRAEIGLPPVEDVFGYGHGERPCWPADPVLAPLQPDVDAVQTGAWLLSDERPLPPELEAFLAAGSPPVHIGFGSSSGRGIADAAKVAVEAIRAQGRRVILSRGWTELVLPDDRDDCFAIDEVNFQALFRRVAAVIHHGSAGTEHVATRAGVPQLVIPRNTDQPYFAGRVAALGIGVAHDGPTPTFESLSAALTTVLAPETRARAEAVAGMVLTDGAAAAADLVLAAVGREKPAVPA","length":408,"molWeight":42881,"crc64":"1233D71CD99D1FBD","md5":"AF868C665255B04D702800907E19AFDD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":8,"Mutagenesis":2,"Beta strand":14,"Helix":21,"Turn":4},"uniParcId":"UPI00000AE849"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O52791","uniProtkbId":"HMAS_AMYOR","entryAudit":{"firstPublicDate":"2012-09-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-06-01","entryVersion":81,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"4-hydroxymandelate synthase"},"shortNames":[{"value":"HMS"},{"value":"HmaS"}],"ecNumbers":[{"value":"1.13.11.46"}]},"alternativeNames":[{"fullName":{"value":"4-hydroxyphenylpyruvate dioxygenase II"}}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"}],"value":"Required to synthesize hydroxyphenylglycine, a recurring skeletal component of nonproteinogenic macrocyclic peptide antibiotics such as vancomycin. Catalyzes the conversion of p-hydroxyphenylpyruvate to p-hydroxymandelate. The decarboxylation and hydroxylation activities of HmaS show novel and distinct regioselectivity, compared to all other known p-hydroxyphenylpyruvate dioxygenases, by hydroxylating the benzylic position of the substrate instead of the phenyl ring"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-(4-hydroxyphenyl)pyruvate + O2 = (S)-4-hydroxymandelate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21376"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17210"},{"database":"ChEBI","id":"CHEBI:36242"}],"ecNumber":"1.13.11.46","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe cation","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18215022"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:24875"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18215022"}],"value":"Binds 1 Fe cation per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9545426"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18215022"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the 4HPPD family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"4-hydroxymandelate synthase","featureId":"PRO_0000418534"},{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"VOC 1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Domain","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"VOC 2","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18215022"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18215022"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18215022"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"18215022"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:24875"}],"ligand":{"name":"Fe cation","id":"ChEBI:CHEBI:24875"}},{"type":"Beta strand","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Turn","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Beta strand","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]},{"type":"Helix","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2R5V"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"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":"9545426","citationType":"journal article","authors":["van Wageningen A.","Kirkpatrick P.","Williams D.","Harris B.","Kershaw J.","Lennard N.","Jones M.","Jones S.","Solenberg P."],"citationCrossReferences":[{"database":"PubMed","id":"9545426"},{"database":"DOI","id":"10.1016/s1074-5521(98)90060-6"}],"title":"Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic.","publicationDate":"1998","journal":"Chem. Biol.","firstPage":"155","lastPage":"162","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PATHWAY"]},{"referenceNumber":2,"citation":{"id":"11137816","citationType":"journal article","authors":["Hubbard B.K.","Thomas M.G.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11137816"},{"database":"DOI","id":"10.1016/s1074-5521(00)00043-0"}],"title":"Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics.","publicationDate":"2000","journal":"Chem. Biol.","firstPage":"931","lastPage":"942","volume":"7"},"referencePositions":["FUNCTION IN THE BIOSYNTHESIS OF L-P-HYDROXYPHENYLGLYCINE AND AS A HYDROXYMANDELATE SYNTHASE","CATALYTIC ACTIVITY","NOMENCLATURE"]},{"referenceNumber":3,"citation":{"id":"18215022","citationType":"journal article","authors":["Brownlee J.","He P.","Moran G.R.","Harrison D.H."],"citationCrossReferences":[{"database":"PubMed","id":"18215022"},{"database":"DOI","id":"10.1021/bi701438r"}],"title":"Two roads diverged: the structure of hydroxymandelate synthase from Amycolatopsis orientalis in complex with 4-hydroxymandelate.","publicationDate":"2008","journal":"Biochemistry","firstPage":"2002","lastPage":"2013","volume":"47"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH SUBSTRATE AND METAL","REACTION MECHANISM","COFACTOR","SUBUNIT"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ223998","properties":[{"key":"ProteinId","value":"CAA11761.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T17470","properties":[{"key":"EntryName","value":"T17470"}]},{"database":"PDB","id":"2R5V","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.30 A"},{"key":"Chains","value":"A/B=1-357"}]},{"database":"AlphaFoldDB","id":"O52791","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O52791","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33645","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB07896","properties":[{"key":"GenericName","value":"(2S)-hydroxy(4-hydroxyphenyl)ethanoic acid"}]},{"database":"KEGG","id":"ag:CAA11761","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"1.1.3.46","properties":[{"key":"OrganismId","value":"315"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"O52791","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0050585","properties":[{"key":"GoTerm","value":"F:4-hydroxymandelate synthase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11137816"}]},{"database":"GO","id":"GO:0003868","properties":[{"key":"GoTerm","value":"F:4-hydroxyphenylpyruvate dioxygenase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"18215022"}]},{"database":"GO","id":"GO:0006572","properties":[{"key":"GoTerm","value":"P:L-tyrosine catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11137816"}]},{"database":"CDD","id":"cd07250","properties":[{"key":"EntryName","value":"HPPD_C_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08342","properties":[{"key":"EntryName","value":"HPPD_N_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.180.10:FF:000041","properties":[{"key":"EntryName","value":"4-hydroxymandelate synthase"},{"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":"IPR005956","properties":[{"key":"EntryName","value":"4OHPhenylPyrv_dOase"}]},{"database":"InterPro","id":"IPR041735","properties":[{"key":"EntryName","value":"4OHPhenylPyrv_dOase_C"}]},{"database":"InterPro","id":"IPR041736","properties":[{"key":"EntryName","value":"4OHPhenylPyrv_dOase_N"}]},{"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":"NCBIfam","id":"TIGR01263","properties":[{"key":"EntryName","value":"4HPPD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11959","properties":[{"key":"EntryName","value":"4-HYDROXYPHENYLPYRUVATE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11959:SF1","properties":[{"key":"EntryName","value":"4-HYDROXYPHENYLPYRUVATE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00903","properties":[{"key":"EntryName","value":"Glyoxalase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14696","properties":[{"key":"EntryName","value":"Glyoxalase_5"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF009283","properties":[{"key":"EntryName","value":"HPP_dOase"},{"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":"PS51819","properties":[{"key":"EntryName","value":"VOC"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MQNFEIDYVEMYVENLEVAAFSWVDKYAFAVAGTSRSADHRSIALRQGQVTLVLTEPTSDRHPAAAYLQTHGDGVADIAMATSDVAAAYEAAVRAGAEAVRAPGQHSEAAVTTATIGGFGDVVHTLIQRDGTSAELPPGFTGSMDVTNHGKGDVDLLGIDHFAICLNAGDLGPTVEYYERALGFRQIFDEHIVVGAQAMNSTVVQSASGAVTLTLIEPDRNADPGQIDEFLKDHQGAGVQHIAFNSNDAVRAVKALSERGVEFLKTPGAYYDLLGERITLQTHSLDDLRATNVLADEDHGGQLFQIFTASTHPRHTIFFEVIERQGAGTFGSSNIKALYEAVELERTGQSEFGAARR","length":357,"molWeight":38339,"crc64":"F146FCE537CEF2CA","md5":"D6A2EC69B677987A3879A84216B3A2D1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":2,"Binding site":8,"Beta strand":18,"Helix":9,"Turn":1},"uniParcId":"UPI00000B8DAC"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G4V4T4","uniProtkbId":"DPGA_AMYOR","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2011-12-14","entryVersion":36,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11752437"}],"value":"3,5-dihydroxyphenylacetyl-CoA synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"2.3.1.246"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"3,5-dihydroxyphenylacetyl-CoA synthase polyketide synthase type III"}}]},"genes":[{"geneName":{"value":"dpgA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the Claisen condensation of four molecules of malonyl-CoA to yield 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) and three free coenzyme A (CoA). DpgA requires the presence of the dehydratases DpgB and DpgD to facilitate the aromatization of the DPA-S-DgpA or DPA-S-CoA intermediate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 malonyl-CoA + 4 H(+) = (3,5-dihydroxyphenyl)acetyl-CoA + 4 CO2 + 3 CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44744"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:84554"}],"ecNumber":"2.3.1.246","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":5.0,"unit":"uM","substrate":"malonyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"kcat is 1 min(-1) for transferase activity with malonyl-CoA as substrate."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11752437"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the thiolase-like superfamily. Chalcone/stilbene synthases family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"3,5-dihydroxyphenylacetyl-CoA synthase","featureId":"PRO_0000435602"},{"type":"Active site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q939X3"}]}],"keywords":[{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-334RPSRS0J50E","citationType":"submission","authors":["Woertz T.","Dietz S.","Zerbe K.","Robinson J.A."],"title":"The vancomycin biosynthetic gene cluster.","publicationDate":"SEP-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC19795","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"11752437","citationType":"journal article","authors":["Chen H.","Tseng C.C.","Hubbard B.K.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11752437"},{"database":"DOI","id":"10.1073/pnas.221582098"}],"title":"Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.","publicationDate":"2001","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"14901","lastPage":"14906","volume":"98"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"NRRL18098","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HE589771","properties":[{"key":"ProteinId","value":"CCD33159.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"G4V4T4","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"G4V4T4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33610","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG3424","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0016747","properties":[{"key":"GoTerm","value":"F:acyltransferase activity, transferring groups other than amino-acyl groups"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"14744141"}]},{"database":"GO","id":"GO:0030639","properties":[{"key":"GoTerm","value":"P:polyketide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd00831","properties":[{"key":"EntryName","value":"CHS_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.47.10:FF:000103","properties":[{"key":"EntryName","value":"3,5-dihydroxyphenylacetyl-CoA synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.47.10:FF:000014","properties":[{"key":"EntryName","value":"Chalcone synthase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.47.