{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O24750","uniProtkbId":"RIBD_CORAM","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2025-02-05","lastSequenceUpdateDate":"1998-01-01","entryVersion":95,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Riboflavin biosynthesis protein RibD"}},"includes":[{"recommendedName":{"fullName":{"value":"Diaminohydroxyphosphoribosylaminopyrimidine deaminase"},"shortNames":[{"value":"DRAP deaminase"}],"ecNumbers":[{"value":"3.5.4.26"}]},"alternativeNames":[{"fullName":{"value":"Riboflavin-specific deaminase"}}]},{"recommendedName":{"fullName":{"value":"5-amino-6-(5-phosphoribosylamino)uracil reductase"},"ecNumbers":[{"value":"1.1.1.193"}]},"alternativeNames":[{"fullName":{"value":"HTP reductase"}}]}]},"genes":[{"geneName":{"value":"ribD"},"synonyms":[{"value":"ribG"}]}],"comments":[{"texts":[{"value":"Converts 2,5-diamino-6-(ribosylamino)-4(3h)-pyrimidinone 5'-phosphate into 5-amino-6-(ribosylamino)-2,4(1h,3h)-pyrimidinedione 5'-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + H2O + H(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21868"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:58453"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.26"}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-amino-6-(5-phospho-D-ribitylamino)uracil + NADP(+) = 5-amino-6-(5-phospho-D-ribosylamino)uracil + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17845"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58421"},{"database":"ChEBI","id":"CHEBI:58453"}],"ecNumber":"1.1.1.193"}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Binds 1 zinc ion."}]}},{"texts":[{"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the N-terminal section; belongs to the cytidine and deoxycytidylate deaminase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"In the C-terminal section; belongs to the HTP reductase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Riboflavin biosynthesis protein RibD","featureId":"PRO_0000171720"},{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"CMP/dCMP-type deaminase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01083"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Deaminase"},{"type":"Region","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"Reductase"},{"type":"Active site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Binding site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}}],"keywords":[{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"id":"KW-0521","category":"Ligand","name":"NADP"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-ENUC894M3TFNM","citationType":"patent","authors":["Koizumi S.","Yonetani Y.","Teshiba S."],"title":"Process for producing riboflavin.","publicationDate":"31-DEC-1996","patentNumber":"US5589355"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003693","properties":[{"key":"ProteinId","value":"BAA20053.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O24750","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O24750","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00401"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00402"}]},{"database":"GO","id":"GO:0008703","properties":[{"key":"GoTerm","value":"F:5-amino-6-(5-phosphoribosylamino)uracil reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008835","properties":[{"key":"GoTerm","value":"F:diaminohydroxyphosphoribosylaminopyrimidine deaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd01284","properties":[{"key":"EntryName","value":"Riboflavin_deaminase-reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.140.10","properties":[{"key":"EntryName","value":"Cytidine Deaminase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.430.10","properties":[{"key":"EntryName","value":"Dihydrofolate Reductase, subunit A"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR016192","properties":[{"key":"EntryName","value":"APOBEC/CMP_deaminase_Zn-bd"}]},{"database":"InterPro","id":"IPR002125","properties":[{"key":"EntryName","value":"CMP_dCMP_dom"}]},{"database":"InterPro","id":"IPR016193","properties":[{"key":"EntryName","value":"Cytidine_deaminase-like"}]},{"database":"InterPro","id":"IPR024072","properties":[{"key":"EntryName","value":"DHFR-like_dom_sf"}]},{"database":"InterPro","id":"IPR004794","properties":[{"key":"EntryName","value":"Eubact_RibD"}]},{"database":"InterPro","id":"IPR002734","properties":[{"key":"EntryName","value":"RibDG_C"}]},{"database":"InterPro","id":"IPR050765","properties":[{"key":"EntryName","value":"Riboflavin_Biosynth_HTPR"}]},{"database":"NCBIfam","id":"TIGR00326","properties":[{"key":"EntryName","value":"eubact_ribD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR38011:SF7","properties":[{"key":"EntryName","value":"2,5-DIAMINO-6-RIBOSYLAMINO-4(3H)-PYRIMIDINONE 5'-PHOSPHATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR38011","properties":[{"key":"EntryName","value":"DIHYDROFOLATE REDUCTASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_8G06820)"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00383","properties":[{"key":"EntryName","value":"dCMP_cyt_deam_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01872","properties":[{"key":"EntryName","value":"RibD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006769","properties":[{"key":"EntryName","value":"RibD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53927","properties":[{"key":"EntryName","value":"Cytidine deaminase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53597","properties":[{"key":"EntryName","value":"Dihydrofolate reductase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00903","properties":[{"key":"EntryName","value":"CYT_DCMP_DEAMINASES_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51747","properties":[{"key":"EntryName","value":"CYT_DCMP_DEAMINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDSNPGADQAVAPIVEQALRTAMSAGWEVRGTTSPNPPVGAVIISTSGEIVGTGATQPVGGVHAEVQALADAAGKTEGATAVVTLEPCRHTGRTGPCTQALIEAGIKDVLFLHSDPNPSAGGGEQVLVDAGINVVQLPSPEGVPDALIPWLKSVQLRRPHVTLKFAQTIDGFTAAADGTSQWITGEMARDYVHADREHRDAIIIGTGTALIDNPSLTARYPDGTQREHQPRRVVIGRRNIADAGDAASNLNRLGFEQYATIDEALAELYATGARDVLVEGGAGLASGFANQGLVDWLQVYQAPLLLGEGISVLAHPLTNTLKGASALCPRAASGAGR","length":337,"molWeight":34888,"crc64":"2BBDA7B8BF2C243D","md5":"CC33A1098D9F9F35747615C24B5E3503"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":2},"countByFeatureType":{"Chain":1,"Domain":1,"Region":2,"Active site":1,"Binding site":14},"uniParcId":"UPI00001338D8"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O24752","uniProtkbId":"RIBBA_CORAM","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-01-01","entryVersion":112,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Riboflavin biosynthesis protein RibBA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"4.1.99.12"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase II"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"ribBA"},"synonyms":[{"value":"ribA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"Riboflavin biosynthesis protein RibBA","featureId":"PRO_0000151726"},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"DHBP synthase"},{"type":"Region","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II"},{"type":"Active site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"Proton acceptor; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01283"}]}],"keywords":[{"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-ENUC894M3TFNM","citationType":"patent","authors":["Koizumi S.","Yonetani Y.","Teshiba S."],"title":"Process for producing riboflavin.","publicationDate":"31-DEC-1996","patentNumber":"US5589355"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003693","properties":[{"key":"ProteinId","value":"BAA20055.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O24752","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O24752","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00399"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00400"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II 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:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01283","properties":[{"key":"EntryName","value":"RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"InterPro","id":"IPR016299","properties":[{"key":"EntryName","value":"Riboflavin_synth_RibBA"}]},{"database":"NCBIfam","id":"NF006803","properties":[{"key":"EntryName","value":"PRK09311.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNAPLNSAVRLDSIEEAIADIAAGKAVVVVDNEDRENEGDLIFAAELATPELVAFMVRYSSGYICVPLLPEDCKRLNLPPMMGRNEDVRGTAYTVTVDANTGTTGISATSRAETMLRLADPMSVVDDFTRPGHVVPLAARPNGVLERDGHTEAAIDLARLAGLRPAGVLCEIVSEEDPTTMARSEELRRFSDEHDLKMISIEQLIEWRRHNETQVRRTVETQLPTDFGSFTALGYKHEIDGQEHVALIAGGVEELNGAEDVFVRVHSECLTGDVFHSRRCDCGQQLHQSMEIIQEAGQGIIIYLRGHEGRGIGLLAKLKAYSLQDSGLDTVDANLEQGLPEDAREYSVAGQILRDLGIKSANLLTNNPHKGEGLRGFGVEASAHTPVEIEPNADNIDYLRTKRDRMNHDLPQVARWDAAHALK","length":423,"molWeight":46399,"crc64":"EBBE9CA3E902BD25","md5":"E8895E981D1AFD0330CDDDA87827FAED"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2},"countByFeatureType":{"Chain":1,"Region":2,"Active site":2,"Binding site":16,"Site":2},"uniParcId":"UPI000012B2CE"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q59263","uniProtkbId":"RIBF_CORAM","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":106,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Bifunctional riboflavin kinase/FMN adenylyltransferase"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Riboflavin biosynthesis protein RibF"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Riboflavin kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}],"value":"2.7.1.26"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Flavokinase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"FMN adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}],"value":"2.7.7.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"FAD pyrophosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"FAD synthase"}}]}]},"genes":[{"geneName":{"value":"ribF"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}],"value":"Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"riboflavin + ATP = FMN + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14357"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57986"},{"database":"ChEBI","id":"CHEBI:58210"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.26","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"FMN + ATP + H(+) = FAD + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17237"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58210"}],"ecNumber":"2.7.7.2","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}],"value":"Higher divalent cation concentrations lead to decrease in the turnover of riboflavin and the 5'-phosphotransferase activity, while the adenylyltransferase activity increases"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":5.0,"unit":"uM","substrate":"Mg-ATP (for riboflavin kinase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}]},{"constant":160.0,"unit":"uM","substrate":"Mg-ATP (for FMN adenylyltransferase activity)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}],"value":"With magnesium ions the highest turnover of riboflavin is observed between pH 6 and 7.5, while that of FAD is between 7.0 and 9.0. With zinc ions a steady increase in riboflavin turnover is observed between pH 4.5 and 10, while FAD is the major product at pH 7.0 and decreases rapidly above pH 8.0."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the RibF family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"Bifunctional riboflavin kinase/FMN adenylyltransferase","featureId":"PRO_0000194136"},{"type":"Beta strand","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Turn","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Turn","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Helix","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"2X0K"}]},{"type":"Beta strand","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Beta strand","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5FNZ"}]},{"type":"Helix","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Beta strand","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Beta strand","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Beta strand","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A8A"}]},{"type":"Beta strand","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Turn","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Beta strand","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Beta strand","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Helix","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]},{"type":"Turn","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"4UZE"}]},{"type":"Helix","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"5A89"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0274","category":"Ligand","name":"FAD"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0288","category":"Ligand","name":"FMN"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"7772835","citationType":"journal article","authors":["Nakagawa S.","Igarashi A.","Ohta T.","Hagihara T.","Fujio T.","Aisaka K."],"citationCrossReferences":[{"database":"PubMed","id":"7772835"},{"database":"DOI","id":"10.1271/bbb.59.694"}],"title":"Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli.","publicationDate":"1995","journal":"Biosci. Biotechnol. Biochem.","firstPage":"694","lastPage":"702","volume":"59"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"3023344","citationType":"journal article","authors":["Manstein D.J.","Pai E.F."],"citationCrossReferences":[{"database":"PubMed","id":"3023344"},{"database":"DOI","id":"10.1016/s0021-9258(18)66693-1"}],"title":"Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes.","publicationDate":"1986","journal":"J. Biol. Chem.","firstPage":"16169","lastPage":"16173","volume":"261"},"referencePositions":["PROTEIN SEQUENCE OF 1-18","FUNCTION","CATALYTIC ACTIVITY","COFACTOR","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D37967","properties":[{"key":"ProteinId","value":"BAA07182.