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR001099","properties":[{"key":"EntryName","value":"Chalcone/stilbene-like_synt_N"}]},{"database":"InterPro","id":"IPR012328","properties":[{"key":"EntryName","value":"Chalcone/stilbene_synt_C"}]},{"database":"InterPro","id":"IPR053446","properties":[{"key":"EntryName","value":"DPA-CoA_Synthase"}]},{"database":"InterPro","id":"IPR011141","properties":[{"key":"EntryName","value":"Polyketide_synthase_type-III"}]},{"database":"InterPro","id":"IPR016039","properties":[{"key":"EntryName","value":"Thiolase-like"}]},{"database":"NCBIfam","id":"NF042429","properties":[{"key":"EntryName","value":"DHPHCoAsyn_DpgA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11877","properties":[{"key":"EntryName","value":"HYDROXYMETHYLGLUTARYL-COA SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11877:SF46","properties":[{"key":"EntryName","value":"TYPE III POLYKETIDE SYNTHASE A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02797","properties":[{"key":"EntryName","value":"Chal_sti_synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00195","properties":[{"key":"EntryName","value":"Chal_sti_synt_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000451","properties":[{"key":"EntryName","value":"PKS_III"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53901","properties":[{"key":"EntryName","value":"Thiolase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDVSMTTGIELTEELSVLNGLTEITRFAGVGTAVSETSYSQTELLDILDVEDPKIRSVFLNSAIDRRFLTLPPENPGGGRLAEPQGDLLDKHKKIAVDMGCRALEACLKSAGATLSDLRHLCCVTSTGFLTPGLSALIIREMGIDPHCSRSDIVGMGCNAGLNALNVVSGWSAAHPGELGVVLCSEACSAAYALDGTMRTAVVNSLFGDGSAALAVISGDGRVAGPRVLKFASYIITDAVDAMRYDWDRDQDRFSFFLDPQIPYVVGAHAEIVVDRLLSGTGLRRSDIGHWLVHSGGKKVVDAVVVNLGLSRHDVRHTTGVLRDYGNLSSGSFLFSYERLSEEDVTRPGDYGVLMTMGPGSTIEMALIQW","length":370,"molWeight":39582,"crc64":"1A08B816E38282F5","md5":"5510F35F05923B6CA2C8EBACD3C56EDC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1},"uniParcId":"UPI00022AB468"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P96558","uniProtkbId":"GTFA_AMYOR","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1997-05-01","entryVersion":108,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"dTDP-epi-vancosaminyltransferase"},"ecNumbers":[{"value":"2.4.1.311"}]},"alternativeNames":[{"fullName":{"value":"Glycosyltransferase AH1"},"shortNames":[{"value":"GtfAH1"}]},{"fullName":{"value":"Glycosyltransferase GtfA"}}]},"genes":[{"geneName":{"value":"gtfA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15070728"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"19549605"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9115410"}],"value":"Catalyzes the attachment of 4-epi-vancosamine from a TDP donor to the beta-OH-Tyr-6 of the aglycone cosubstrate in the biosynthesis of glycopeptide antibiotic chloroeremomycin, a member of the vancomycin group of antibiotics. Strongly prefers devancoaminyl-vancomycin (DVV) as substrate rather than the heptapeptide vancomycin aglycone (AGV). Acts downstream of GtfB"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dTDP-beta-L-4-epi-vancosamine + devancoaminyl-vancomycin = chloroorienticin B + dTDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:38591"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58369"},{"database":"ChEBI","id":"CHEBI:75953"},{"database":"ChEBI","id":"CHEBI:75957"},{"database":"ChEBI","id":"CHEBI:75963"}],"ecNumber":"2.4.1.311","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15070728"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15070728"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9545426"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"value":"In A.orientalis different glycosyltransferases are involved in biosynthesis of the vancomycin group of antibiotics. GtfA, GtfB (AC P96559) and GtfC (AC P96560) are involved in biosynthesis of antibiotic chloroeremomycin, while GtfD (AC Q9AFC7) and GtfE (AC G4V4R9) are involved in biosynthesis of vancomycin"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyltransferase 28 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"dTDP-epi-vancosaminyltransferase","featureId":"PRO_0000430436"},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75957"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"dTDP-beta-L-4-epi-vancosamine","id":"ChEBI:CHEBI:75957"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75953"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"devancoaminyl-vancomycin","id":"ChEBI:CHEBI:75953"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75953"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"devancoaminyl-vancomycin","id":"ChEBI:CHEBI:75953"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75953"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"devancoaminyl-vancomycin","id":"ChEBI:CHEBI:75953"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75953"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"devancoaminyl-vancomycin","id":"ChEBI:CHEBI:75953"}},{"type":"Binding site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75957"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"dTDP-beta-L-4-epi-vancosamine","id":"ChEBI:CHEBI:75957"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75957"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"dTDP-beta-L-4-epi-vancosamine","id":"ChEBI:CHEBI:75957"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75957"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"dTDP-beta-L-4-epi-vancosamine","id":"ChEBI:CHEBI:75957"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:75957"}],"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"12874381"}],"ligand":{"name":"dTDP-beta-L-4-epi-vancosamine","id":"ChEBI:CHEBI:75957"}},{"type":"Beta strand","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Beta strand","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Beta strand","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Beta strand","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Beta strand","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Helix","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Turn","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3H4T"}]},{"type":"Beta strand","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PNV"}]},{"type":"Helix","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Beta strand","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Beta strand","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Beta strand","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Turn","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Beta strand","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Beta strand","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Beta strand","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Beta strand","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":360,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]},{"type":"Helix","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1PN3"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9115410","citationType":"journal article","authors":["Solenberg P.J.","Matsushima P.","Stack D.R.","Wilkie S.C.","Thompson R.C.","Baltz R.H."],"citationCrossReferences":[{"database":"PubMed","id":"9115410"},{"database":"DOI","id":"10.1016/s1074-5521(97)90288-x"}],"title":"Production of hybrid glycopeptide antibiotics in vitro and in Streptomyces toyocaensis.","publicationDate":"1997","journal":"Chem. Biol.","firstPage":"195","lastPage":"202","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION"]},{"referenceNumber":2,"citation":{"id":"9545426","citationType":"journal article","authors":["van Wageningen A.","Kirkpatrick P.","Williams D.","Harris B.","Kershaw J.","Lennard N.","Jones M.","Jones S.","Solenberg P."],"citationCrossReferences":[{"database":"PubMed","id":"9545426"},{"database":"DOI","id":"10.1016/s1074-5521(98)90060-6"}],"title":"Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic.","publicationDate":"1998","journal":"Chem. Biol.","firstPage":"155","lastPage":"162","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PATHWAY"]},{"referenceNumber":3,"citation":{"id":"15070728","citationType":"journal article","authors":["Lu W.","Oberthuer M.","Leimkuhler C.","Tao J.","Kahne D.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"15070728"},{"database":"DOI","id":"10.1073/pnas.0400277101"}],"title":"Characterization of a regiospecific epivancosaminyl transferase GtfA and enzymatic reconstitution of the antibiotic chloroeremomycin.","publicationDate":"2004","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"4390","lastPage":"4395","volume":"101"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","PATHWAY"]},{"referenceNumber":4,"citation":{"id":"12874381","citationType":"journal article","authors":["Mulichak A.M.","Losey H.C.","Lu W.","Wawrzak Z.","Walsh C.T.","Garavito R.M."],"citationCrossReferences":[{"database":"PubMed","id":"12874381"},{"database":"DOI","id":"10.1073/pnas.1233577100"}],"title":"Structure of the TDP-epi-vancosaminyltransferase GtfA from the chloroeremomycin biosynthetic pathway.","publicationDate":"2003","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"9238","lastPage":"9243","volume":"100"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH VANCOMYCIN AND DTDP-BETA-L-4-EPI-VANCOSAMINE"]},{"referenceNumber":5,"citation":{"id":"19549605","citationType":"journal article","authors":["Truman A.W.","Dias M.V.","Wu S.","Blundell T.L.","Huang F.","Spencer J.B."],"citationCrossReferences":[{"database":"PubMed","id":"19549605"},{"database":"DOI","id":"10.1016/j.chembiol.2009.04.013"}],"title":"Chimeric glycosyltransferases for the generation of hybrid glycopeptides.","publicationDate":"2009","journal":"Chem. Biol.","firstPage":"676","lastPage":"685","volume":"16"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH UDP-2-DEOXY-2-FLUORO-GLUCOSE","FUNCTION"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U84349","properties":[{"key":"ProteinId","value":"AAB49292.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AJ223998","properties":[{"key":"ProteinId","value":"CAA11774.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T30584","properties":[{"key":"EntryName","value":"T30584"}]},{"database":"PDB","id":"1PN3","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.80 A"},{"key":"Chains","value":"A/B=1-396"}]},{"database":"PDB","id":"1PNV","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.80 A"},{"key":"Chains","value":"A/B=1-396"}]},{"database":"PDB","id":"3H4I","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.30 A"},{"key":"Chains","value":"A=1-205"}]},{"database":"PDB","id":"3H4T","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.15 A"},{"key":"Chains","value":"A=1-205"}]},{"database":"AlphaFoldDB","id":"P96558","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P96558","properties":[{"key":"Description","value":"-"}]},{"database":"DrugBank","id":"DB04529","properties":[{"key":"GenericName","value":"Desvancosaminyl vancomycin"}]},{"database":"CAZy","id":"GT1","properties":[{"key":"FamilyName","value":"Glycosyltransferase Family 1"}]},{"database":"KEGG","id":"ag:CAA11774","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.4.1.311","properties":[{"key":"OrganismId","value":"315"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"P96558","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016758","properties":[{"key":"GoTerm","value":"F:hexosyltransferase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15070728"}]},{"database":"GO","id":"GO:0008194","properties":[{"key":"GoTerm","value":"F:UDP-glycosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15070728"}]},{"database":"CDD","id":"cd03784","properties":[{"key":"EntryName","value":"GT1_Gtf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000292","properties":[{"key":"EntryName","value":"Glycosyltransferase GtfE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000009","properties":[{"key":"EntryName","value":"Sterol 3-beta-glucosyltransferase UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR010610","properties":[{"key":"EntryName","value":"EryCIII-like_C"}]},{"database":"InterPro","id":"IPR050426","properties":[{"key":"EntryName","value":"Glycosyltransferase_28"}]},{"database":"InterPro","id":"IPR004276","properties":[{"key":"EntryName","value":"GlycoTrans_28_N"}]},{"database":"InterPro","id":"IPR002213","properties":[{"key":"EntryName","value":"UDP_glucos_trans"}]},{"database":"PANTHER","id":"PTHR48050","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48050:SF13","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06722","properties":[{"key":"EntryName","value":"EryCIII-like_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03033","properties":[{"key":"EntryName","value":"Glyco_transf_28"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVLITGCGSRGDTEPLVALAARLRELGADARMCLPPDYVERCAEVGVPMVPVGRAVRAGAREPGELPPGAAEVVTEVVAEWFDKVPAAIEGCDAVVTTGLLPAAVAVRSMAEKLGIPYRYTVLSPDHLPSEQSQAERDMYNQGADRLFGDAVNSHRASIGLPPVEHLYDYGYTDQPWLAADPVLSPLRPTDLGTVQTGAWILPDERPLSAELEAFLAAGSTPVYVGFGSSSRPATADAAKMAIKAVRASGRRIVLSRGWADLVLPDDGADCFVVGEVNLQELFGRVAAAIHHDSAGTTLLAMRAGIPQIVVRRVVDNVVEQAYHADRVAELGVGVAVDGPVPTIDSLSAALDTALAPEIRARATTVADTIRADGTTVAAQLLFDAVSLEKPTVPA","length":396,"molWeight":41662,"crc64":"A771471559C6CBF5","md5":"0D47E03F6A2B5CDB7E1FD3F4B285227C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":9,"Beta strand":13,"Helix":21,"Turn":2},"uniParcId":"UPI00000AF9B6"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G4V4T6","uniProtkbId":"DPGC_AMYOR","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-12-14","entryVersion":36,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11752437"}],"value":"(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"1.13.11.80"}]}},"genes":[{"geneName":{"value":"dpgC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the unusual conversion 3,5-dihydroxyphenylacetyl-CoA (DPA-CoA) to 3,5-dihydroxyphenylglyoxylate. DpgC performed a net four-electron oxidation of the benzylic carbon of DPA-CoA and the hydrolysis of the thioester bond to generate free CoA. It can also use phenylacetyl-CoA (PA-CoA) as substrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3,5-dihydroxyphenyl)acetyl-CoA + O2 = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44632"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:75210"},{"database":"ChEBI","id":"CHEBI:84554"}],"ecNumber":"1.13.11.80","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":6.0,"unit":"uM","substrate":"DPA-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]},{"constant":300.0,"unit":"uM","substrate":"PA-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"kcat is 10 min(-1) for dioxygenase activity."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"value":"Homohexamer; dimer of trimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the enoyl-CoA hydratase/isomerase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"(3,5-dihydroxyphenyl)acetyl-CoA 1,2-dioxygenase","featureId":"PRO_0000435522"},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q8KLK7"}],"ligand":{"name":"substrate"}}],"keywords":[{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-334RPSRS0J50E","citationType":"submission","authors":["Woertz T.","Dietz S.","Zerbe K.","Robinson J.A."],"title":"The vancomycin biosynthetic gene cluster.","publicationDate":"SEP-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC19795","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"11752437","citationType":"journal article","authors":["Chen H.","Tseng C.C.","Hubbard B.K.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11752437"},{"database":"DOI","id":"10.1073/pnas.221582098"}],"title":"Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.","publicationDate":"2001","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"14901","lastPage":"14906","volume":"98"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"NRRL18098","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HE589771","properties":[{"key":"ProteinId","value":"CCD33161.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"G4V4T6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"G4V4T6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33600","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1024","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"BRENDA","id":"1.13.11.80","properties":[{"key":"OrganismId","value":"315"}]},{"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":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11752437"}]},{"database":"GO","id":"GO:0006635","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06558","properties":[{"key":"EntryName","value":"crotonase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.1300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR053482","properties":[{"key":"EntryName","value":"DPA-CoA_Dioxygenase"}]},{"database":"InterPro","id":"IPR001753","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra/iso"}]},{"database":"NCBIfam","id":"NF042432","properties":[{"key":"EntryName","value":"DHPACoAdixog_DpgC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11941:SF54","properties":[{"key":"EntryName","value":"ENOYL-COA HYDRATASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11941","properties":[{"key":"EntryName","value":"ENOYL-COA HYDRATASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00378","properties":[{"key":"EntryName","value":"ECH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTDSPTLSLSPGLDHRALAKAAQRVDELLDGLPSPSARTPAQREAASSALDEIRAARTEYVEAHAEEIYDRLTDGRTRYLRLDELVRAAASAYPGLVPTEAQMAAERSRRQAEKEGREIDQGIFLRGILSAPKAGPHLLDAMLRPTARALELLPEFVETGVVRMEAASLERRDGVAYLTLCRDDCLNAEDAQQVDDMETAVDLALLDPAVRVGMLRGGVMSHPRYAGRRVFCAGINLKKLSSGDIPLVDFLLRRELGYIHKIVRGVATDGSWRARVIDKPWLAAVDSFAIGGGAQLLLVFDHVVAASDAYFSLPAATEGIIPGAANYRLSRFTGPRLARQVILGGRRITADEPDARLLVDQVVPPEEMDAAIESALAALDGDAVRANRRMVNLAEEPPDGFRRYMAEFALQQALRIYGADVIGKVGGFAAGSR","length":434,"molWeight":47089,"crc64":"6AACB8A601BDED25","md5":"73AB9ACFCFF36F059E6617CFBCF94A77"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":7},"uniParcId":"UPI00022AB46A"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G4V4T7","uniProtkbId":"DPGD_AMYOR","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-12-14","entryVersion":40,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11752437"}],"value":"Enoyl-CoA-hydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"4.2.1.17"}]}},"genes":[{"geneName":{"value":"dpgD"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA thioester, resulting in the formation of a beta-hydroxyacyl-CoA thioester. Physiologically, DpgD could act as a dehydratase, facilitating the aromatization of the DPA-S-DgpA or DPA-S-CoA intermediate. It can use the non physiological substrates crotonyl-CoA and beta-methylcrotonyl-CoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16105"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:58856"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20724"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:137480"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":20.0,"unit":"uM","substrate":"crotonyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]},{"constant":40.0,"unit":"uM","substrate":"beta-methylcrotonyl-CoA","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"kcat is 1.7 min(-1) for enoyl-CoA-hydratase activity."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11752437"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the enoyl-CoA hydratase/isomerase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Enoyl-CoA-hydratase","featureId":"PRO_0000435606"}],"keywords":[{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-334RPSRS0J50E","citationType":"submission","authors":["Woertz T.","Dietz S.","Zerbe K.","Robinson J.A."],"title":"The vancomycin biosynthetic gene cluster.","publicationDate":"SEP-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC19795","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"11752437","citationType":"journal article","authors":["Chen H.","Tseng C.C.","Hubbard B.K.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11752437"},{"database":"DOI","id":"10.1073/pnas.221582098"}],"title":"Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.","publicationDate":"2001","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"14901","lastPage":"14906","volume":"98"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBSTRATE SPECIFICITY"],"referenceComments":[{"value":"NRRL18098","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HE589771","properties":[{"key":"ProteinId","value":"CCD33162.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037311097.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBVIZS010000050.1"}]},{"database":"AlphaFoldDB","id":"G4V4T7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"G4V4T7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33595","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1024","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0018812","properties":[{"key":"GoTerm","value":"F:3-hydroxyacyl-CoA dehydratase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]},{"database":"GO","id":"GO:0004300","properties":[{"key":"GoTerm","value":"F:enoyl-CoA hydratase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11752437"}]},{"database":"GO","id":"GO:0006635","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd06558","properties":[{"key":"EntryName","value":"crotonase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000009","properties":[{"key":"EntryName","value":"Carnitinyl-CoA dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.12.10","properties":[{"key":"EntryName","value":"Lyase 2-enoyl-coa Hydratase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR054898","properties":[{"key":"EntryName","value":"EnCoAhydt_DpgD"}]},{"database":"InterPro","id":"IPR018376","properties":[{"key":"EntryName","value":"Enoyl-CoA_hyd/isom_CS"}]},{"database":"InterPro","id":"IPR001753","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra/iso"}]},{"database":"InterPro","id":"IPR014748","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra_C"}]},{"database":"NCBIfam","id":"NF042430","properties":[{"key":"EntryName","value":"EnCoAhydt_DpgD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11941:SF54","properties":[{"key":"EntryName","value":"ENOYL-COA HYDRATASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11941","properties":[{"key":"EntryName","value":"ENOYL-COA HYDRATASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00378","properties":[{"key":"EntryName","value":"ECH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00166","properties":[{"key":"EntryName","value":"ENOYL_COA_HYDRATASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSETRVRYEKKDHVAYVTMDRPAVLNAMDRRMHEELAGIWDDVEADDDVRAVVLTGAGDRAFSVGQDLKERARLNESGVAPTTFGSGGQAGHPRLTDRFTLSKPVVARVRGYALGGGFELVLACDIVIAAEDAVFALPEVRLGLIAGAGGVFRLPRQLPQKVAMGYLLTGRRMDAATALRHGLVNEVVPAAELDQCVADWTDSLVRAAPLSVRAIKEAALRSVDLPLEEAFTTSYHWEERRRRSADAIEGVRAFAEKRDPIWTGQ","length":265,"molWeight":29008,"crc64":"ED6635B3A8CD0A12","md5":"2D6C4B44C666A611D346F218CF383ED3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00022AB46B"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O52815","uniProtkbId":"HPGT_AMYOR","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-06-01","entryVersion":75,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"(S)-3,5-dihydroxyphenylglycine transaminase"},"ecNumbers":[{"value":"2.6.1.103"}]},"alternativeNames":[{"fullName":{"value":"p-hydroxyphenylglycine transaminase"}}]},"genes":[{"geneName":{"value":"hpgT"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"}],"value":"Catalyzes the transamination of p-hydroxybenzoylformate to L-p-hydroxyphenylglycine as part of the biosynthesis of the (S)-3,5-dihydroxyphenylglycine constituent of the glycopeptide antibiotic chloroeremomycin, a member of the vancomycin group of antibiotics"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-3,5-dihydroxyphenylglycine + 2-oxoglutarate = 2-(3,5-dihydroxyphenyl)-2-oxoacetate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:38347"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:75204"},{"database":"ChEBI","id":"CHEBI:75210"}],"ecNumber":"2.6.1.103","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11137816"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9545426"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the class-I pyridoxal-phosphate-dependent aminotransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"(S)-3,5-dihydroxyphenylglycine transaminase","featureId":"PRO_0000430442"},{"type":"Modified residue","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250"}]}],"keywords":[{"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9545426","citationType":"journal article","authors":["van Wageningen A.","Kirkpatrick P.","Williams D.","Harris B.","Kershaw J.","Lennard N.","Jones M.","Jones S.","Solenberg P."],"citationCrossReferences":[{"database":"PubMed","id":"9545426"},{"database":"DOI","id":"10.1016/s1074-5521(98)90060-6"}],"title":"Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic.","publicationDate":"1998","journal":"Chem. Biol.","firstPage":"155","lastPage":"162","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PATHWAY"]},{"referenceNumber":2,"citation":{"id":"11137816","citationType":"journal article","authors":["Hubbard B.K.","Thomas M.G.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11137816"},{"database":"DOI","id":"10.1016/s1074-5521(00)00043-0"}],"title":"Biosynthesis of L-p-hydroxyphenylglycine, a non-proteinogenic amino acid constituent of peptide antibiotics.","publicationDate":"2000","journal":"Chem. Biol.","firstPage":"931","lastPage":"942","volume":"7"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY","COFACTOR"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AJ223998","properties":[{"key":"ProteinId","value":"CAA11790.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T30600","properties":[{"key":"EntryName","value":"T30600"}]},{"database":"AlphaFoldDB","id":"O52815","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O52815","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33665","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.6.1.B17","properties":[{"key":"OrganismId","value":"315"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008483","properties":[{"key":"GoTerm","value":"F:transaminase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11137816"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11137816"}]},{"database":"CDD","id":"cd00609","properties":[{"key":"EntryName","value":"AAT_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000305","properties":[{"key":"EntryName","value":"(S)-3,5-dihydroxyphenylglycine transaminase"},{"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":"IPR004839","properties":[{"key":"EntryName","value":"Aminotransferase_I/II_large"}]},{"database":"InterPro","id":"IPR050859","properties":[{"key":"EntryName","value":"Class-I_PLP-dep_aminotransf"}]},{"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":"PANTHER","id":"PTHR42790","properties":[{"key":"EntryName","value":"AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42790:SF19","properties":[{"key":"EntryName","value":"KYNURENINE_ALPHA-AMINOADIPATE AMINOTRANSFERASE, MITOCHONDRIAL"},{"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"}]}],"sequence":{"value":"MEILVFMDSYGLSTQLSMETLHGSLTDPAISSMNLLNELIDEYPVAISMAAGRPYEEFFDVRLIHEYIDAYCDHLRHDRKLAEAVVTRTLFQYGTTKGIIADLIARNLAEDENIDAAAESVVVTVGAQEAMFLILRTLRADERDVLLAPAPTYVGLTGAALLTDTPVWPVQSTANGVDPEDLVLQLKRADEQGKRVRACYVTPNFANPTGTSMDLPARHRLLEVAEANGILLLEDNAYGLFGSERLPSLKSLDRSGNVVYIGSFAKTGMPGARVGYVVADQRVAGGGLLADQLSKLKGMLTVNTSPIAQAVIAGKLLLNDFSLTKANAREIAIYQRNLQLTLSELERTLGGLPEVGWNTPTGGFFVTVTVPFVVDDELLAHAARDHGVLFTPMHHFYGGKDGFNQLRLSISLLTPELIKEGVTRLAALITARLRWPRA","length":438,"molWeight":47777,"crc64":"AD4C89C8B6938BF7","md5":"E4A199B8961B9BEA8A2E1CDAD9E4482A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Modified residue":1},"uniParcId":"UPI00000BB622"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8RN04","uniProtkbId":"C5B3_AMYOR","entryAudit":{"firstPublicDate":"2003-09-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2002-06-01","entryVersion":89,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAL90878.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Cytochrome P450 165B3"},"ecNumbers":[{"value":"1.14.-.