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"JC4008","properties":[{"key":"EntryName","value":"JC4008"}]},{"database":"PDB","id":"2X0K","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A/B=1-338"}]},{"database":"PDB","id":"3ZUG","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.05 A"},{"key":"Chains","value":"A/B=1-338"}]},{"database":"PDB","id":"4UZE","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.34 A"},{"key":"Chains","value":"A/B=1-338"}]},{"database":"PDB","id":"4UZF","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.52 A"},{"key":"Chains","value":"A/B=1-338"}]},{"database":"PDB","id":"5A88","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.08 A"},{"key":"Chains","value":"A/B/C/D=183-338"}]},{"database":"PDB","id":"5A89","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.65 A"},{"key":"Chains","value":"A/B=183-338"}]},{"database":"PDB","id":"5A8A","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.80 A"},{"key":"Chains","value":"A/B=183-338"}]},{"database":"PDB","id":"5FNZ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.52 A"},{"key":"Chains","value":"A/B=1-338"}]},{"database":"PDB","id":"5FO0","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.51 A"},{"key":"Chains","value":"A/B=1-338"}]},{"database":"PDB","id":"5FO1","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.45 A"},{"key":"Chains","value":"A/B=1-338"}]},{"database":"AlphaFoldDB","id":"Q59263","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q59263","properties":[{"key":"Description","value":"-"}]},{"database":"MoonProt","id":"Q59263","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.7.1.26","properties":[{"key":"OrganismId","value":"959"}]},{"database":"BRENDA","id":"2.7.7.2","properties":[{"key":"OrganismId","value":"959"}]},{"database":"UniPathway","id":"UPA00276","properties":[{"key":"RectionId","value":"UER00406"}]},{"database":"UniPathway","id":"UPA00277","properties":[{"key":"RectionId","value":"UER00407"}]},{"database":"EvolutionaryTrace","id":"Q59263","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003919","properties":[{"key":"GoTerm","value":"F:FMN adenylyltransferase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}]},{"database":"GO","id":"GO:0008531","properties":[{"key":"GoTerm","value":"F:riboflavin kinase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"3023344"}]},{"database":"GO","id":"GO:0006747","properties":[{"key":"GoTerm","value":"P:FAD biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0009398","properties":[{"key":"GoTerm","value":"P:FMN biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02064","properties":[{"key":"EntryName","value":"FAD_synthetase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.30:FF:000003","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000021","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.30","properties":[{"key":"EntryName","value":"Riboflavin kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015864","properties":[{"key":"EntryName","value":"FAD_synthase"}]},{"database":"InterPro","id":"IPR023468","properties":[{"key":"EntryName","value":"Riboflavin_kinase"}]},{"database":"InterPro","id":"IPR002606","properties":[{"key":"EntryName","value":"Riboflavin_kinase_bac"}]},{"database":"InterPro","id":"IPR015865","properties":[{"key":"EntryName","value":"Riboflavin_kinase_bac/euk"}]},{"database":"InterPro","id":"IPR023465","properties":[{"key":"EntryName","value":"Riboflavin_kinase_dom_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF004160","properties":[{"key":"EntryName","value":"PRK05627.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00083","properties":[{"key":"EntryName","value":"ribF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22749:SF6","properties":[{"key":"EntryName","value":"RIBOFLAVIN KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22749","properties":[{"key":"EntryName","value":"RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06574","properties":[{"key":"EntryName","value":"FAD_syn"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01687","properties":[{"key":"EntryName","value":"Flavokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF004491","properties":[{"key":"EntryName","value":"FAD_Synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00904","properties":[{"key":"EntryName","value":"Flavokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF82114","properties":[{"key":"EntryName","value":"Riboflavin kinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDIWYGTAAVPKDLDNSAVTIGVFDGVHRGHQKLINATVEKAREVGAKAIMVTFDPHPVSVFLPRRAPLGITTLAERFALAESFGIDGVLVIDFTRELSGTSPEKYVEFLLEDTLHASHVVVGANFTFGENAAGTADSLRQICQSRLTVDVIDLLDDEGVRISSTTVREFLSEGDVARANWALGRHFYVTGPVVRGAGRGGKELGFPTANQYFHDTVALPADGVYAGWLTILPTEAPVSGNMEPEVAYAAAISVGTNPTFGDEQRSVESFVLDRDADLYGHDVKVEFVDHVRAMEKFDSVEQLLEVMAKDVQKTRTLLAQDVQAHKMAPETYFLQAES","length":338,"molWeight":36844,"crc64":"B714FD885412CC68","md5":"7A97913157DDFBDBA9C7BD1DD8E66480"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":2,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Beta strand":17,"Helix":13,"Turn":4},"uniParcId":"UPI00001338DD"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P58101","uniProtkbId":"COAE_CORAM","entryAudit":{"firstPublicDate":"2001-06-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2001-06-01","entryVersion":89,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"value":"Dephospho-CoA kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"value":"2.7.1.24"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"value":"Dephosphocoenzyme A kinase"}}],"flag":"Fragment"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"value":"coaE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"value":"Catalyzes the phosphorylation of the 3'-hydroxyl group of dephosphocoenzyme A to form coenzyme A"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3'-dephospho-CoA + ATP = ADP + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18245"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57328"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.24","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 5/5"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"},{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the CoaE family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"OUTSIDE"}},"description":"Dephospho-CoA kinase","featureId":"PRO_0000172933"},{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":30,"modifier":"OUTSIDE"}},"description":"DPCK","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00376"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Non-terminal residue","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":""}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0173","category":"Biological process","name":"Coenzyme A biosynthesis"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"11292795","citationType":"journal article","authors":["Mishra P.K.","Park P.K.","Drueckhammer D.G."],"citationCrossReferences":[{"database":"PubMed","id":"11292795"},{"database":"DOI","id":"10.1128/jb.183.9.2774-2778.2001"}],"title":"Identification of yacE (coaE) as the structural gene for dephosphocoenzyme A kinase in Escherichia coli K-12.","publicationDate":"2001","journal":"J. Bacteriol.","firstPage":"2774","lastPage":"2778","volume":"183"},"referencePositions":["PROTEIN SEQUENCE"],"referenceComments":[{"value":"ATCC 6871 / DSM 20306 / IAM 1641 / JCM 1305 / KCTC 1018 / NCIMB 8143 / NCTC 2398","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"AlphaFoldDB","id":"P58101","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P58101","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00356"}]},{"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:InterPro"}]},{"database":"GO","id":"GO:0004140","properties":[{"key":"GoTerm","value":"F:dephospho-CoA kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001977","properties":[{"key":"EntryName","value":"Depp_CoAkinase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"Pfam","id":"PF01121","properties":[{"key":"EntryName","value":"CoaE"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51219","properties":[{"key":"EntryName","value":"DPCK"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIIGLIGGIGSGKTTVAQLFVDEGFPLVD","length":30,"molWeight":3077,"crc64":"7BED57C45B54C536","md5":"DA7B01C04BF384DE47D2120922F3CC32"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":1,"Non-terminal residue":1},"uniParcId":"UPI0000127CDB"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9RHX0","uniProtkbId":"PURQ_CORAM","entryAudit":{"firstPublicDate":"2001-07-11","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2000-05-01","entryVersion":107,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Phosphoribosylformylglycinamidine synthase subunit PurQ"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"FGAM synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"6.3.5.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Formylglycinamide ribonucleotide amidotransferase subunit I"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"FGAR amidotransferase I"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"FGAR-AT I"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Glutaminase PurQ"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"3.5.1.2"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Phosphoribosylformylglycinamidine synthase subunit I"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"purQ"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17129"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:147286"},{"database":"ChEBI","id":"CHEBI:147287"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.3","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Cytoplasm","id":"SL-0086"}}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Phosphoribosylformylglycinamidine synthase subunit PurQ","featureId":"PRO_0000100549"},{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Glutamine amidotransferase type-1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}]},{"type":"Active site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}]},{"type":"Active site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}]},{"type":"Active site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00421"}]}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EKPUSFVR9CAJF","citationType":"submission","authors":["Yonetani Y.","Teshiba S."],"title":"Sequence analysis of Corynebacterium ammoniagenes purL.","publicationDate":"APR-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003162","properties":[{"key":"ProteinId","value":"BAA89450.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9RHX0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9RHX0","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00128"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004642","properties":[{"key":"GoTerm","value":"F:phosphoribosylformylglycinamidine synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01740","properties":[{"key":"EntryName","value":"GATase1_FGAR_AT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000019","properties":[{"key":"EntryName","value":"Phosphoribosylformylglycinamidine synthase subunit PurQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00421","properties":[{"key":"EntryName","value":"PurQ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR010075","properties":[{"key":"EntryName","value":"PRibForGlyAmidine_synth_PurQ"}]},{"database":"NCBIfam","id":"TIGR01737","properties":[{"key":"EntryName","value":"FGAM_synth_I"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002957","properties":[{"key":"EntryName","value":"purQ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47552","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47552:SF1","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13507","properties":[{"key":"EntryName","value":"GATase_5"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001586","properties":[{"key":"EntryName","value":"FGAM_synth_I"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01211","properties":[{"key":"EntryName","value":"GATase_5"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAKIGVITFPGTLDDVDAQRAVRLAGAEAVSLWHADTDLKGVDAVVVPGGFSYGDYLRSGAISALAPVMQSVVDRARQGMPTLGICNGFQILTEAGLLEGALTRNKGLHFHCVDTHLEVVNNNTAWTTEFEAGDKIFVPAKHGEGRFQAAPETIDKLEGEGQVVFRYTDNFNGSLNDIAGITNETGRIVGLMPHPEHAIETLTGPSTDGLGLFVSAINAITATV","length":225,"molWeight":23803,"crc64":"11CC6B55E5A53256","md5":"5D3B1A1720425677A2FB9E92A489F475"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1},"countByFeatureType":{"Chain":1,"Domain":1,"Active site":3},"uniParcId":"UPI0000132B51"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9RHX4","uniProtkbId":"PUR2_CORAM","entryAudit":{"firstPublicDate":"2003-05-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-05-01","entryVersion":90,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Phosphoribosylamine--glycine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"6.3.4.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"GARS"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Glycinamide ribonucleotide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Phosphoribosylglycinamide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"purD"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-phospho-beta-D-ribosylamine + glycine + ATP = N(1)-(5-phospho-beta-D-ribosyl)glycinamide + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17453"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:58681"},{"database":"ChEBI","id":"CHEBI:143788"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.13","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Binds 1 Mg(2+) or Mn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Belongs to the GARS family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"Phosphoribosylamine--glycine ligase","featureId":"PRO_0000151445"},{"type":"Domain","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}]},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00138"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0464","category":"Ligand","name":"Manganese"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-31ISCU7V6788A","citationType":"submission","authors":["Yonetani Y.","Teshiba S."],"title":"Sequence analysis of Corynebacterium ammoniagenes purD/B/C region.","publicationDate":"APR-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003161","properties":[{"key":"ProteinId","value":"BAA89446.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9RHX4","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9RHX4","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00125"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004637","properties":[{"key":"GoTerm","value":"F:phosphoribosylamine-glycine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009113","properties":[{"key":"GoTerm","value":"P:purine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"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":"1"}]},{"database":"Gene3D","id":"3.90.600.10","properties":[{"key":"EntryName","value":"Phosphoribosylglycinamide synthetase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00138","properties":[{"key":"EntryName","value":"GARS"},{"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":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"InterPro","id":"IPR020561","properties":[{"key":"EntryName","value":"PRibGlycinamid_synth_ATP-grasp"}]},{"database":"InterPro","id":"IPR000115","properties":[{"key":"EntryName","value":"PRibGlycinamide_synth"}]},{"database":"InterPro","id":"IPR020560","properties":[{"key":"EntryName","value":"PRibGlycinamide_synth_C-dom"}]},{"database":"InterPro","id":"IPR037123","properties":[{"key":"EntryName","value":"PRibGlycinamide_synth_C_sf"}]},{"database":"InterPro","id":"IPR020559","properties":[{"key":"EntryName","value":"PRibGlycinamide_synth_CS"}]},{"database":"InterPro","id":"IPR020562","properties":[{"key":"EntryName","value":"PRibGlycinamide_synth_N"}]},{"database":"InterPro","id":"IPR011054","properties":[{"key":"EntryName","value":"Rudment_hybrid_motif"}]},{"database":"NCBIfam","id":"TIGR00877","properties":[{"key":"EntryName","value":"purD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43472","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINE--GLYCINE LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43472:SF1","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINE--GLYCINE LIGASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01071","properties":[{"key":"EntryName","value":"GARS_A"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02843","properties":[{"key":"EntryName","value":"GARS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02844","properties":[{"key":"EntryName","value":"GARS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01209","properties":[{"key":"EntryName","value":"GARS_A"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01210","properties":[{"key":"EntryName","value":"GARS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51246","properties":[{"key":"EntryName","value":"Rudiment single hybrid motif"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00184","properties":[{"key":"EntryName","value":"GARS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRILVIGSGGREHAILKGLAADPATTDLHVAPGSPAFASLATVHADYKEVADPARMLELAQDIKPELVVIGPEIPLVAGVADTLRAEGIAVFGPNADAAQIEGSKAFAKEVMEAAGVATARAQTLPPGMTDDDIEHELDYFGPMYVVKDDGLAAGKGVVVTADRAEARQHIHLVHAAGNPVLLESFLDGPEVSLFCLVDGETVVPLLPAQDHKRAYDNDEGPNTGGMGAYTPLPWLSAEGVDRIVREVCEPVAKQMVERGTPYSGLLYAGLAWGQEGPSVIEFNCRFGDPETQPLLSLLKTPLAGVLNAVATGTLDELPALEWEDAYAVTVVLAAANYPESPRKGDAITSPDLADTDKILHAGTAVKDAEVISNGGRVLNVIGKGETLSAARAAAYEVLENIELADSFYRTDIGQAAEEGRISIDS","length":426,"molWeight":44756,"crc64":"BF1E7CEDD889900E","md5":"415484EA8C71918E58DD31D5E04A9A25"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":3},"uniParcId":"UPI00000B3528"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9RHX5","uniProtkbId":"PURA_CORAM","entryAudit":{"firstPublicDate":"2003-02-12","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2000-05-01","entryVersion":97,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Adenylosuccinate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"AMPSase"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"AdSS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"6.3.4.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"IMP--aspartate ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"purA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Plays an important role in the de novo pathway of purine nucleotide biosynthesis. Catalyzes the first committed step in the biosynthesis of AMP from IMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + L-aspartate + GTP = N(6)-(1,2-dicarboxyethyl)-AMP + GDP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15753"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57567"},{"database":"ChEBI","id":"CHEBI:58053"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"6.3.4.4","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Purine metabolism; AMP biosynthesis via de novo pathway; AMP from IMP: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"value":"Belongs to the adenylosuccinate synthetase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"Adenylosuccinate synthetase","featureId":"PRO_0000095169"},{"type":"Active site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}]},{"type":"Active site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00011"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-DMLJA9E5SC9TI","citationType":"submission","authors":["Yonetani Y.","Teshiba S."],"title":"Sequence Analysis of Corynebacterium ammoniagenes purA.","publicationDate":"APR-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003160","properties":[{"key":"ProteinId","value":"BAA89445.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9RHX5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9RHX5","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00075","properties":[{"key":"RectionId","value":"UER00335"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004019","properties":[{"key":"GoTerm","value":"F:adenylosuccinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP 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:0044208","properties":[{"key":"GoTerm","value":"P:'de novo' AMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046040","properties":[{"key":"GoTerm","value":"P:IMP metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03108","properties":[{"key":"EntryName","value":"AdSS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.300.10:FF:000001","properties":[{"key":"EntryName","value":"Adenylosuccinate synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.170.10:FF:000001","properties":[{"key":"EntryName","value":"Adenylosuccinate synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.440.10","properties":[{"key":"EntryName","value":"Adenylosuccinate Synthetase, subunit A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.300.10","properties":[{"key":"EntryName","value":"Adenylosuccinate Synthetase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.170.10","properties":[{"key":"EntryName","value":"Adenylosuccinate Synthetase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00011","properties":[{"key":"EntryName","value":"Adenylosucc_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018220","properties":[{"key":"EntryName","value":"Adenylosuccin_syn_GTP-bd"}]},{"database":"InterPro","id":"IPR033128","properties":[{"key":"EntryName","value":"Adenylosuccin_syn_Lys_AS"}]},{"database":"InterPro","id":"IPR042109","properties":[{"key":"EntryName","value":"Adenylosuccinate_synth_dom1"}]},{"database":"InterPro","id":"IPR042110","properties":[{"key":"EntryName","value":"Adenylosuccinate_synth_dom2"}]},{"database":"InterPro","id":"IPR042111","properties":[{"key":"EntryName","value":"Adenylosuccinate_synth_dom3"}]},{"database":"InterPro","id":"IPR001114","properties":[{"key":"EntryName","value":"Adenylosuccinate_synthetase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF002223","properties":[{"key":"EntryName","value":"PRK01117.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00184","properties":[{"key":"EntryName","value":"purA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11846","properties":[{"key":"EntryName","value":"ADENYLOSUCCINATE SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11846:SF0","properties":[{"key":"EntryName","value":"ADENYLOSUCCINATE SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00709","properties":[{"key":"EntryName","value":"Adenylsucc_synt"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00788","properties":[{"key":"EntryName","value":"Adenylsucc_synt"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01266","properties":[{"key":"EntryName","value":"ADENYLOSUCCIN_SYN_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00513","properties":[{"key":"EntryName","value":"ADENYLOSUCCIN_SYN_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAAIVIVGAQWGDEGKGKATDILGGRVDYVVKPNGGNNAGHTVVVGGEKYELKLLPAGILSENAVPVLGNGVVINLEALFEEIEGLEARGADASRLRISANAHLVAPYHQTLDRVQERFLGKRAIGTTGRGIGPAYADKVARVGVRVQDIFDESILRQKVESALDIKNQMLVKMYNRKAIDPETIVEYFLSYRDRLEPMVVDSEYELNTALDAGKHVLMEGGQATMLDVDHGTYPFVTSSNPTAGGASVGSGVGPTRITHSLGIIKAYTTRVGAGPFPTELFDKWGEYLQTTGGEVGVNTGRTRRCGWYDSVIARYASRVNGFTDYFLTKLDVLTGIGEIPICVAYDVDGERFDEMPLTQSQFHHAQPIYETMPAWEEDITGCTTFEELPQKAQDYVLRLEELSGTRMSYIGVGPGRDQTIVRHDVLDEK","length":430,"molWeight":46991,"crc64":"75458C5EC7F21B06","md5":"CBE8B0D5B018E672641BC6BDCF621DD1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":15},"uniParcId":"UPI0000132AEC"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O33924","uniProtkbId":"KPRS_CORAM","entryAudit":{"firstPublicDate":"2002-10-25","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1998-01-01","entryVersion":110,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Ribose-phosphate pyrophosphokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"RPPK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"2.7.6.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"5-phospho-D-ribosyl alpha-1-diphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Phosphoribosyl diphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Phosphoribosyl pyrophosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"P-Rib-PP synthase"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"PRPP synthase"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"PRPPase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"prs"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribose 5-phosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15609"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:78346"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.6.1","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Binds 2 Mg(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Ribose-phosphate pyrophosphokinase","featureId":"PRO_0000141129"},{"type":"Active site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}]},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0545","category":"Biological process","name":"Nucleotide biosynthesis"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-AL4I2MP4QJC0K","citationType":"submission","authors":["Kim M.K.","Park B.C.","Park J.H.","Lim B.L.","Lee D.-S."],"title":"Cloning and expression of the gene encoding phosphoribosylpyrophosphate synthetase from Brevibacterium ammoniagenes KCTC1019.","publicationDate":"OCT-1996","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U76387","properties":[{"key":"ProteinId","value":"AAB64352.