-"}]},"alternativeNames":[{"fullName":{"value":"Vancomycin biosynthesis protein OxyB"}}]},"genes":[{"geneName":{"value":"cyp165B3"},"synonyms":[{"value":"oxyB"}]}],"comments":[{"texts":[{"value":"Involved in the coupling of aromatic side chains of the heptapeptide of vancomycin"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme","cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the cytochrome P450 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Cytochrome P450 165B3","featureId":"PRO_0000052239"},{"type":"Binding site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Helix","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Turn","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LG9"}]},{"type":"Beta strand","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Turn","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Turn","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Turn","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Helix","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]},{"type":"Beta strand","location":{"start":{"value":395,"modifier":"EXACT"},"end":{"value":397,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1LFK"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"12207020","citationType":"journal article","authors":["Zerbe K.","Pylypenko O.","Vitali F.","Zhang W.","Rousett S.","Heck M.","Vrijbloed J.W.","Bischoff D.","Bister B.","Suessmuth R.D.","Pelzer S.","Wohlleben W.","Robinson J.A.","Schlichting I."],"citationCrossReferences":[{"database":"PubMed","id":"12207020"},{"database":"DOI","id":"10.1074/jbc.m206342200"}],"title":"Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis.","publicationDate":"2002","journal":"J. Biol. Chem.","firstPage":"47476","lastPage":"47485","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","X-RAY CRYSTALLOGRAPHY"],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF486630","properties":[{"key":"ProteinId","value":"AAL90878.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"1LFK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.70 A"},{"key":"Chains","value":"A=1-398"}]},{"database":"PDB","id":"1LG9","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.00 A"},{"key":"Chains","value":"A=1-398"}]},{"database":"PDB","id":"1LGF","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.20 A"},{"key":"Chains","value":"A=1-398"}]},{"database":"AlphaFoldDB","id":"Q8RN04","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8RN04","properties":[{"key":"Description","value":"-"}]},{"database":"DIP","id":"DIP-61594N","properties":[{"key":"Description","value":"-"}]},{"database":"IntAct","id":"Q8RN04","properties":[{"key":"Interactions","value":"2"}]},{"database":"STRING","id":"31958.SD37_33705","properties":[{"key":"Description","value":"-"}]},{"database":"BindingDB","id":"Q8RN04","properties":[{"key":"Description","value":"-"}]},{"database":"ChEMBL","id":"CHEMBL1075039","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG2124","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q8RN04","properties":[{"key":"Description","value":"-"}]},{"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:0004497","properties":[{"key":"GoTerm","value":"F:monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016705","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd11030","properties":[{"key":"EntryName","value":"CYP105-like"},{"key":"MatchStatus","value":"1"}]},{"database":"DisProt","id":"DP04035","properties":[{"key":"Description","value":"-"}]},{"database":"FunFam","id":"1.10.630.10:FF:000018","properties":[{"key":"EntryName","value":"Cytochrome P450 monooxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.630.10","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001128","properties":[{"key":"EntryName","value":"Cyt_P450"}]},{"database":"InterPro","id":"IPR002397","properties":[{"key":"EntryName","value":"Cyt_P450_B"}]},{"database":"InterPro","id":"IPR017972","properties":[{"key":"EntryName","value":"Cyt_P450_CS"}]},{"database":"InterPro","id":"IPR036396","properties":[{"key":"EntryName","value":"Cyt_P450_sf"}]},{"database":"PANTHER","id":"PTHR46696","properties":[{"key":"EntryName","value":"P450, PUTATIVE (EUROFUNG)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46696:SF6","properties":[{"key":"EntryName","value":"P450, PUTATIVE (EUROFUNG)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00067","properties":[{"key":"EntryName","value":"p450"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00359","properties":[{"key":"EntryName","value":"BP450"}]},{"database":"SUPFAM","id":"SSF48264","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00086","properties":[{"key":"EntryName","value":"CYTOCHROME_P450"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEDDPRPLHIRRQGLDPADELLAAGALTRVTIGSGADAETHWMATAHAVVRQVMGDHQQFSTRRRWDPRDEIGGKGIFRPRELVGNLMDYDPPEHTRLRRKLTPGFTLRKMQRMAPYIEQIVNDRLDEMERAGSPADLIAFVADKVPGAVLCELVGVPRDDRDMFMKLCHGHLDASLSQKRRAALGDKFSRYLLAMIARERKEPGEGMIGAVVAEYGDDATDEELRGFCVQVMLAGDDNISGMIGLGVLAMLRHPEQIDAFRGDEQSAQRAVDELIRYLTVPYSPTPRIAREDLTLAGQEIKKGDSVICSLPAANRDPALAPDVDRLDVTREPIPHVAFGHGVHHCLGAALARLELRTVFTELWRRFPALRLADPAQDTEFRLTTPAYGLTELMVAW","length":398,"molWeight":44367,"crc64":"F91FEA7FB0E91783","md5":"7790AF4FBD7837A2FD3170EAA85CAFDD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":1,"Helix":20,"Beta strand":13,"Turn":4},"uniParcId":"UPI00000BEFD2"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"G4V4T5","uniProtkbId":"DPGB_AMYOR","entryAudit":{"firstPublicDate":"2016-02-17","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2011-12-14","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"11752437"}],"value":"Enoyl-CoA-hydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"4.2.1.17"}]}},"genes":[{"geneName":{"value":"dpgB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}],"value":"Involved in the biosynthesis of the nonproteinogenic amino acid monomer (S)-3,5-dihydroxyphenylglycine (Dpg) responsible of the production of vancomycin and teicoplanin antibiotics. Catalyzes the syn-addition of a water molecule across the double bond of a trans-2-enoyl-CoA thioester, resulting in the formation of a beta-hydroxyacyl-CoA thioester. Physiologically, DpgB could act as a dehydratase, facilitating the aromatization of the DPA-S-DgpA or DPA-S-CoA intermediate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16105"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:58856"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20724"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:137480"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11752437"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the enoyl-CoA hydratase/isomerase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Enoyl-CoA-hydratase","featureId":"PRO_0000435605"}],"keywords":[{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-334RPSRS0J50E","citationType":"submission","authors":["Woertz T.","Dietz S.","Zerbe K.","Robinson J.A."],"title":"The vancomycin biosynthetic gene cluster.","publicationDate":"SEP-2011","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC19795","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"11752437","citationType":"journal article","authors":["Chen H.","Tseng C.C.","Hubbard B.K.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11752437"},{"database":"DOI","id":"10.1073/pnas.221582098"}],"title":"Glycopeptide antibiotic biosynthesis: enzymatic assembly of the dedicated amino acid monomer (S)-3,5-dihydroxyphenylglycine.","publicationDate":"2001","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"14901","lastPage":"14906","volume":"98"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY"],"referenceComments":[{"value":"NRRL18098","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"HE589771","properties":[{"key":"ProteinId","value":"CCD33160.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"G4V4T5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"G4V4T5","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33605","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1024","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0018812","properties":[{"key":"GoTerm","value":"F:3-hydroxyacyl-CoA dehydratase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11752437"}]},{"database":"GO","id":"GO:0004300","properties":[{"key":"GoTerm","value":"F:enoyl-CoA hydratase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11752437"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR053545","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydratase-like"}]},{"database":"NCBIfam","id":"NF042431","properties":[{"key":"EntryName","value":"EnCoAhydt_DpgB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43459:SF1","properties":[{"key":"EntryName","value":"EG:BACN32G11.4 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43459","properties":[{"key":"EntryName","value":"ENOYL-COA HYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNGELVLRLDGARPLSPASVEELSALCDRAEDDREAGPVTVHVTGVPSAGWTAGLTVGLVSKWERVVRRFERLGRLTIAVASGECAGTALDLLLAADLRIVTPGTRLRLAPVGGSTWPGMSVYRLTQQAGAAGIRRAVLLGTPIEVDRALALNLVDEVSDDPAKTLAGLAEAAAALDGAETAIRRQLIFEDGSTTFEDALGAHLAAADRALRREATS","length":217,"molWeight":22686,"crc64":"D6EDD164011B98CB","md5":"0046DD7A87E2A18D215590BA41D69615"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00022AB469"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P96559","uniProtkbId":"GTFB_AMYOR","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1997-05-01","entryVersion":93,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Vancomycin aglycone glucosyltransferase"},"ecNumbers":[{"value":"2.4.1.310"}]},"alternativeNames":[{"fullName":{"value":"Glycosyltransferase GtfB"}}]},"genes":[{"geneName":{"value":"gtfB"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9115410"}],"value":"Glucosyltransferase that transfers glucose to the 4-OH-Phegly(4) residue of vancomycin aglycone (AGV) to produce devancoaminyl-vancomycin (DVV) in the biosynthesis of glycopeptide antibiotic chloroeremomycin, a member of the vancomycin group of antibiotics"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"vancomycin aglycone + UDP-alpha-D-glucose = devancoaminyl-vancomycin + UDP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:38587"},{"database":"ChEBI","id":"CHEBI:58223"},{"database":"ChEBI","id":"CHEBI:58885"},{"database":"ChEBI","id":"CHEBI:75953"},{"database":"ChEBI","id":"CHEBI:77981"}],"ecNumber":"2.4.1.310","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11470430"}]}},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":1.3,"unit":"mM","substrate":"UDP-glucose","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11470430"}]}],"note":{"texts":[{"value":"kcat is 33 min(-1)."}]}}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9545426"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"value":"In A.orientalis different glycosyltransferases are involved in biosynthesis of the vancomycin group of antibiotics. GtfA (AC P96558), GtfB and GtfC (AC P96560) are involved in biosynthesis of antibiotic chloroeremomycin, while GtfD (AC Q9AFC7) and GtfE (AC G4V4R9) are involved in biosynthesis of vancomycin"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyltransferase 28 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Vancomycin aglycone glucosyltransferase","featureId":"PRO_0000430437"},{"type":"Mutagenesis","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Decreased kcat, while it does not affect the KM for UDP-glucose.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11470430"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"No decrease in catalytic rate.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11470430"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Strongly decreased activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11470430"}],"alternativeSequence":{"originalSequence":"D","alternativeSequences":["A"]}},{"type":"Beta strand","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Turn","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Turn","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Beta strand","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]},{"type":"Helix","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1IIR"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9115410","citationType":"journal article","authors":["Solenberg P.J.","Matsushima P.","Stack D.R.","Wilkie S.C.","Thompson R.C.","Baltz R.H."],"citationCrossReferences":[{"database":"PubMed","id":"9115410"},{"database":"DOI","id":"10.1016/s1074-5521(97)90288-x"}],"title":"Production of hybrid glycopeptide antibiotics in vitro and in Streptomyces toyocaensis.","publicationDate":"1997","journal":"Chem. Biol.","firstPage":"195","lastPage":"202","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION"]},{"referenceNumber":2,"citation":{"id":"9545426","citationType":"journal article","authors":["van Wageningen A.","Kirkpatrick P.","Williams D.","Harris B.","Kershaw J.","Lennard N.","Jones M.","Jones S.","Solenberg P."],"citationCrossReferences":[{"database":"PubMed","id":"9545426"},{"database":"DOI","id":"10.1016/s1074-5521(98)90060-6"}],"title":"Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic.","publicationDate":"1998","journal":"Chem. Biol.","firstPage":"155","lastPage":"162","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PATHWAY"]},{"referenceNumber":3,"citation":{"id":"11294642","citationType":"journal article","authors":["Losey H.C.","Peczuh M.W.","Chen Z.","Eggert U.S.","Dong S.D.","Pelczer I.","Kahne D.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11294642"},{"database":"DOI","id":"10.1021/bi010050w"}],"title":"Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides.","publicationDate":"2001","journal":"Biochemistry","firstPage":"4745","lastPage":"4755","volume":"40"},"referencePositions":["FUNCTION"]},{"referenceNumber":4,"citation":{"id":"11470430","citationType":"journal article","authors":["Mulichak A.M.","Losey H.C.","Walsh C.T.","Garavito R.M."],"citationCrossReferences":[{"database":"PubMed","id":"11470430"},{"database":"DOI","id":"10.1016/s0969-2126(01)00616-5"}],"title":"Structure of the UDP-glucosyltransferase GtfB that modifies the heptapeptide aglycone in the biosynthesis of vancomycin group antibiotics.","publicationDate":"2001","journal":"Structure","firstPage":"547","lastPage":"557","volume":"9"},"referencePositions":["X-RAY CRYSTALLOGRAPHY","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","MUTAGENESIS OF ASP-13; HIS-125 AND ASP-332"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U84349","properties":[{"key":"ProteinId","value":"AAB49293.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AJ223998","properties":[{"key":"ProteinId","value":"CAA11775.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T30585","properties":[{"key":"EntryName","value":"T30585"}]},{"database":"PDB","id":"1IIR","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A=1-407"}]},{"database":"AlphaFoldDB","id":"P96559","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P96559","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GT1","properties":[{"key":"FamilyName","value":"Glycosyltransferase Family 1"}]},{"database":"KEGG","id":"ag:CAA11775","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.4.1.310","properties":[{"key":"OrganismId","value":"315"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"P96559","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016758","properties":[{"key":"GoTerm","value":"F:hexosyltransferase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11470430"}]},{"database":"GO","id":"GO:0008194","properties":[{"key":"GoTerm","value":"F:UDP-glycosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11470430"}]},{"database":"CDD","id":"cd03784","properties":[{"key":"EntryName","value":"GT1_Gtf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000292","properties":[{"key":"EntryName","value":"Glycosyltransferase GtfE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000009","properties":[{"key":"EntryName","value":"Sterol 3-beta-glucosyltransferase UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR010610","properties":[{"key":"EntryName","value":"EryCIII-like_C"}]},{"database":"InterPro","id":"IPR050426","properties":[{"key":"EntryName","value":"Glycosyltransferase_28"}]},{"database":"InterPro","id":"IPR004276","properties":[{"key":"EntryName","value":"GlycoTrans_28_N"}]},{"database":"InterPro","id":"IPR002213","properties":[{"key":"EntryName","value":"UDP_glucos_trans"}]},{"database":"PANTHER","id":"PTHR48050","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48050:SF13","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06722","properties":[{"key":"EntryName","value":"EryCIII-like_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03033","properties":[{"key":"EntryName","value":"Glyco_transf_28"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVLLATCGSRGDTEPLVALAVRVRDLGADVRMCAPPDCAERLAEVGVPHVPVGPSARAPIQRAKPLTAEDVRRFTTEAIATQFDEIPAAAEGCAAVVTTGLLAAAIGVRSVAEKLGIPYFYAFHCPSYVPSPYYPPPPLGEPSTQDTIDIPAQWERNNQSAYQRYGGLLNSHRDAIGLPPVEDIFTFGYTDHPWVAADPVLAPLQPTDLDAVQTGAWILPDERPLSPELAAFLDAGPPPVYLGFGSLGAPADAVRVAIDAIRAHGRRVILSRGWADLVLPDDGADCFAIGEVNHQVLFGRVAAVIHHGGAGTTHVAARAGAPQILLPQMADQPYYAGRVAELGVGVAHDGPIPTFDSLSAALATALTPETHARATAVAGTIRTDGAAVAARLLLDAVSREKPTVSA","length":407,"molWeight":42666,"crc64":"DDCC0CF29A311201","md5":"56913B6874AA29BA959FE455B41A290C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Mutagenesis":3,"Beta strand":13,"Helix":22,"Turn":2},"uniParcId":"UPI00000BE191"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P96560","uniProtkbId":"GTFC_AMYOR","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"1997-05-01","entryVersion":73,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Glycosyltransferase GtfC"},"ecNumbers":[{"value":"2.4.1.-"}]}},"genes":[{"geneName":{"value":"gtfC"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15070728"}],"value":"Catalyzes the attachment of dTDP-L-4-epi-vancosamine to chloroorienticin B to form chloroeremomycin in the biosynthesis of glycopeptide antibiotic chloroeremomycin, a member of the vancomycin group of antibiotics. Also able to use dTDP-L-4-epi-vancosamine and devancoaminyl-vancomycin (DVV) to create epivancomycin. Acts downstream of GtfA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dTDP-beta-L-vancosamine + devancoaminyl-vancomycin = epivancomycin + dTDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45904"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58369"},{"database":"ChEBI","id":"CHEBI:75953"},{"database":"ChEBI","id":"CHEBI:76839"},{"database":"ChEBI","id":"CHEBI:85491"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15070728"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"chloroorienticin B + dTDP-beta-L-vancosamine = chloroeremomycin + dTDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45908"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58369"},{"database":"ChEBI","id":"CHEBI:75963"},{"database":"ChEBI","id":"CHEBI:76839"},{"database":"ChEBI","id":"CHEBI:85488"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15070728"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9545426"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"value":"In A.orientalis different glycosyltransferases are involved in biosynthesis of the vancomycin group of antibiotics. GtfA (AC P96558), GtfB (AC P96559) and GtfC are involved in biosynthesis of antibiotic chloroeremomycin, while GtfD (AC Q9AFC7) and GtfE (AC G4V4R9) are involved in biosynthesis of vancomycin"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyltransferase 28 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Glycosyltransferase GtfC","featureId":"PRO_0000430438"}],"keywords":[{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9115410","citationType":"journal article","authors":["Solenberg P.J.","Matsushima P.","Stack D.R.","Wilkie S.C.","Thompson R.C.","Baltz R.H."],"citationCrossReferences":[{"database":"PubMed","id":"9115410"},{"database":"DOI","id":"10.1016/s1074-5521(97)90288-x"}],"title":"Production of hybrid glycopeptide antibiotics in vitro and in Streptomyces toyocaensis.","publicationDate":"1997","journal":"Chem. Biol.","firstPage":"195","lastPage":"202","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]},{"referenceNumber":2,"citation":{"id":"9545426","citationType":"journal article","authors":["van Wageningen A.","Kirkpatrick P.","Williams D.","Harris B.","Kershaw J.","Lennard N.","Jones M.","Jones S.","Solenberg P."],"citationCrossReferences":[{"database":"PubMed","id":"9545426"},{"database":"DOI","id":"10.1016/s1074-5521(98)90060-6"}],"title":"Sequencing and analysis of genes involved in the biosynthesis of a vancomycin group antibiotic.","publicationDate":"1998","journal":"Chem. Biol.","firstPage":"155","lastPage":"162","volume":"5"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PATHWAY"]},{"referenceNumber":3,"citation":{"id":"11294642","citationType":"journal article","authors":["Losey H.C.","Peczuh M.W.","Chen Z.","Eggert U.S.","Dong S.D.","Pelczer I.","Kahne D.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11294642"},{"database":"DOI","id":"10.1021/bi010050w"}],"title":"Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides.","publicationDate":"2001","journal":"Biochemistry","firstPage":"4745","lastPage":"4755","volume":"40"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY"]},{"referenceNumber":4,"citation":{"id":"15070728","citationType":"journal article","authors":["Lu W.","Oberthuer M.","Leimkuhler C.","Tao J.","Kahne D.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"15070728"},{"database":"DOI","id":"10.1073/pnas.0400277101"}],"title":"Characterization of a regiospecific epivancosaminyl transferase GtfA and enzymatic reconstitution of the antibiotic chloroeremomycin.","publicationDate":"2004","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"4390","lastPage":"4395","volume":"101"},"referencePositions":["FUNCTION","CATALYTIC ACTIVITY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U84349","properties":[{"key":"ProteinId","value":"AAB49294.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AJ223998","properties":[{"key":"ProteinId","value":"CAA11776.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"T30586","properties":[{"key":"EntryName","value":"T30586"}]},{"database":"AlphaFoldDB","id":"P96560","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P96560","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GT1","properties":[{"key":"FamilyName","value":"Glycosyltransferase Family 1"}]},{"database":"KEGG","id":"ag:CAA11776","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0016758","properties":[{"key":"GoTerm","value":"F:hexosyltransferase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15070728"}]},{"database":"GO","id":"GO:0008194","properties":[{"key":"GoTerm","value":"F:UDP-glycosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000314","source":"PubMed","id":"15070728"}]},{"database":"CDD","id":"cd03784","properties":[{"key":"EntryName","value":"GT1_Gtf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000292","properties":[{"key":"EntryName","value":"Glycosyltransferase GtfE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000009","properties":[{"key":"EntryName","value":"Sterol 3-beta-glucosyltransferase UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR010610","properties":[{"key":"EntryName","value":"EryCIII-like_C"}]},{"database":"InterPro","id":"IPR050426","properties":[{"key":"EntryName","value":"Glycosyltransferase_28"}]},{"database":"InterPro","id":"IPR004276","properties":[{"key":"EntryName","value":"GlycoTrans_28_N"}]},{"database":"InterPro","id":"IPR002213","properties":[{"key":"EntryName","value":"UDP_glucos_trans"}]},{"database":"PANTHER","id":"PTHR48050","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48050:SF13","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06722","properties":[{"key":"EntryName","value":"EryCIII-like_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03033","properties":[{"key":"EntryName","value":"Glyco_transf_28"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVLLSTAGSRGDVEPLVALAVRLQGLGVEARMCASPASAERLAEVGVPHVPVGLQLEGMLLQEGMPPPSPEEERRLAAKAIDMQFDEVPAAAEGCAAVVAAGELAAAAAVRSVAEMLGIPYFYAAYSPNYLPSPHHAPPEDERTTPGVTDNKVLWDERGQRFAKRYGDTLNSRRASVGLPPVEDVFGYGYSERPWLATDPILAPLPPDFDAVQTGTWILPDERPLSAELEAFLAAGSPPVYLGFGSASGPGIDDAARVAIEAIRAHGRRIVLLSGWADLVRPDDGADCFSVDEVNLQVLFSRAAAAIHHGSAGTEHLATLAGIPQIVIPRHTDQPYYAERVADLGIGVALEGPVPTFDAMSAAVATALAPETRARATAVAGTIRTDGAAVAARLLLDAVSREKSAVLA","length":409,"molWeight":42920,"crc64":"3244092F8E26F82B","md5":"52EB92A23A382250FC07EAE54B38E0CC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00000BE537"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8RN03","uniProtkbId":"C5C4_AMYOR","entryAudit":{"firstPublicDate":"2003-09-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2002-06-01","entryVersion":89,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAL90879.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Cytochrome P450 165C4"},"ecNumbers":[{"value":"1.14.-.-"}]},"alternativeNames":[{"fullName":{"value":"Vancomycin biosynthesis protein OxyC"}}]},"genes":[{"geneName":{"value":"cyp165C4"},"synonyms":[{"value":"oxyC"}]}],"comments":[{"texts":[{"value":"Involved in the coupling of aromatic side chains of the heptapeptide of vancomycin"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12888556"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the cytochrome P450 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"Cytochrome P450 165C4","featureId":"PRO_0000052240"},{"type":"Binding site","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"12888556"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"1UED"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Beta strand","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Turn","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":263,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Turn","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Helix","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]},{"type":"Beta strand","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1UED"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"12207020","citationType":"journal article","authors":["Zerbe K.","Pylypenko O.","Vitali F.","Zhang W.","Rousett S.","Heck M.","Vrijbloed J.W.","Bischoff D.","Bister B.","Suessmuth R.D.","Pelzer S.","Wohlleben W.","Robinson J.A.","Schlichting I."],"citationCrossReferences":[{"database":"PubMed","id":"12207020"},{"database":"DOI","id":"10.1074/jbc.m206342200"}],"title":"Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis.","publicationDate":"2002","journal":"J. Biol. Chem.","firstPage":"47476","lastPage":"47485","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000305"}]},{"referenceNumber":2,"citation":{"id":"12888556","citationType":"journal article","authors":["Pylypenko O.","Vitali F.","Zerbe K.","Robinson J.A.","Schlichting I."],"citationCrossReferences":[{"database":"PubMed","id":"12888556"},{"database":"DOI","id":"10.1074/jbc.m306486200"}],"title":"Crystal structure of OxyC, a cytochrome P450 implicated in an oxidative C-C coupling reaction during vancomycin biosynthesis.","publicationDate":"2003","journal":"J. Biol. Chem.","firstPage":"46727","lastPage":"46733","volume":"278"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH HEME"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF486630","properties":[{"key":"ProteinId","value":"AAL90879.