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O33924","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O33924","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00087","properties":[{"key":"RectionId","value":"UER00172"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0002189","properties":[{"key":"GoTerm","value":"C:ribose phosphate diphosphokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004749","properties":[{"key":"GoTerm","value":"F:ribose phosphate diphosphokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006015","properties":[{"key":"GoTerm","value":"P:5-phosphoribose 1-diphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006164","properties":[{"key":"GoTerm","value":"P:purine nucleotide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009156","properties":[{"key":"GoTerm","value":"P:ribonucleoside monophosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000002","properties":[{"key":"EntryName","value":"Ribose-phosphate pyrophosphokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000014","properties":[{"key":"EntryName","value":"Ribose-phosphate pyrophosphokinase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00583_B","properties":[{"key":"EntryName","value":"RibP_PPkinase_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000842","properties":[{"key":"EntryName","value":"PRib_PP_synth_CS"}]},{"database":"InterPro","id":"IPR029099","properties":[{"key":"EntryName","value":"Pribosyltran_N"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR005946","properties":[{"key":"EntryName","value":"Rib-P_diPkinase"}]},{"database":"InterPro","id":"IPR037515","properties":[{"key":"EntryName","value":"Rib-P_diPkinase_bac"}]},{"database":"NCBIfam","id":"NF002320","properties":[{"key":"EntryName","value":"PRK01259.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002618","properties":[{"key":"EntryName","value":"PRK02269.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01251","properties":[{"key":"EntryName","value":"ribP_PPkin"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10210","properties":[{"key":"EntryName","value":"RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10210:SF41","properties":[{"key":"EntryName","value":"RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14572","properties":[{"key":"EntryName","value":"Pribosyl_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13793","properties":[{"key":"EntryName","value":"Pribosyltran_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01400","properties":[{"key":"EntryName","value":"Pribosyltran_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00114","properties":[{"key":"EntryName","value":"PRPP_SYNTHASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTQYLNSNLKVFSLNSNKELAEQIAKHIGVGLGKCSVDRFSDGEVQINIEESIRGCDVFIIQSTSFPVNEHIMELLIMIDALKRASAKTINIVIPYYGYARQDRKARSREPITSKLVANLLETAGATRVITLDLHAPQIQGFFDIPIDHLMGVPILSDYFETKGLKDIVIVSPDHGGVTRARKMADRLKAPIAIIDKRRPRPNVSEVMNIIGNIEGKTALLIDDIIDTAGTITLAANALVENGASEVYACCTHPVLSGPAIERIQNSNIKELVVTNSIVLPEEKKIDKVHELSVAPLIGEAIIRVYEEESVSVLFN","length":317,"molWeight":34836,"crc64":"11413BD2142AA24A","md5":"58D3893F8DC5DAC071CD71E90751A51A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":7},"uniParcId":"UPI000012DFB2"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9RHX6","uniProtkbId":"PUR9_CORAM","entryAudit":{"firstPublicDate":"2003-06-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2000-05-01","entryVersion":94,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"Bifunctional purine biosynthesis protein PurH"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"Phosphoribosylaminoimidazolecarboxamide formyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"2.1.2.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"AICAR transformylase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"IMP cyclohydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"3.5.4.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"ATIC"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"IMP synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"Inosinicase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"purH"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-10-formyltetrahydrofolate + 5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamide = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide + (6S)-5,6,7,8-tetrahydrofolate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22192"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:58467"},{"database":"ChEBI","id":"CHEBI:58475"},{"database":"ChEBI","id":"CHEBI:195366"}],"ecNumber":"2.1.2.3","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + H2O = 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18445"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58053"},{"database":"ChEBI","id":"CHEBI:58467"}],"ecNumber":"3.5.4.10","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (10-formyl THF route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"The IMP cyclohydrolase activity resides in the N-terminal region"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00139"}],"value":"Belongs to the PurH family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":516,"modifier":"EXACT"}},"description":"Bifunctional purine biosynthesis protein PurH","featureId":"PRO_0000192087"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU01202"}]}],"keywords":[{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9BSQ9813ESRUQ","citationType":"submission","authors":["Yonetani Y.","Teshiba S."],"title":"Corynebacterium ammoniagenes purNH region.","publicationDate":"APR-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003159","properties":[{"key":"ProteinId","value":"BAA89444.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9RHX6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9RHX6","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00133"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00135"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003937","properties":[{"key":"GoTerm","value":"F:IMP cyclohydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004643","properties":[{"key":"GoTerm","value":"F:phosphoribosylaminoimidazolecarboxamide formyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01421","properties":[{"key":"EntryName","value":"IMPCH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.140.20:FF:000001","properties":[{"key":"EntryName","value":"Bifunctional purine biosynthesis protein PurH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000001","properties":[{"key":"EntryName","value":"Bifunctional purine biosynthesis protein PurH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.140.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00139","properties":[{"key":"EntryName","value":"PurH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024051","properties":[{"key":"EntryName","value":"AICAR_Tfase_dup_dom_sf"}]},{"database":"InterPro","id":"IPR016193","properties":[{"key":"EntryName","value":"Cytidine_deaminase-like"}]},{"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":"IPR002695","properties":[{"key":"EntryName","value":"PurH-like"}]},{"database":"NCBIfam","id":"NF002049","properties":[{"key":"EntryName","value":"purH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00355","properties":[{"key":"EntryName","value":"purH"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11692:SF0","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN ATIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11692","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PURINE BIOSYNTHESIS PROTEIN PURH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01808","properties":[{"key":"EntryName","value":"AICARFT_IMPCHas"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000414","properties":[{"key":"EntryName","value":"AICARFT_IMPCHas"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00798","properties":[{"key":"EntryName","value":"AICARFT_IMPCHas"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53927","properties":[{"key":"EntryName","value":"Cytidine deaminase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDDRKQIKRALISVYDKTGLEELARTLDSAGVEIVSTGSTAAKIADLGINVTPVESLTGFPECLEGRVKTLHPRVHAGILADTRKPDHLNQLEELEIEPFQLVVVNLYPFKETVASGADFDGCVEQIDIGGPSMVRAAAKNHPSVAVVVDPARYGDIAEAVAQGGFDLAQRRQLAATAFKHTADYDVAVSGWFAQQLADDSVASAELEGDALRYGENPHQQASIVREGTTGVANAKQLHGKEMSYNNYQDADAAWRAAWDHERPCVAIIKHANPCGIAVSDESIAAAHAAAHACDPMSAFGGVIAVNREVTKEMATQVADIFTEVIIAPSYEDGAVEILQGKKNIRILVAEHEVPAVEVKEISGGRLLQEADVYQAEGDKASSWTLAAGEAASEEKLAELEFAWRAVRSVKSNAILLAHEGATVGVGMGQVNRVDSAKLAVDRANTLADSAERARGSVAASDAFFPFADGLQVLIDAGVSAVVQPGGSIRDEEVIAAAEAAGITMYFTGTRHFAH","length":516,"molWeight":54757,"crc64":"14EF915D6DB72B93","md5":"499625338481F450F38F90280CC494B7"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"PATHWAY":2,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1},"uniParcId":"UPI00000B3A1B"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O52831","secondaryAccessions":["Q9RHY6"],"uniProtkbId":"GUAA_CORAM","entryAudit":{"firstPublicDate":"1998-12-15","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2001-04-27","entryVersion":120,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"GMP synthase [glutamine-hydrolyzing]"},"ecNumbers":[{"value":"6.3.5.2"}]},"alternativeNames":[{"fullName":{"value":"GMP synthetase"}},{"fullName":{"value":"Glutamine amidotransferase"}}]},"genes":[{"geneName":{"value":"guaA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Catalyzes the synthesis of GMP from XMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP + diphosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11680"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:58115"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.5.2"}},{"texts":[{"value":"Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Homodimer"}],"commentType":"SUBUNIT"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"GMP synthase [glutamine-hydrolyzing]","featureId":"PRO_0000140116"},{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Glutamine amidotransferase type-1"},{"type":"Domain","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"GMPS ATP-PPase"},{"type":"Active site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Sequence conflict","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"in Ref. 1; CAA71524","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["R"]}},{"type":"Sequence conflict","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"in Ref. 1; CAA71524","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"KL","alternativeSequences":["NV"]}},{"type":"Sequence conflict","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"in Ref. 1; CAA71524","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"G","alternativeSequences":["R"]}},{"type":"Sequence conflict","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"in Ref. 1; CAA71524","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"FKDEVRAVG","alternativeSequences":["LRRSPCRS"]}},{"type":"Sequence conflict","location":{"start":{"value":446,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"in Ref. 1; CAA71524","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"PVVLLADVRSVGVQGDGRTYG","alternativeSequences":["QSYCLPMSAPSSPRRRPHLR"]}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"id":"KW-0332","category":"Biological process","name":"GMP biosynthesis"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1LVBUFO34PQ90","citationType":"submission","authors":["Han J.K."],"publicationDate":"JAN-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"BA 17-2","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"CI-KF4FAAR2V8SP","citationType":"submission","authors":["Yonetani Y.","Teshiba S."],"title":"Cloning and sequence analysis of Corynebacterium ammoniagenes guaA gene.","publicationDate":"APR-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"Y10499","properties":[{"key":"ProteinId","value":"CAA71524.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"AB003155","properties":[{"key":"ProteinId","value":"BAA89456.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O52831","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O52831","properties":[{"key":"Description","value":"-"}]},{"database":"MEROPS","id":"C26.A07","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00189","properties":[{"key":"RectionId","value":"UER00296"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"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:0003921","properties":[{"key":"GoTerm","value":"F:GMP synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd01742","properties":[{"key":"EntryName","value":"GATase1_GMP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01997","properties":[{"key":"EntryName","value":"GMP_synthase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.300.10:FF:000002","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000001","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000001","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00344","properties":[{"key":"EntryName","value":"GMP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR001674","properties":[{"key":"EntryName","value":"GMP_synth_C"}]},{"database":"InterPro","id":"IPR004739","properties":[{"key":"EntryName","value":"GMP_synth_GATase"}]},{"database":"InterPro","id":"IPR022955","properties":[{"key":"EntryName","value":"GMP_synthase"}]},{"database":"InterPro","id":"IPR025777","properties":[{"key":"EntryName","value":"GMPS_ATP_PPase_dom"}]},{"database":"InterPro","id":"IPR022310","properties":[{"key":"EntryName","value":"NAD/GMP_synthase"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF000848","properties":[{"key":"EntryName","value":"guaA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00884","properties":[{"key":"EntryName","value":"guaA_Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00888","properties":[{"key":"EntryName","value":"guaA_Nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922:SF2","properties":[{"key":"EntryName","value":"GMP SYNTHASE [GLUTAMINE-HYDROLYZING]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922","properties":[{"key":"EntryName","value":"GMP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00958","properties":[{"key":"EntryName","value":"GMP_synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02540","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00097","properties":[{"key":"EntryName","value":"ANTSNTHASEII"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"PRINTS","id":"PR00096","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54810","properties":[{"key":"EntryName","value":"GMP synthetase C-terminal dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51553","properties":[{"key":"EntryName","value":"GMPS_ATP_PPASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQPATTPRPVLVVDFGAQYAQLIARRVREASIYSEVVPHSATVKEIKAKNPAALILSGGPSSVYADGAPQLKPELLELGVPVFGICYGFQAMNHALGGNVAQTGDREYGRTEITHTGGVLHDGLEENHKVWMSHGDAVDKAPEGFTVTASSAGAPVAAMECVAKQMAGVQYHPEVMHSPHGQEVLVRFLTEVAGLEQTWTSANIAQQLIDDVRAQIGPEGRAICGLSGGVDSAVAAALVQRAIGDRLTCVFVDHGLLRAGEREQVEKDFVASTGAKLITAHEADAFLSKLAGVTDPEAKRKAIGAEFIRSFERAVAQALEESPEDSTVDFLVQGTLYPDVVESGGGDGTANIKSHHNVGGLPDDVEFELVEPLRLLFKDEVRAVGRELGLPEEIVARQPFPGPGLGIRIIGEVTEERLEILRQADLIARTELTNAGLDGDIWQCPVVLLADVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWTRVPYDVLEKISTRITNEVNDVNRVVVDITSKPPGTIEWE","length":524,"molWeight":56180,"crc64":"2ABE1AB9305641C5","md5":"FCEFE90F2CF3BF95265AC5B5FCBDB4C4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1},"countByFeatureType":{"Chain":1,"Domain":2,"Active site":3,"Binding site":1,"Sequence conflict":5},"uniParcId":"UPI000012BD58"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9RHW9","uniProtkbId":"PURL_CORAM","entryAudit":{"firstPublicDate":"2001-07-11","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2000-05-01","entryVersion":107,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Phosphoribosylformylglycinamidine synthase subunit PurL"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"FGAM synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"6.3.5.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Formylglycinamide ribonucleotide amidotransferase subunit II"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"FGAR amidotransferase II"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"FGAR-AT II"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Glutamine amidotransferase PurL"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Phosphoribosylformylglycinamidine synthase subunit II"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"purL"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17129"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:147286"},{"database":"ChEBI","id":"CHEBI:147287"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.3","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Belongs to the FGAMS family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":758,"modifier":"EXACT"}},"description":"Phosphoribosylformylglycinamidine synthase subunit PurL","featureId":"PRO_0000100450"},{"type":"Active site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}]},{"type":"Active site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}]},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":326,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":509,"modifier":"EXACT"},"end":{"value":509,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":546,"modifier":"EXACT"},"end":{"value":546,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":547,"modifier":"EXACT"},"end":{"value":547,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":549,"modifier":"EXACT"},"end":{"value":549,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EKPUSFVR9CAJF","citationType":"submission","authors":["Yonetani Y.","Teshiba S."],"title":"Sequence analysis of Corynebacterium ammoniagenes purL.","publicationDate":"APR-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003162","properties":[{"key":"ProteinId","value":"BAA89451.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9RHW9","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9RHW9","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00128"}]},{"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:0004642","properties":[{"key":"GoTerm","value":"F:phosphoribosylformylglycinamidine synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02203","properties":[{"key":"EntryName","value":"PurL_repeat1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02204","properties":[{"key":"EntryName","value":"PurL_repeat2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1330.10:FF:000004","properties":[{"key":"EntryName","value":"Phosphoribosylformylglycinamidine synthase subunit PurL"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.650.10","properties":[{"key":"EntryName","value":"PurM-like C-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1330.10","properties":[{"key":"EntryName","value":"PurM-like, N-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00420","properties":[{"key":"EntryName","value":"PurL_2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010074","properties":[{"key":"EntryName","value":"PRibForGlyAmidine_synth_PurL"}]},{"database":"InterPro","id":"IPR041609","properties":[{"key":"EntryName","value":"PurL_linker"}]},{"database":"InterPro","id":"IPR010918","properties":[{"key":"EntryName","value":"PurM-like_C_dom"}]},{"database":"InterPro","id":"IPR036676","properties":[{"key":"EntryName","value":"PurM-like_C_sf"}]},{"database":"InterPro","id":"IPR016188","properties":[{"key":"EntryName","value":"PurM-like_N"}]},{"database":"InterPro","id":"IPR036921","properties":[{"key":"EntryName","value":"PurM-like_N_sf"}]},{"database":"NCBIfam","id":"TIGR01736","properties":[{"key":"EntryName","value":"FGAM_synth_II"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002290","properties":[{"key":"EntryName","value":"purL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43555","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43555:SF1","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00586","properties":[{"key":"EntryName","value":"AIRS"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02769","properties":[{"key":"EntryName","value":"AIRS_C"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF18072","properties":[{"key":"EntryName","value":"FGAR-AT_linker"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001587","properties":[{"key":"EntryName","value":"FGAM_synthase_II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56042","properties":[{"key":"EntryName","value":"PurM C-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF55326","properties":[{"key":"EntryName","value":"PurM N-terminal domain-like"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTVSNDTVDNAKATPELDQPWEELGLKQDEYDKIVGILGRRPTDAELTVYSVMWSEHCSYKSSKTHLRYFGETTTEEMASKILAGIGENAGVVDIGDGDAVTFRVESHNHPSFVEPYQGAATGVGGIVRDIMAMGARPIAVMDQLRFGPADAPDTARVLPGVVSGIGGYGNSLGLPNIGGETVFDESYAGNPLVNALCVGTLRVEDLKLAFASGTGNKVMLFGSRTGLDGIGGVSVLGSASFEEGEERKLPAVQVGDPFAEKVLIECCLELYAAGVVVGIQDLGGGGLACATSELAAAGDGGMVVNLDNVPLRAENMSAAEILASESQERMCAVVSPDNVEKFREICEKWDVTCAEIGEVTDKKDTYLVYHNGELVVDAPPSTIDEGPVYERPYARPQWQDEIQQAPEIARPESLVQAFKDMVSSPALSSRAFITEQYDRYVRGNTVKAKQSDSGVLRINEETSRGVAISADGSGRYTKLDPNMGARLALAEAYRNVAVTGARPYAVTNCLNFGSPENTDVMWQFREAVHGLADGSKELNIPVSGGNVSFYNQTGDEPILPTPVVGVLGVIDDVHKALAHDLGGIDEPETLILLGETKEEFGGSIWQQVSGGGLQGLPPQVDLANEAKLADFFVGNTSVAASHDLSEGGLAIAAFEMAQKNNVGVDLDLSVVHEDALTALFSESASRVLISTASDHLDGILQRASELGIPAVVVGTTNDSGNITFAGEEVATAELREAWSATLPNLFGHAVGANSVVE","length":758,"molWeight":80146,"crc64":"7BA7E5DFF2E1F43B","md5":"948933829C002E0493CDD247C9FFEE60"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":2,"Binding site":13},"uniParcId":"UPI0000132B2C"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q44678","uniProtkbId":"PURK_CORAM","entryAudit":{"firstPublicDate":"1998-12-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":106,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"N5-carboxyaminoimidazole ribonucleotide synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"N5-CAIR synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"6.3.4.18"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"5-(carboxyamino)imidazole ribonucleotide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"purK"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + hydrogencarbonate + ATP = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19317"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58730"},{"database":"ChEBI","id":"CHEBI:137981"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.18","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"value":"Belongs to the PurK/PurT family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"N5-carboxyaminoimidazole ribonucleotide synthase","featureId":"PRO_0000074996"},{"type":"Domain","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"8998996","citationType":"journal article","authors":["Chung S.O.","Lee J.H.","Lee S.Y.","Lee D.S."],"citationCrossReferences":[{"database":"PubMed","id":"8998996"},{"database":"DOI","id":"10.1111/j.1574-6968.1996.tb08116.x"}],"title":"Genomic organization of purK and purE in Brevibacterium ammoniagenes ATCC 6872: purE locus provides a clue for genomic evolution.","publicationDate":"1996","journal":"FEMS Microbiol. Lett.","firstPage":"265","lastPage":"268","volume":"137"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X91189","properties":[{"key":"ProteinId","value":"CAA62598.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q44678","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q44678","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00942"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034028","properties":[{"key":"GoTerm","value":"F:5-(carboxyamino)imidazole ribonucleotide synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004638","properties":[{"key":"GoTerm","value":"F:phosphoribosylaminoimidazole carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"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":"1"}]},{"database":"HAMAP","id":"MF_01928","properties":[{"key":"EntryName","value":"PurK"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR003135","properties":[{"key":"EntryName","value":"ATP-grasp_carboxylate-amine"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"InterPro","id":"IPR005875","properties":[{"key":"EntryName","value":"PurK"}]},{"database":"InterPro","id":"IPR040686","properties":[{"key":"EntryName","value":"PurK_C"}]},{"database":"InterPro","id":"IPR054350","properties":[{"key":"EntryName","value":"PurT/PurK_preATP-grasp"}]},{"database":"InterPro","id":"IPR011054","properties":[{"key":"EntryName","value":"Rudment_hybrid_motif"}]},{"database":"NCBIfam","id":"NF004680","properties":[{"key":"EntryName","value":"PRK06019.1-6"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01161","properties":[{"key":"EntryName","value":"purK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11609:SF5","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11609","properties":[{"key":"EntryName","value":"PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02222","properties":[{"key":"EntryName","value":"ATP-grasp"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17769","properties":[{"key":"EntryName","value":"PurK_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22660","properties":[{"key":"EntryName","value":"RS_preATP-grasp-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51246","properties":[{"key":"EntryName","value":"Rudiment single hybrid motif"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKRVSEQAGNPDGNPQAHVPGMPVIAVIGDGQLARMMQTAAIELGQSLRLLAGARDASAAQVCADVVLGDYTNYDDLLKAVDGATAVTFDHEHVPNEHLTALIDAGYNDQPQPAALINAQDKLVMRERLAELGAPVPRFAPIESAQDAYDFWTLTSGQVCLKARRGGYDGKGVWFPNNESELTALVSDLSRRGVALMAEEKVGWSRELSVLVARTPSGEVATWPLTESVQRNGVCAEAVAPAPGVDPQLQQRAETLGEKIATELGVTGVLAVELFAFANESGAEDIAVNELAMRPHNTGHWTLVGSVTSQFEQHLRAVMDEPLGDTSTLAPVTVMANVLGADEDQRCQWASVPRSGAPVPATKVHLYGKGIAQGRKIGHVNLTGEDEEATRRDARLAADFLVNAAWSDNWSAK","length":413,"molWeight":44111,"crc64":"F738B230DF5D119A","md5":"456496BA71B90284CCBD36C5CFB5760A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Region":1,"Binding site":5},"uniParcId":"UPI0000132B1D"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q3S664","uniProtkbId":"RS4_CORAM","entryAudit":{"firstPublicDate":"2006-03-21","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2005-10-11","entryVersion":69,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01306"}],"value":"Small ribosomal subunit protein uS4"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"30S ribosomal protein S4"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01306"}],"value":"rpsD"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01306"}],"value":"One of the primary rRNA binding proteins, it binds directly to 16S rRNA where it nucleates assembly of the body of the 30S subunit"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01306"}],"value":"With S5 and S12 plays an important role in translational accuracy"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01306"}],"value":"Part of the 30S ribosomal subunit. Contacts protein S5. The interaction surface between S4 and S5 is involved in control of translational fidelity"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01306"}],"value":"Belongs to the universal ribosomal protein uS4 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"Small ribosomal subunit protein uS4","featureId":"PRO_0000228889"},{"type":"Domain","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"S4 RNA-binding","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01306"}]}],"keywords":[{"id":"KW-0687","category":"Molecular function","name":"Ribonucleoprotein"},{"id":"KW-0689","category":"Molecular function","name":"Ribosomal protein"},{"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"id":"KW-0699","category":"Molecular function","name":"rRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3BPOQD8BSBJ2N","citationType":"submission","authors":["Ham S.H.","Kim J.H.","Lee B.R."],"title":"Molecular analysis of RNA polymerase alpha operon from Corynebacterium ammoniagenes.","publicationDate":"AUG-2005","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"DQ157860","properties":[{"key":"ProteinId","value":"AAZ91711.