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"1UED","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.90 A"},{"key":"Chains","value":"A/B=1-406"}]},{"database":"AlphaFoldDB","id":"Q8RN03","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8RN03","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33700","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG2124","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q8RN03","properties":[{"key":"Description","value":"-"}]},{"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:0004497","properties":[{"key":"GoTerm","value":"F:monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016705","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd11030","properties":[{"key":"EntryName","value":"CYP105-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.630.10:FF:000018","properties":[{"key":"EntryName","value":"Cytochrome P450 monooxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.630.10","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001128","properties":[{"key":"EntryName","value":"Cyt_P450"}]},{"database":"InterPro","id":"IPR002397","properties":[{"key":"EntryName","value":"Cyt_P450_B"}]},{"database":"InterPro","id":"IPR017972","properties":[{"key":"EntryName","value":"Cyt_P450_CS"}]},{"database":"InterPro","id":"IPR036396","properties":[{"key":"EntryName","value":"Cyt_P450_sf"}]},{"database":"PANTHER","id":"PTHR46696","properties":[{"key":"EntryName","value":"P450, PUTATIVE (EUROFUNG)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46696:SF6","properties":[{"key":"EntryName","value":"P450, PUTATIVE (EUROFUNG)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00067","properties":[{"key":"EntryName","value":"p450"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00359","properties":[{"key":"EntryName","value":"BP450"}]},{"database":"SUPFAM","id":"SSF48264","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00086","properties":[{"key":"EntryName","value":"CYTOCHROME_P450"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGHDIDQVAPLLREPANFQLRTNCDPHEDNFGLRAHGPLVRIVGESSTQLGRDFVWQAHGYEVVRRILGDHEHFTTRPQFTQSKSGAHVEAQFVGQISTYDPPEHTRLRKMLTPEFTVRRIRRMEPAIQSLIDDRLDLLEAEGPSADLQGLFADPVGAHALCELLGIPRDDQREFVRRIRRNADLSRGLKARAADSAAFNRYLDNLLARQRADPDDGLLGMIVRDHGDNVTDEELKGLCTALILGGVETVAGMIGFGVLALLDNPGQIELLFESPEKAERVVNELVRYLSPVQAPNPRLAIKDVVIDGQLIKAGDYVLCSILMANRDEALTPDPDVLDANRAAVSDVGFGHGIHYCVGAALARSMLRMAYQTLWRRFPGLRLAVPIEEVKYRSAFVDCPDQVPVTW","length":406,"molWeight":45187,"crc64":"6C0E2EFA167A747A","md5":"080E5E7F2E0F0A4F1DA4BCEBEDE28473"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":1,"Beta strand":12,"Turn":2,"Helix":21},"uniParcId":"UPI00000BEFD4"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8RN05","uniProtkbId":"C5A3_AMYOR","entryAudit":{"firstPublicDate":"2003-09-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2002-06-01","entryVersion":76,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"AAL90877.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Cytochrome P450 165A3"},"ecNumbers":[{"value":"1.14.-.-"}]},"alternativeNames":[{"fullName":{"value":"Vancomycin biosynthesis protein OxyA"}}]},"genes":[{"geneName":{"value":"cyp165A3"},"synonyms":[{"value":"oxyA"}]}],"comments":[{"texts":[{"value":"Involved in the coupling of aromatic side chains of the heptapeptide of vancomycin"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:30413"}}]},{"texts":[{"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the cytochrome P450 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"Cytochrome P450 165A3","featureId":"PRO_0000052238"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"keywords":[{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0503","category":"Molecular function","name":"Monooxygenase"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"12207020","citationType":"journal article","authors":["Zerbe K.","Pylypenko O.","Vitali F.","Zhang W.","Rousett S.","Heck M.","Vrijbloed J.W.","Bischoff D.","Bister B.","Suessmuth R.D.","Pelzer S.","Wohlleben W.","Robinson J.A.","Schlichting I."],"citationCrossReferences":[{"database":"PubMed","id":"12207020"},{"database":"DOI","id":"10.1074/jbc.m206342200"}],"title":"Crystal structure of OxyB, a cytochrome P450 implicated in an oxidative phenol coupling reaction during vancomycin biosynthesis.","publicationDate":"2002","journal":"J. Biol. Chem.","firstPage":"47476","lastPage":"47485","volume":"277"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"evidences":[{"evidenceCode":"ECO:0000305"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF486630","properties":[{"key":"ProteinId","value":"AAL90877.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q8RN05","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8RN05","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33710","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG2124","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"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:0004497","properties":[{"key":"GoTerm","value":"F:monooxygenase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016705","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd11030","properties":[{"key":"EntryName","value":"CYP105-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.630.10:FF:000018","properties":[{"key":"EntryName","value":"Cytochrome P450 monooxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.630.10","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001128","properties":[{"key":"EntryName","value":"Cyt_P450"}]},{"database":"InterPro","id":"IPR002397","properties":[{"key":"EntryName","value":"Cyt_P450_B"}]},{"database":"InterPro","id":"IPR017972","properties":[{"key":"EntryName","value":"Cyt_P450_CS"}]},{"database":"InterPro","id":"IPR036396","properties":[{"key":"EntryName","value":"Cyt_P450_sf"}]},{"database":"PANTHER","id":"PTHR46696:SF1","properties":[{"key":"EntryName","value":"CYTOCHROME P450 YJIB-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46696","properties":[{"key":"EntryName","value":"P450, PUTATIVE (EUROFUNG)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00067","properties":[{"key":"EntryName","value":"p450"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00359","properties":[{"key":"EntryName","value":"BP450"}]},{"database":"SUPFAM","id":"SSF48264","properties":[{"key":"EntryName","value":"Cytochrome P450"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00086","properties":[{"key":"EntryName","value":"CYTOCHROME_P450"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFEEKNALRGTEIHRRERFDPGPELRALMAEGRMSVMESEESPGGRTGWLATGYEETRQVLGSDKFSAKLLFGGTAAGRIWPGFLNQYDPPEHTRLRRMVASAFTVRRMRDFRPRIEAVVKATLDDIEATGGPVDFVPRFAWPIATTVICDFLGIPRDDQAELSRVLHASRSERSGKRRVAAGNKYWTYMGQVAAKTRRDPGDDMFGAVVREHGDDITDAELLGVAAFVMGASGDQVARFLSAGAWLMVEHPEQFAVLRDDPDSVPDWLNEVARYLTSDEKTTPRIALEDVRIGDQLVKKGDAVTCSLLASNRHRFPDPEDRFDITREKPSHVTFGHGIHHCLGRPLAEMVFRTAIPALAHRFPTLRLAEPDREIKLGPPPFDVEALLLDW","length":391,"molWeight":43829,"crc64":"CA62DA0611E03EE4","md5":"C489109CD7A203553CC86AD515F88A11"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Region":1,"Compositional bias":1,"Binding site":1},"uniParcId":"UPI00000BEFD3"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9AFC6","uniProtkbId":"GTFE_AMYOR","entryAudit":{"firstPublicDate":"2014-10-01","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2001-06-01","entryVersion":59,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Glycosyltransferase GtfE"},"ecNumbers":[{"value":"2.4.1.-"}]}},"genes":[{"geneName":{"value":"gtfE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9115410"}],"value":"D-glucosyltransferase that acts on the aglycone core, transferring D-glucose to the phenolic hydroxyl of OH-Phegly(4) to form a devancoaminyl-vancomycin (DVV) intermediate in the biosynthesis of glycopeptide antibiotic vancomycin. Also able to glycosylate A47934, an antibiotic with a teicoplanin-like heptapeptide, but lacking sugar residues"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11294642"}],"value":"Antibiotic biosynthesis; vancomycin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"value":"In A.orientalis different glycosyltransferases are involved in biosynthesis of the vancomycin group of antibiotics. GtfA (AC P96558), GtfB (AC P96559) and GtfC (AC P96560) are involved in biosynthesis of antibiotic chloroeremomycin, while GtfD (AC Q9AFC7) and GtfE are involved in biosynthesis of vancomycin"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyltransferase 28 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Glycosyltransferase GtfE","featureId":"PRO_0000430440"}],"keywords":[{"id":"KW-0045","category":"Biological process","name":"Antibiotic biosynthesis"},{"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"11294642","citationType":"journal article","authors":["Losey H.C.","Peczuh M.W.","Chen Z.","Eggert U.S.","Dong S.D.","Pelczer I.","Kahne D.","Walsh C.T."],"citationCrossReferences":[{"database":"PubMed","id":"11294642"},{"database":"DOI","id":"10.1021/bi010050w"}],"title":"Tandem action of glycosyltransferases in the maturation of vancomycin and teicoplanin aglycones: novel glycopeptides.","publicationDate":"2001","journal":"Biochemistry","firstPage":"4745","lastPage":"4755","volume":"40"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","PATHWAY"],"referenceComments":[{"value":"ATCC 19795 / DSM 40040 / CBS 547.68 / JCM 4235 / KCTC 9412 / NBRC 12806 / NCIMB 12945 / M43-05865","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"9115410","citationType":"journal article","authors":["Solenberg P.J.","Matsushima P.","Stack D.R.","Wilkie S.C.","Thompson R.C.","Baltz R.H."],"citationCrossReferences":[{"database":"PubMed","id":"9115410"},{"database":"DOI","id":"10.1016/s1074-5521(97)90288-x"}],"title":"Production of hybrid glycopeptide antibiotics in vitro and in Streptomyces toyocaensis.","publicationDate":"1997","journal":"Chem. Biol.","firstPage":"195","lastPage":"202","volume":"4"},"referencePositions":["FUNCTION"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF351622","properties":[{"key":"ProteinId","value":"AAK31353.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9AFC6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9AFC6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_33685","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"GT1","properties":[{"key":"FamilyName","value":"Glycosyltransferase Family 1"}]},{"database":"eggNOG","id":"COG1819","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00162","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0016758","properties":[{"key":"GoTerm","value":"F:hexosyltransferase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11294642"}]},{"database":"GO","id":"GO:0008194","properties":[{"key":"GoTerm","value":"F:UDP-glycosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033072","properties":[{"key":"GoTerm","value":"P:vancomycin biosynthetic process"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"11294642"}]},{"database":"CDD","id":"cd03784","properties":[{"key":"EntryName","value":"GT1_Gtf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000292","properties":[{"key":"EntryName","value":"Glycosyltransferase GtfE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2000:FF:000009","properties":[{"key":"EntryName","value":"Sterol 3-beta-glucosyltransferase UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR010610","properties":[{"key":"EntryName","value":"EryCIII-like_C"}]},{"database":"InterPro","id":"IPR050426","properties":[{"key":"EntryName","value":"Glycosyltransferase_28"}]},{"database":"InterPro","id":"IPR004276","properties":[{"key":"EntryName","value":"GlycoTrans_28_N"}]},{"database":"InterPro","id":"IPR002213","properties":[{"key":"EntryName","value":"UDP_glucos_trans"}]},{"database":"PANTHER","id":"PTHR48050","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48050:SF13","properties":[{"key":"EntryName","value":"STEROL 3-BETA-GLUCOSYLTRANSFERASE UGT80A2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06722","properties":[{"key":"EntryName","value":"EryCIII-like_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03033","properties":[{"key":"EntryName","value":"Glyco_transf_28"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVLLSTCGSRGDVEPLVALAVRLRARGAEVRMCAPPDCADRLAEVGVPHLPLGRSARPAAAGEAKPLTAEDMLRFTTETIAMQFDRIPAAAEGCDAVVTTGLLAAALGVRSVAEKLGIPYFYAFHCPSYVPSPYYAPPPPLGEPPAPEGTDIRALWERNNQSAFRRYGAPLKSQRAAIGLPPVEDIFEHGYTDHPWMAADQVLAPLQPTDLDAVQTGAWILPDERPLSPEMEAFLDAGTPPVYLGFGSLRAPADAAKVAIEAIRAHGRRVILSRGWADLVLPDDRDDCFATGEVNQQVLFRRVAAVIHHGGAGTTHVATRAGAPQILVPQIADQPYYAGRVAELGIGVAHDGPTPTFESLSAALTTALAPETRVRAEAVAGTVLTDGAAAAADLLFAAVGEEKPAVPA","length":409,"molWeight":43139,"crc64":"6D3A8C83E1679F0B","md5":"054FBEDCB21FA3319D802E45D13A19B0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"PATHWAY":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00000B6345"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BQ30","uniProtkbId":"A0A193BQ30_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-10-05","entryVersion":42,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14306.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Phosphoenolpyruvate carboxykinase [GTP]"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"PEP carboxykinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"PEPCK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"4.1.1.32"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"GTP-dependent phosphoenolpyruvate carboxykinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"GTP-PEPCK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"pckG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14306.1"}],"value":"SD37_00630"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxaloacetate + GTP = phosphoenolpyruvate + GDP + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10388"},{"database":"ChEBI","id":"CHEBI:16452"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:58189"},{"database":"ChEBI","id":"CHEBI:58702"}],"ecNumber":"4.1.1.32","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10113"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Binds 1 Mn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004742"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005796"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Belongs to the phosphoenolpyruvate carboxykinase [GTP] family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"Phosphoenolpyruvate carboxykinase GTP-utilising N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF17297"}]},{"type":"Domain","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":605,"modifier":"EXACT"}},"description":"Phosphoenolpyruvate carboxykinase C-terminal P-loop","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00821"}]},{"type":"Region","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10113"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14306.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14306.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14306.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14306.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14306.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN14306.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_037307401.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BQ30","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_00630","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_00630","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1274","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00138","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004613","properties":[{"key":"GoTerm","value":"F:phosphoenolpyruvate carboxykinase (GTP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071333","properties":[{"key":"GoTerm","value":"P:cellular response to glucose stimulus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006107","properties":[{"key":"GoTerm","value":"P:oxaloacetate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019543","properties":[{"key":"GoTerm","value":"P:propionate catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033993","properties":[{"key":"GoTerm","value":"P:response to lipid"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042594","properties":[{"key":"GoTerm","value":"P:response to starvation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00819","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.449.10:FF:000005","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate carboxykinase [GTP]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.228.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.449.10","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate Carboxykinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.8.10","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate Carboxykinase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00452","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018091","properties":[{"key":"EntryName","value":"PEP_carboxykin_GTP_CS"}]},{"database":"InterPro","id":"IPR013035","properties":[{"key":"EntryName","value":"PEP_carboxykinase_C"}]},{"database":"InterPro","id":"IPR008209","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP"}]},{"database":"InterPro","id":"IPR035077","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP_C"}]},{"database":"InterPro","id":"IPR035078","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP_N"}]},{"database":"InterPro","id":"IPR008210","properties":[{"key":"EntryName","value":"PEP_carboxykinase_N"}]},{"database":"NCBIfam","id":"NF003253","properties":[{"key":"EntryName","value":"PRK04210.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11561","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE CARBOXYKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11561:SF0","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE CARBOXYKINASE [GTP]-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00821","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17297","properties":[{"key":"EntryName","value":"PEPCK_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001348","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF68923","properties":[{"key":"EntryName","value":"PEP carboxykinase N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53795","properties":[{"key":"EntryName","value":"PEP carboxykinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00505","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAVAIPGLEKAPTTHSGVLSWVREVAELTTPDRVVWVDGSDEEAARINAELVAAGTFVQLDAKPNSYWAASDPNDVARVEERTFICSENEEDAGPTNNWMDPAEMKATMTELYRGCMRGRTMYVIPFCMGPLGAEDPKLGIEITDFAYVVASMRVMTRAGKAALDKFVTEDGTEREFVPALHSVGAPLEPGQKDVSWPCNTTKYISHFPESREIWSYGSGYGGNSLLGKKCYSLRIGSVIARDEGWLAEHMLILKLISPEDKVHYVAAAFPSACGKTNLAMLQPTIPGWRAETLGDDIAWMRFGEDGRLYAVNPEFGFFGVAPGTDWHTNPNAMRTIEKGNTVYTNVALTDDGDVWWEGMGEKPAHATSWKKQDWTPESDEKAAHPNSRYCTPMSQCPILAPEWDDPQGVPISAILFGGRRKTTVPLVNEARDWQHGVFMGATMSSETTAAAAGAVGNVRRDPMAMLPFLGYHAGDYFKHWLDLGKNADANKLPKIFYVNWFRRGDDGRFLWPGFGENSRILKWVIDRVEGKGNAKETPVGFVPNAEDLDTEGLKEPLADIQAALDVSADEWRQELPLIEEWFEKIGDKVPASLRDELDALKQRLG","length":607,"molWeight":67218,"crc64":"684EDDEC8BB462A9","md5":"DA07738275241927B90D27B4397D1E9B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":11},"uniParcId":"UPI0004052649"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BQA4","uniProtkbId":"A0A193BQA4_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-10-05","entryVersion":37,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14364.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00069359"}],"value":"Broad-specificity linear acyl-CoA dehydrogenase FadE5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012033"}],"value":"1.3.8.7"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"1.3.8.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077090"}],"value":"Long-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077336"}],"value":"Medium-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075470"}],"value":"Short-chain-acyl-CoA dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14364.1"}],"value":"SD37_00955"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054301"}],"value":"Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates"}],"commentType":"FUNCTION"},{"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":"ARBA00049247"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a medium-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14477"},{"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:83723"},{"database":"ChEBI","id":"CHEBI:83726"}],"ecNumber":"1.3.8.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047882"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"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:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050315"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050695"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"decanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48176"},{"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:61406"},{"database":"ChEBI","id":"CHEBI:61430"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050703"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57330"},{"database":"ChEBI","id":"CHEBI:57375"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050336"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"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:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048375"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47240"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57394"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:71412"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050877"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43448"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57379"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:61526"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052387"}]}},{"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":"ARBA00004872"}],"value":"Lipid metabolism; fatty acid metabolism"}],"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":162,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]},{"type":"Domain","location":{"start":{"value":477,"modifier":"EXACT"},"end":{"value":609,"modifier":"EXACT"}},"description":"Acetyl-CoA dehydrogenase-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12806"}]}],"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":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"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":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14364.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN14364.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN14364.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_044849385.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BQA4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_00955","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_00955","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1960","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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:0070991","properties":[{"key":"GoTerm","value":"F:medium-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0016937","properties":[{"key":"GoTerm","value":"F:short-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"2.40.110.20:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase AidB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000016","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase FadE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.20","properties":[{"key":"EntryName","value":"-"},{"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":"IPR025878","properties":[{"key":"EntryName","value":"Acyl-CoA_dh-like_C_dom"}]},{"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":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"InterPro","id":"IPR052166","properties":[{"key":"EntryName","value":"Diverse_Acyl-CoA_DH"}]},{"database":"PANTHER","id":"PTHR42803","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42803:SF1","properties":[{"key":"EntryName","value":"BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12806","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"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":"MGHYKSNVRDLEFNLFEVLGVQDRLGKGVLAESDEETARGVLTELNKLASGPLADSYADADRNPPVYDPKTFSVKIPESFKKSYQALMDGEWWRLGLPNELGGFGLPPTVQWAAAELILGANAPLFMYMAGPSFAGIVDKNGTEEQKQWAQIMIDRGWGATMVLTEPDAGSDVGAGRTKAVKQEDGSWHIDGVKRFITSAENDMVENIMHLVLARPEGPGIETRPGTKGLSLFLVPKFHFDGKTGELGERNGAFVTNVEHKMGIKASTTCELTFGQHGTPAKGWLLGEVHDGIAQMFQVIEYARMMVGTKAIATLSTGYLNALEYAKERVQGADLPNMLNKTAPRVTITHHPDVRRSLMLQKAYAEGLRAVYLYTASFQDQVWTGEGDEASQKVAHGVNDLLLPIVKGVGSERATEQLVQSLQTLGGSGFLQDYPIEQYIRDAKIDSLYEGTTAIQSLDFFFRKIVRDKGASLAYVAGEITKTVESEVGNGRLKNERGLLKQALEDTQGMLGSLIGYLTSSQEDPQNINKVGQHTVRLLMSVGDLLIGWQLIKHAEVAIAKLDAGASAKDTPFYEGKIAVASFFAKSVLPELTARRAIVEAADNSLMEISEAAF","length":614,"molWeight":66964,"crc64":"464CDF3C1348410C","md5":"A02B9C31F1D43BB0513256D97D9BD4E6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":9,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0005CEAAC3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BSL0","uniProtkbId":"A0A193BSL0_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-10-05","entryVersion":46,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN15185.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN15185.1"}],"value":"SD37_05610"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"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":140,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":360,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":395,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":432,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN15185.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN15185.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN15185.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_044852145.