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q3S664","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q3S664","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0015935","properties":[{"key":"GoTerm","value":"C:small ribosomal subunit"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003735","properties":[{"key":"GoTerm","value":"F:structural constituent of ribosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042274","properties":[{"key":"GoTerm","value":"P:ribosomal small subunit biogenesis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006412","properties":[{"key":"GoTerm","value":"P:translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00165","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.290.10:FF:000001","properties":[{"key":"EntryName","value":"30S ribosomal protein S4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1050.10","properties":[{"key":"EntryName","value":"Ribosomal Protein S4 Delta 41, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.290.10","properties":[{"key":"EntryName","value":"RNA-binding S4 domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01306_B","properties":[{"key":"EntryName","value":"Ribosomal_uS4_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022801","properties":[{"key":"EntryName","value":"Ribosomal_uS4"}]},{"database":"InterPro","id":"IPR005709","properties":[{"key":"EntryName","value":"Ribosomal_uS4_bact"}]},{"database":"InterPro","id":"IPR018079","properties":[{"key":"EntryName","value":"Ribosomal_uS4_CS"}]},{"database":"InterPro","id":"IPR001912","properties":[{"key":"EntryName","value":"Ribosomal_uS4_N"}]},{"database":"InterPro","id":"IPR002942","properties":[{"key":"EntryName","value":"S4_RNA-bd"}]},{"database":"InterPro","id":"IPR036986","properties":[{"key":"EntryName","value":"S4_RNA-bd_sf"}]},{"database":"NCBIfam","id":"NF003717","properties":[{"key":"EntryName","value":"rpsD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01017","properties":[{"key":"EntryName","value":"rpsD_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11831","properties":[{"key":"EntryName","value":"30S 40S RIBOSOMAL PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11831:SF4","properties":[{"key":"EntryName","value":"SMALL RIBOSOMAL SUBUNIT PROTEIN US4M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00163","properties":[{"key":"EntryName","value":"Ribosomal_S4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01479","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01390","properties":[{"key":"EntryName","value":"Ribosomal_S4"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00363","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55174","properties":[{"key":"EntryName","value":"Alpha-L RNA-binding motif"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00632","properties":[{"key":"EntryName","value":"RIBOSOMAL_S4"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50889","properties":[{"key":"EntryName","value":"S4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MARYTGPATRVSRRLRVDLVGGDMAFERRPYPPGQAGRNRIKESEYLLQLQEKQKAKYTYGVLERQFRRYYVEANRQPGKTGDNLVVLLETRLDNVVYRAGLARTRRQARQLVSHGHFTVNGKKTNVPSYRVSQYDIIDIRERSRKMEWFEEAQDRLGEAVVPAWLQVVPESLRILVHQLPERAQIDVPLQEQLIVELYSK","length":201,"molWeight":23510,"crc64":"FD779660D3DE7FB7","md5":"AC80F2D21B557208C533143E6E6013B4"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1},"uniParcId":"UPI00005ADD18"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q44679","uniProtkbId":"PURE_CORAM","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2025-02-05","lastSequenceUpdateDate":"1996-11-01","entryVersion":104,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"N5-carboxyaminoimidazole ribonucleotide mutase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"N5-CAIR mutase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"5.4.99.18"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"5-(carboxyamino)imidazole ribonucleotide mutase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"purE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"Catalyzes the conversion of N5-carboxyaminoimidazole ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole ribonucleotide (CAIR)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + H(+) = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13193"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58730"},{"database":"ChEBI","id":"CHEBI:77657"}],"ecNumber":"5.4.99.18","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"value":"Belongs to the AIR carboxylase family. Class I subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"N5-carboxyaminoimidazole ribonucleotide mutase","featureId":"PRO_0000074972"},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_01929"}],"ligand":{"name":"substrate"}}],"keywords":[{"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"8998996","citationType":"journal article","authors":["Chung S.O.","Lee J.H.","Lee S.Y.","Lee D.S."],"citationCrossReferences":[{"database":"PubMed","id":"8998996"},{"database":"DOI","id":"10.1111/j.1574-6968.1996.tb08116.x"}],"title":"Genomic organization of purK and purE in Brevibacterium ammoniagenes ATCC 6872: purE locus provides a clue for genomic evolution.","publicationDate":"1996","journal":"FEMS Microbiol. Lett.","firstPage":"265","lastPage":"268","volume":"137"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X91189","properties":[{"key":"ProteinId","value":"CAA62599.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q44679","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q44679","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00943"}]},{"database":"GO","id":"GO:0034023","properties":[{"key":"GoTerm","value":"F:5-(carboxyamino)imidazole ribonucleotide mutase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01929","properties":[{"key":"EntryName","value":"PurE_classI"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR033747","properties":[{"key":"EntryName","value":"PurE_ClassI"}]},{"database":"InterPro","id":"IPR000031","properties":[{"key":"EntryName","value":"PurE_dom"}]},{"database":"InterPro","id":"IPR024694","properties":[{"key":"EntryName","value":"PurE_prokaryotes"}]},{"database":"NCBIfam","id":"TIGR01162","properties":[{"key":"EntryName","value":"purE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23046:SF2","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23046","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE CATALYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00731","properties":[{"key":"EntryName","value":"AIRC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001338","properties":[{"key":"EntryName","value":"AIR_carboxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01001","properties":[{"key":"EntryName","value":"AIRC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52255","properties":[{"key":"EntryName","value":"N5-CAIR mutase (phosphoribosylaminoimidazole carboxylase, PurE)"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAPLVGLIMGSDSDWPTVEPAAEVLDEFGVPFEVGVVSAHRTPEKMLDYAKQAHTRGIKVIVACAGGAAHLPGMVAAATPLPVIGIPRALKDLEGLDSLLSIVQMPAGVPVATVSIGGAKNAGLLAIRTLGVQYSELVERMADYQENMADYQPKIWPRKLSKKTPIFAPSSWGTRP","length":177,"molWeight":18741,"crc64":"EAFA45863C7265BB","md5":"EA67A6963E00F3F7BD0B9A2E27425F62"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":3},"uniParcId":"UPI0000132A71"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O24753","uniProtkbId":"RISB_CORAM","entryAudit":{"firstPublicDate":"2000-12-01","lastAnnotationUpdateDate":"2025-02-05","lastSequenceUpdateDate":"1998-01-01","entryVersion":87,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"6,7-dimethyl-8-ribityllumazine synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"DMRL synthase"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"LS"},{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"Lumazine synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"2.5.1.78"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"ribH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + phosphate + 2 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26152"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15934"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58201"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"2.5.1.78","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"value":"Belongs to the DMRL synthase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"6,7-dimethyl-8-ribityllumazine synthase","featureId":"PRO_0000134746"},{"type":"Active site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}]},{"type":"Binding site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15934"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"ligand":{"name":"5-amino-6-(D-ribitylamino)uracil","id":"ChEBI:CHEBI:15934"}},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15934"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"ligand":{"name":"5-amino-6-(D-ribitylamino)uracil","id":"ChEBI:CHEBI:15934"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15934"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"ligand":{"name":"5-amino-6-(D-ribitylamino)uracil","id":"ChEBI:CHEBI:15934"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58830"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"ligand":{"name":"(2S)-2-hydroxy-3-oxobutyl phosphate","id":"ChEBI:CHEBI:58830"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15934"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"ligand":{"name":"5-amino-6-(D-ribitylamino)uracil","id":"ChEBI:CHEBI:15934"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58830"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00178"}],"ligand":{"name":"(2S)-2-hydroxy-3-oxobutyl phosphate","id":"ChEBI:CHEBI:58830"}}],"keywords":[{"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-ENUC894M3TFNM","citationType":"patent","authors":["Koizumi S.","Yonetani Y.","Teshiba S."],"title":"Process for producing riboflavin.","publicationDate":"31-DEC-1996","patentNumber":"US5589355"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003693","properties":[{"key":"ProteinId","value":"BAA20056.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O24753","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O24753","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"2.5.1.78","properties":[{"key":"OrganismId","value":"959"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00404"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009349","properties":[{"key":"GoTerm","value":"C:riboflavin synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000906","properties":[{"key":"GoTerm","value":"F:6,7-dimethyl-8-ribityllumazine synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd09209","properties":[{"key":"EntryName","value":"Lumazine_synthase-I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.960","properties":[{"key":"EntryName","value":"Lumazine/riboflavin synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00178","properties":[{"key":"EntryName","value":"Lumazine_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR034964","properties":[{"key":"EntryName","value":"LS"}]},{"database":"InterPro","id":"IPR002180","properties":[{"key":"EntryName","value":"LS/RS"}]},{"database":"InterPro","id":"IPR036467","properties":[{"key":"EntryName","value":"LS/RS_sf"}]},{"database":"NCBIfam","id":"TIGR00114","properties":[{"key":"EntryName","value":"lumazine-synth"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21058:SF0","properties":[{"key":"EntryName","value":"6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21058","properties":[{"key":"EntryName","value":"6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00885","properties":[{"key":"EntryName","value":"DMRL_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52121","properties":[{"key":"EntryName","value":"Lumazine synthase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKEGLPEVATIDATGISVAVISATWNADICDRLHERALAHAQQLGAEADGFRVVGALEIPVAVQEAARHYDAVVALGCVIRGGTPHFDYVCDSVTQGLTRIALDTSKPIANGVLTVNTHDQAVDRSGAPGAAEDKGVEAMQAALDTVLQLRNIKERASKRGL","length":163,"molWeight":17109,"crc64":"14664D7886BE69D4","md5":"9CB186A4B752A4A134580D1EAED07D50"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":6},"uniParcId":"UPI00001339B1"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q9RHX2","uniProtkbId":"PUR7_CORAM","entryAudit":{"firstPublicDate":"2003-05-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2000-05-01","entryVersion":80,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00137"}],"value":"Phosphoribosylaminoimidazole-succinocarboxamide synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00137"}],"value":"6.3.2.