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BSL0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_05610","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_05610","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG1207","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00113","properties":[{"key":"RectionId","value":"UER00532"}]},{"database":"UniPathway","id":"UPA00973","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"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":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010932","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTGPLSTLILAAGEGTRMRSSTPKVLHPIAGRPLVEHAVRAAAGLNPEHLVVVIGHGRDSVGARLAEVGEALGREVVTAVQEEQKGTGHAVSCALSALPDGLTGTVVVSYGDVPLLDTETLGSLVAEHNSTGNAVTVLTAVVADPTGYGRIIRDENGVVTSIVEQKDATPEQHEIAEINSGVYAFDASVLVDGLSKLSTDNAQGELYLTDVLGIARGDGKGVGALVIDDPWVTEGVNDRVQLSVLGAELNRRIVRGWQRAGVTVVDPSSTWIDAGVTLSRDVVIEPGVQLKGSTSVGEGAQIGPDSTLENVSVGAGASVVRTHGSDSELGDGVKVGPFTYLRPGSKLGTKGKLGAFVETKNADIGAGTKVPHLTYVGDATIGENSNIGCSSVFVNYDGVNKHHTTIGSHVRLGADNTFVAPVTIGDGAYSGAGTVIRQDVPPGALAVSTGPQRNIEDWVSRRRPGTPAAEAASAAKQDTTAVSDSNKGNDGESPA","length":495,"molWeight":50735,"crc64":"2DDE3C3F51FCBAF4","md5":"86F6C393313F4CAFFC34DE3E74558C92"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":4,"Compositional bias":1,"Active site":1,"Binding site":17},"uniParcId":"UPI0005CEC925"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BVX9","uniProtkbId":"A0A193BVX9_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-10-05","entryVersion":34,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16324.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16324.1"}],"value":"SD37_12140"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"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"}}]}],"features":[{"type":"Transmembrane","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023228"}],"id":"KW-0458","category":"Cellular component","name":"Lysosome"},{"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:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"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":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16324.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16324.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN16324.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_044854128.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BVX9","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_12140","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_12140","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG2271","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06174","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF3","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTGRATRRSWFIWLAAVTVYLLAVFHRTSFGVAGLQAADRFGVGAAALGTFTVLQVGVYASMQIPTGVLVDRYGPRRVLTGAVFFLGLGQILLAVADSYPLGLLARAVVGFGDALTFVSILRLIAAHFPGRQYALIAALTGAIGYVGNLGATLPLGLLLDGPGWTPTFLAVGLVTALYTAVVALRVEDIPRGAPEPVREKVRPKALGRQVADAWRTPGTRLGFWVHFSTMFAPNVLTMLWGVPFLVQGQGYPKATASSLLIVFVFGSMIGGPVVGALIGRRPSLRMPLVGGYIGAAAVLWAVLLGWSGTIPVAVLVPAFAFLSLGGPVSMIGFALARDYNPLARVGTATGVVNVGGFVATTISALAVGVLLEWTGGAFRWALLSVMAVLAFGTFRMLVWWRRTRAVLFEAEARGEEIPVQIRRRRWDAEAPLPVSS","length":436,"molWeight":46273,"crc64":"C71F03C1F90F43DE","md5":"3FFB4786C8FF194F0F96A1864A1E9923"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Transmembrane":11,"Domain":1},"uniParcId":"UPI0005CDCFE1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BW31","uniProtkbId":"A0A193BW31_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-10-05","entryVersion":40,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16385.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-tripeptide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramyl-tripeptide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16385.1"}],"value":"SD37_12490"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":472,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16385.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16385.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16385.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN16385.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_044854182.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BW31","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_12490","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_12490","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0769","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"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:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPLGTLLARAGARLVVDGDDYPAAAELTVTGSTLRAQHVLPGDLFAALPGARAHGADFSDQAIAAGAAAVLTDEAGAERPVLRDAGVPILVHPDPRAALGEIAAWIYGEPSLELSVLGITGTSGKTTTSYLVDAGLKAAGLTTGLIGTVETRIAGERLASGFTTPEAPDLQALLAVMVERGVTHVPMEVSSHALALGRVNGTRFAVGAFTNLSQDHLDFHKDMEEYFAAKSLLFDGRSTAEVVVVDSAWGHALLTPHTVTVSTEPGSDAHWRATDLTPTPAGEQTFTLHGPDGLTASAKIPLPGEFNVANAVLAAAILTTAGVPLDAIVAGLAAVEVPGRMERVYLGQPFTAVVDYAHKPAAVAQGLDALRARTEGRIITVLGCGGDRDTAKRPMMGEAAVRRSEVLIVTDDNPRSEDPAAIRAAMLAGARNAGPALGGEILEIADRREAIIHAVGLAKPGDIVLIAGKGHETGQEVQGVVHPFSDRDELASAIRRRLETP","length":501,"molWeight":51879,"crc64":"04C414FDC8DEDCFA","md5":"E0D4422435E93C7BA048E5460F29BB9D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":9,"Modified residue":1},"uniParcId":"UPI0005CE2AD6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BWA4","uniProtkbId":"A0A193BWA4_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-10-05","entryVersion":37,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16511.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate--fructose 6-phosphate 1-phosphotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"2.7.1.90"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"6-phosphofructokinase, pyrophosphate dependent"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-dependent phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-PFK"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate-dependent 6-phosphofructose-1-kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"pfp"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16511.1"}],"value":"SD37_13175"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13613"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57634"}],"ecNumber":"2.7.1.90","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Non-allosteric"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33019"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"diphosphate","id":"ChEBI:CHEBI:33019"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16511.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16511.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN16511.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_044854286.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BWA4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_13175","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_13175","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0205","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0047334","properties":[{"key":"GoTerm","value":"F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01976","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR012829","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02483","properties":[{"key":"EntryName","value":"PFK_mixed"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF52","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVGVLTGGGDCPGLNAVIRAVVRKGIEVHGWDIVGFRNGWNGPLTGDSRPLGLNDVEDILTRGGTILRSSRTNPYKVDGGVDKIKAVLAEQQVDALIAIGGEDTLGVAKRLTDDGVGVVGVPKTIDNDLGATDYTFGFDTAVSIATEAIDRLHTTAESHHRALVVEVMGRHAGWIALHSGLAGGASVILVPERHFNVDQVVSWVERRFEKEYAPIIVVAEGALPEGGEEKLLTGEKDAFGHVRLGGIGTWLADEIAARTGKESRAVVLGHVQRGGTPTAYDRVLATRFGLNAVDAVADGDFGVMVALRGTDIVRVKLAEATAELKTVPVERYEEAEVFFG","length":341,"molWeight":36201,"crc64":"78CBEFE688EC5A0B","md5":"B00D510B2517DAEE0E3DC7D7AA242A57"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":8,"Site":2},"uniParcId":"UPI0005CEC2D7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BX24","uniProtkbId":"A0A193BX24_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-10-05","entryVersion":44,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16791.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16791.1"}],"value":"SD37_14745"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":876,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":958,"modifier":"EXACT"},"end":{"value":1104,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":958,"modifier":"EXACT"},"end":{"value":1104,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":721,"modifier":"EXACT"},"end":{"value":721,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":760,"modifier":"EXACT"},"end":{"value":760,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":762,"modifier":"EXACT"},"end":{"value":762,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":767,"modifier":"EXACT"},"end":{"value":767,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":792,"modifier":"EXACT"},"end":{"value":792,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":793,"modifier":"EXACT"},"end":{"value":793,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":794,"modifier":"EXACT"},"end":{"value":794,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":795,"modifier":"EXACT"},"end":{"value":795,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":847,"modifier":"EXACT"},"end":{"value":847,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":847,"modifier":"EXACT"},"end":{"value":847,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":847,"modifier":"EXACT"},"end":{"value":847,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":847,"modifier":"EXACT"},"end":{"value":847,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":847,"modifier":"EXACT"},"end":{"value":847,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Binding site","location":{"start":{"value":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16791.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16791.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN16791.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_044850391.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BX24","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_14745","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_14745","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0458","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00171"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"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:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000014","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRTDIQHVLVIGSGPIVIGQAAEFDYSGTQACRVLREEGLRVSLVNSNPATIMTDPEFADATYIEPVTPEFVEKVIAEERPDAILATLGGQTALNCAVALHERGVLEKYGVELIGADVEAIQRGEDRQKFKDIVRTIGAEVPRSRVCHDMDEVRATVAEVGLPVVIRPSFTMGGLGSGMAHTDAELERLASTGLTESPVTEVLIEESVLGWKEFELELMRDRHDNVVVVCSIENIDAMGVHTGDSVTVAPAMTLTDREYQHMRDVGIAVLREVGVDTGGCNIQFAINPADGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAIGYTLDEIRNDITGETPAAFEPTLDYVVVKVPRFAFEKFPGADPTLTTTMKSVGEAMSFGRSFPEALGKALRSIDTKATGFWTRPDPEGATKESILDALRTPHDGRIYEVERALRFGATVEEIHEASGIDPWFIDQIALIGEVGAEVRDAQVLDEPLLRRAKRTGLSDRQIAALRPELAGEDGVRALRRRLGVRPVYKTVDTCAAEFAAKTPYHYSAYETDPAAQSEITAQTDKPKVLILGSGPNRIGQGIEFDYSCVHAAIALREAGFEAVMVNCNPETVSTDYDTSDRLYFEPLSFEDVLEVVNAEQESGTVAGVIVQLGGQTPLSLAKRLADAGVPVIGTSPDAIHLAEDRGAFGEVLTDAGLPAPKYGTATSFEGAKRIADKIGYPVLVRPSYVLGGRGMEIVYDEESLAGYIHRATEVTPEHPVLVDRFLDDAIEIDVDALFDGDELFLGGVMEHIEEAGIHSGDSSCALPPITLGRTDIETVRRSTEAIARGVGVRGLLNVQYALKDDVLYVLEANPRASRTVPFVSKATAVPLAKAAALIMTGSSIKDLRESGVLPAEGDGGHMPADSPVAVKEAVLPFHRFRTPEGHGVDSLLGPEMKSTGEVMGVDVSFGKAFAKSQAGAYGSLPTSGKVFVSVANRDKRSLVFPVKRLADLGFEILATSGTAEVLRRNGIACTVVRKHYEGSAEGEQNVVDVILSGEVQMVINTPYGNSGPRIDGYEIRTAAVSRDIPCITTVQGAAAAVHGIEAVIKGDIGVRSLQSLQAALKAKA","length":1104,"molWeight":118284,"crc64":"12081A7671706D55","md5":"1489B3C79A59E867F58183272D3EE4C0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":38},"uniParcId":"UPI0005CEBFD5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A193BX29","uniProtkbId":"A0A193BX29_AMYOR","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-10-05","entryVersion":36,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Amycolatopsis orientalis","commonName":"Nocardia orientalis","taxonId":31958,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16796.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Amycolatopsis"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16796.1"}],"value":"SD37_14770"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"25977416","citationType":"journal article","authors":["Lei X.","Yuan F.","Shi Y.","Li X.","Wang L.","Hong B."],"citationCrossReferences":[{"database":"PubMed","id":"25977416"}],"title":"Draft Genome Sequence of Norvancomycin-Producing Strain Amycolatopsis orientalis CPCC200066.","publicationDate":"2015","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"3"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16796.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}],"value":"B-37","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ANN16796.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000093695"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP016174","properties":[{"key":"ProteinId","value":"ANN16796.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_044850388.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP016174.1"}]},{"database":"AlphaFoldDB","id":"A0A193BX29","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"31958.SD37_14770","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"aori:SD37_14770","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0452","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000093695","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKPKVVLGVGGGIAAYKACEVLRGLTESGHDVRVVPTEAALNFVGAATFEALSGNPVHTGVFTEVPEVQHVRVGKEADLVIVVPATANLLAKAAHGIADDLLTNTLLTARCPVAFFPAMHTEMWEHPATRDNVALLRSRGLVVAEPAAGRLTGADTGKGRLADPAEIVDLARLLLAVPDALPRDLEGVHVAISAGGTREPLDPVRYLGNRSSGKQGYALARVAAQRGAEVTLVAAHTIALPEPAGAKVVHVSTAEEMRQAMHAEAASADVVVMAAAVADFRPSNRAEHKIKKSDDTPDPVVELSRNADILAELVRNRAEGQLVVGFAAETGDDRGGVLDHARVKLKRKGADLLVVNAVGEGKAFGTEDNSGWLLGADGTEIPIPLGAKAELASTLWDAVVTLMKR","length":406,"molWeight":42427,"crc64":"7111679779F14BC9","md5":"A99B89C3B09C97D5121615370DE31EEA"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":5},"uniParcId":"UPI0005CEDFAB"}}]}