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00137"}],"value":"SAICAR synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00137"}],"value":"purC"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-aspartate + ATP = (2S)-2-[5-amino-1-(5-phospho-beta-D-ribosyl)imidazole-4-carboxamido]succinate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22628"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58443"},{"database":"ChEBI","id":"CHEBI:77657"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.6","evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00137"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00137"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"HAMAP-Rule","id":"MF_00137"}],"value":"Belongs to the SAICAR synthetase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"Phosphoribosylaminoimidazole-succinocarboxamide synthase","featureId":"PRO_0000100820"}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-31ISCU7V6788A","citationType":"submission","authors":["Yonetani Y.","Teshiba S."],"title":"Sequence analysis of Corynebacterium ammoniagenes purD/B/C region.","publicationDate":"APR-1997","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB003161","properties":[{"key":"ProteinId","value":"BAA89448.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q9RHX2","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q9RHX2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00131"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004639","properties":[{"key":"GoTerm","value":"F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01414","properties":[{"key":"EntryName","value":"SAICAR_synt_Sc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000015","properties":[{"key":"EntryName","value":"Phosphoribosylaminoimidazole-succinocarboxamide synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.200.20","properties":[{"key":"EntryName","value":"Phosphorylase Kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00137","properties":[{"key":"EntryName","value":"SAICAR_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR028923","properties":[{"key":"EntryName","value":"SAICAR_synt/ADE2_N"}]},{"database":"InterPro","id":"IPR001636","properties":[{"key":"EntryName","value":"SAICAR_synth"}]},{"database":"InterPro","id":"IPR018236","properties":[{"key":"EntryName","value":"SAICAR_synthetase_CS"}]},{"database":"NCBIfam","id":"NF010568","properties":[{"key":"EntryName","value":"PRK13961.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00081","properties":[{"key":"EntryName","value":"purC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43700","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43700:SF1","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINOIMIDAZOLE-SUCCINOCARBOXAMIDE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01259","properties":[{"key":"EntryName","value":"SAICAR_synt"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56104","properties":[{"key":"EntryName","value":"SAICAR synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01057","properties":[{"key":"EntryName","value":"SAICAR_SYNTHETASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01058","properties":[{"key":"EntryName","value":"SAICAR_SYNTHETASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRPQLSDYQHVSSGKVRDIYEVDDNTLLMVVTDRISAYDFALEPAIPDKGRVLTATTMFFFDAIDFPNHLAGPIDDARIPEEVLGRAIIVKKLNMLPFECVARGYLTGSGLKEYNANGTVCGIELPEGLVEASRLPEPIFTPATKAEQGDHDENVSFERVVQDLGQERAEQLRDETLRIYSAAAKIAEEKGIILADTKFEFGLDSEGNLVLGDEVLTPDSSRYWPADTYAEGIVQPSFDKQYVRNWLTSEESGWDVESETQPPVLPDDIVAATRLRYIEAYERLSGKRFIDFIGG","length":295,"molWeight":32947,"crc64":"B1CD2E68FB6490AC","md5":"B7B0F46716EE868E9930354F8F150BE0"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00000B0108"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O69272","uniProtkbId":"NRDI_CORAM","entryAudit":{"firstPublicDate":"2000-05-30","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"1998-08-01","entryVersion":79,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Protein NrdI"}}},"genes":[{"geneName":{"value":"nrdI"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Probably involved in ribonucleotide reductase function"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the NrdI family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Protein NrdI","featureId":"PRO_0000164311"}],"references":[{"referenceNumber":1,"citation":{"id":"9468481","citationType":"journal article","authors":["Fieschi F.","Torrents E.","Toulokhonova L.","Jordan A.","Hellman U.","Barbe J.","Gibert I.","Karlsson M.","Sjoeberg B.-M."],"citationCrossReferences":[{"database":"PubMed","id":"9468481"},{"database":"DOI","id":"10.1074/jbc.273.8.4329"}],"title":"The manganese-containing ribonucleotide reductase of Corynebacterium ammoniagenes is a class Ib enzyme.","publicationDate":"1998","journal":"J. Biol. Chem.","firstPage":"4329","lastPage":"4337","volume":"273"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"Y09572","properties":[{"key":"ProteinId","value":"CAA70764.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"O69272","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O69272","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.360","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00128","properties":[{"key":"EntryName","value":"NrdI"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029039","properties":[{"key":"EntryName","value":"Flavoprotein-like_sf"}]},{"database":"InterPro","id":"IPR020852","properties":[{"key":"EntryName","value":"RNR_Ib_NrdI_bac"}]},{"database":"InterPro","id":"IPR004465","properties":[{"key":"EntryName","value":"RNR_NrdI"}]},{"database":"NCBIfam","id":"TIGR00333","properties":[{"key":"EntryName","value":"nrdI"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR37297","properties":[{"key":"EntryName","value":"PROTEIN NRDI"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR37297:SF1","properties":[{"key":"EntryName","value":"PROTEIN NRDI"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07972","properties":[{"key":"EntryName","value":"Flavodoxin_NdrI"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005087","properties":[{"key":"EntryName","value":"NrdI"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52218","properties":[{"key":"EntryName","value":"Flavoproteins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLVVYSSSVTDNTHRFVQKLDLPNVRIPLRLKDEPLIVNEPYVLVCPTYGGGVSLTGENSRPVPRQVIRFLNNEHNRSFIRAVVAGGNSNFGADFGKAGEVISAKCKVPYVYRFEMMGNEDDVRICRGGLVQNAAKLGLEKQAS","length":144,"molWeight":15897,"crc64":"FE1D345DB629D251","md5":"4417BE2541A0C26C71C725757E135E8C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00001304D7"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q45825","uniProtkbId":"YRI3_CORAM","entryAudit":{"firstPublicDate":"1997-11-01","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"1996-11-01","entryVersion":73,"sequenceVersion":1},"annotationScore":1.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Uncharacterized protein in ribF 3'region"}},"flag":"Fragment"},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the IUNH family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":92,"modifier":"OUTSIDE"}},"description":"Uncharacterized protein in ribF 3'region","featureId":"PRO_0000206842"},{"type":"Non-terminal residue","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":""}],"references":[{"referenceNumber":1,"citation":{"id":"7772835","citationType":"journal article","authors":["Nakagawa S.","Igarashi A.","Ohta T.","Hagihara T.","Fujio T.","Aisaka K."],"citationCrossReferences":[{"database":"PubMed","id":"7772835"},{"database":"DOI","id":"10.1271/bbb.59.694"}],"title":"Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli.","publicationDate":"1995","journal":"Biosci. Biotechnol. Biochem.","firstPage":"694","lastPage":"702","volume":"59"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D37967","properties":[{"key":"ProteinId","value":"BAA07183.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"PC4009","properties":[{"key":"EntryName","value":"PC4009"}]},{"database":"AlphaFoldDB","id":"Q45825","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q45825","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0016799","properties":[{"key":"GoTerm","value":"F:hydrolase activity, hydrolyzing N-glycosyl compounds"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.245.10","properties":[{"key":"EntryName","value":"Ribonucleoside hydrolase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001910","properties":[{"key":"EntryName","value":"Inosine/uridine_hydrolase_dom"}]},{"database":"InterPro","id":"IPR052775","properties":[{"key":"EntryName","value":"IUN_hydrolase"}]},{"database":"InterPro","id":"IPR036452","properties":[{"key":"EntryName","value":"Ribo_hydro-like"}]},{"database":"PANTHER","id":"PTHR46190:SF1","properties":[{"key":"EntryName","value":"SI:CH211-201H21.5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46190","properties":[{"key":"EntryName","value":"SI:CH211-201H21.5-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01156","properties":[{"key":"EntryName","value":"IU_nuc_hydro"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53590","properties":[{"key":"EntryName","value":"Nucleoside hydrolase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKMILDLDTGIDDAFALAYAIAHPGIDLIGVTGTYGNVTIEQGMANTQALLTLLGAADVPVYAGRAIDGFEVSEASARIHGRNGVGEVDIAA","length":92,"molWeight":9446,"crc64":"251074C5B1A0C3C2","md5":"FB5247974448A01C8C7A87A136BA852F"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Non-terminal residue":1},"uniParcId":"UPI000013BFDD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A8CVW0","uniProtkbId":"A8CVW0_CORAM","entryAudit":{"firstPublicDate":"2007-11-13","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2007-11-13","entryVersion":77,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABV25877.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011971"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Orotate phosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"OPRT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"OPRTase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011971"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"2.4.2.10"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABV25877.1"}],"value":"pyrE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10380"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57538"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004889"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30839"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"orotate","id":"ChEBI:CHEBI:30839"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30839"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"orotate","id":"ChEBI:CHEBI:30839"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"17921291","citationType":"journal article","authors":["Wang X.","Ma C.","Wang X.","Xu P."],"citationCrossReferences":[{"database":"PubMed","id":"17921291"},{"database":"DOI","id":"10.1128/JB.01161-07"}],"title":"Orotate phosphoribosyltransferase from Corynebacterium ammoniagenes lacking a conserved lysine.","publicationDate":"2007","journal":"J. Bacteriol.","firstPage":"9030","lastPage":"9036","volume":"189"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABV25877.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ABV25877.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"EU123869","properties":[{"key":"ProteinId","value":"ABV25877.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A8CVW0","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A8CVW0","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00119"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004588","properties":[{"key":"GoTerm","value":"F:orotate phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000029","properties":[{"key":"EntryName","value":"Orotate phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01208","properties":[{"key":"EntryName","value":"PyrE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023031","properties":[{"key":"EntryName","value":"OPRT"}]},{"database":"InterPro","id":"IPR004467","properties":[{"key":"EntryName","value":"Or_phspho_trans_dom"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"NCBIfam","id":"TIGR00336","properties":[{"key":"EntryName","value":"pyrE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19278","properties":[{"key":"EntryName","value":"OROTATE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19278:SF9","properties":[{"key":"EntryName","value":"URIDINE 5'-MONOPHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSNSINAEARAELAELIKELAVVHGEVTLSSGKKADYYIDVRRATLHARASRLIGQLLREATADWDYDAVGGLTLGADPVATAIMHADGRDINAFVVRKEAKKHGMQRRIEGPDLTGKKVLVVEDTTTTGNSPLTAVAALREAGIEVVGVATVVDRATGADEVIAAEGLPYRSLLGLSDLGLN","length":184,"molWeight":19445,"crc64":"BBD7CF256BAB93B0","md5":"92F9905045324D6C73D1168EC1F6E674"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":7},"uniParcId":"UPI00000364F6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"B7UDD2","uniProtkbId":"B7UDD2_CORAM","entryAudit":{"firstPublicDate":"2009-02-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2009-02-10","entryVersion":66,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58442.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Homoserine O-acetyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"HAT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"2.3.1.31"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Homoserine transacetylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"HTA"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58442.1"}],"value":"metX"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"metXA"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-homoserine + acetyl-CoA = O-acetyl-L-homoserine + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13701"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57476"},{"database":"ChEBI","id":"CHEBI:57716"}],"ecNumber":"2.3.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Belongs to the AB hydrolase superfamily. MetX family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00561"}]},{"type":"Active site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000443-1"}]},{"type":"Active site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000443-1"}]},{"type":"Active site","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000443-1"}]},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58442.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1CULPVG0JD9BF","citationType":"submission","authors":["Lee S.-M.","Hwang B.-J.","Lee H.-S."],"publicationDate":"NOV-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58442.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58442.1"}]},{"referenceNumber":2,"citation":{"id":"19383689","citationType":"journal article","authors":["Lee S.M.","Hwang B.J.","Kim Y.","Lee H.S."],"citationCrossReferences":[{"database":"PubMed","id":"19383689"},{"database":"DOI","id":"10.1099/mic.0.024976-0"}],"title":"The cmaR gene of Corynebacterium ammoniagenes performs a novel regulatory role in the metabolism of sulfur-containing amino acids.","publicationDate":"2009","journal":"Microbiology","firstPage":"1878","lastPage":"1889","volume":"155"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58442.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58442.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FJ483537","properties":[{"key":"ProteinId","value":"ACK58442.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"B7UDD2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00051","properties":[{"key":"RectionId","value":"UER00074"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004414","properties":[{"key":"GoTerm","value":"F:homoserine O-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009092","properties":[{"key":"GoTerm","value":"P:L-homoserine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.40.50.1820","properties":[{"key":"EntryName","value":"alpha/beta hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00296","properties":[{"key":"EntryName","value":"MetX_acyltransf"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000073","properties":[{"key":"EntryName","value":"AB_hydrolase_1"}]},{"database":"InterPro","id":"IPR029058","properties":[{"key":"EntryName","value":"AB_hydrolase_fold"}]},{"database":"InterPro","id":"IPR008220","properties":[{"key":"EntryName","value":"HAT_MetX-like"}]},{"database":"NCBIfam","id":"NF001209","properties":[{"key":"EntryName","value":"metX"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF047917","properties":[{"key":"EntryName","value":"MetX_acetyl_MTB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32268","properties":[{"key":"EntryName","value":"HOMOSERINE O-ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32268:SF11","properties":[{"key":"EntryName","value":"HOMOSERINE O-ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00561","properties":[{"key":"EntryName","value":"Abhydrolase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000443","properties":[{"key":"EntryName","value":"Homoser_Ac_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53474","properties":[{"key":"EntryName","value":"alpha/beta-Hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVSTHVLLADEGVLTTIPIGSFTTEAGADIASVDIAYQRWGEFRGSNVLLIEHALTGDSDVATWWCDLVGPGKALDTDFWCVIATNVLGGCNGSTGPSSDFDGKPYGSRFPAISIRDQVEAEKRFLDVLGITEVHAVIGGSMGGARTLEWTLLYPEMLQAACVIAVSARASAWQIGIQSAQISAIERDPLWQGGDYYDGEYPAEGLAAARRIAHLTYRGEMEIDERFGTSAQAGENPLGPYRKLDQRFAVNSYLDYQGAKLTQRFDAGSYVTLTESLNRHDIGRGRGGLNKALASSEVPTMVVGVDTDILYPYHQQEHISRNLGNLLAMAKLSSPVGHDAFLVEGRQMDRILRNFIQQSLPNATESVDGVEYRLGDEYII","length":380,"molWeight":41386,"crc64":"A96AF090702B776E","md5":"8CA068D053DCEE9F94F50392C3D87557"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":3,"Binding site":2},"uniParcId":"UPI000188F447"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"B7UDE0","uniProtkbId":"B7UDE0_CORAM","entryAudit":{"firstPublicDate":"2009-02-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2009-02-10","entryVersion":56,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58450.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Phosphoadenosine 5'-phosphosulfate reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"PAPS reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"1.8.4.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"3'-phosphoadenylylsulfate reductase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"PAPS reductase, thioredoxin dependent"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"PAPS sulfotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"PAdoPS reductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58450.1"}],"value":"cysH"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Catalyzes the formation of sulfite from phosphoadenosine 5'-phosphosulfate (PAPS) using thioredoxin as an electron donor"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[thioredoxin]-disulfide + sulfite + adenosine 3',5'-bisphosphate + 2 H(+) = [thioredoxin]-dithiol + 3'-phosphoadenylyl sulfate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11724"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17359"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:58343"}],"ecNumber":"1.8.4.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009732"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Belongs to the PAPS reductase family. CysH subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"Phosphoadenosine phosphosulphate reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01507"}]},{"type":"Active site","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Nucleophile; cysteine thiosulfonate intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-6DF73KE275EVD","citationType":"submission","authors":["Lee S.-M.","Hwang B.-J.","Kim Y.","Lee H.-S."],"publicationDate":"NOV-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58450.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58450.1"}]},{"referenceNumber":2,"citation":{"id":"19383689","citationType":"journal article","authors":["Lee S.M.","Hwang B.J.","Kim Y.","Lee H.S."],"citationCrossReferences":[{"database":"PubMed","id":"19383689"},{"database":"DOI","id":"10.1099/mic.0.024976-0"}],"title":"The cmaR gene of Corynebacterium ammoniagenes performs a novel regulatory role in the metabolism of sulfur-containing amino acids.","publicationDate":"2009","journal":"Microbiology","firstPage":"1878","lastPage":"1889","volume":"155"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58450.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58450.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FJ483541","properties":[{"key":"ProteinId","value":"ACK58450.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"B7UDE0","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00140","properties":[{"key":"RectionId","value":"UER00206"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004604","properties":[{"key":"GoTerm","value":"F:phosphoadenylyl-sulfate reductase (thioredoxin) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00063","properties":[{"key":"EntryName","value":"CysH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004511","properties":[{"key":"EntryName","value":"PAPS/APS_Rdtase"}]},{"database":"InterPro","id":"IPR002500","properties":[{"key":"EntryName","value":"PAPS_reduct_dom"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR00434","properties":[{"key":"EntryName","value":"cysH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002537","properties":[{"key":"EntryName","value":"PRK02090.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46509","properties":[{"key":"EntryName","value":"PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46509:SF1","properties":[{"key":"EntryName","value":"PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01507","properties":[{"key":"EntryName","value":"PAPS_reduct"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000857","properties":[{"key":"EntryName","value":"PAPS_reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYKRRNPLKVMGMTDLLNAGKNYLDASISPQGTRDTAPLAADVAQKNQELVEQWADKLFDATATDIMAWAAEHAPGRLAVTMSMENTVLAELAAKAGLDADLLFIDTGFHFPETLETADAVEKRYPQLPLKRIKPLLSPEQQDEIYGPRMYSWDLAAYNRMRKVEPLNMAMDEYAGWITGLRRADSEHRAQAPALSLDRTGRLKISPIITWDLADTDKYIADENLVIHPLTLQGYRSIGCAPVTFPVGDGDDARAGRVFADGKTECGLHE","length":270,"molWeight":29964,"crc64":"7B7AE47EA945F973","md5":"09ADB2B0220DCDD6A854F5B118CD87E1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1},"uniParcId":"UPI000188F44F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"O31302","uniProtkbId":"O31302_CORAM","entryAudit":{"firstPublicDate":"1998-01-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-01-01","entryVersion":121,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CAA75358.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Holo-[acyl-carrier-protein] synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Holo-ACP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"2.7.8.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"4'-phosphopantetheinyl transferase AcpS"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CAA75358.1"}],"value":"PPT1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GJN43940.1"}],"value":"acpS"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GJN43940.1"}],"value":"CAT723_24190"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"apo-[ACP] + CoA = holo-[ACP] + adenosine 3',5'-bisphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12068"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9690"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:58343"},{"database":"ChEBI","id":"CHEBI:64479"}],"ecNumber":"2.7.8.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Belongs to the P-Pant transferase superfamily. AcpS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010990"}],"value":"Belongs to the P-Pant transferase superfamily. Gsp/Sfp/HetI/AcpT family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"4'-phosphopantetheinyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01648"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"1"}},{"type":"Binding site","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"2"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"1"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"1"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"2"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"1"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"2"}},{"type":"Binding site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"2"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"1"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"2"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"1"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NE9"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}],"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"9346306","citationType":"journal article","authors":["Stuible H.P.","Meier S.","Schweizer E."],"citationCrossReferences":[{"database":"PubMed","id":"9346306"},{"database":"DOI","id":"10.1111/j.1432-1033.1997.00481.x"}],"title":"Identification, isolation and biochemical characterization of a phosphopantetheine:protein transferase that activates the two type-I fatty acid synthases of Brevibacterium ammoniagenes.","publicationDate":"1997","journal":"Eur. J. Biochem.","firstPage":"481","lastPage":"487","volume":"248"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CAA75358.1"}],"value":"ATCC6871","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"CAA75358.1"}]},{"referenceNumber":2,"citation":{"id":"21697604","citationType":"journal article","authors":["Gokulan K.","Aggarwal A.","Shipman L.","Besra G.S.","Sacchettini J.C."],"citationCrossReferences":[{"database":"PubMed","id":"21697604"},{"database":"DOI","id":"10.1107/s0907444911020221"}],"title":"Mycobacterium tuberculosis acyl carrier protein synthase adopts two different pH-dependent structural conformations.","publicationDate":"2011","journal":"Acta Crystallogr. D","firstPage":"657","lastPage":"669","volume":"67"},"referencePositions":["X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) IN COMPLEX WITH COA"],"evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NE9"},{"evidenceCode":"ECO:0007829","source":"PDB","id":"3NFD"}]},{"referenceNumber":3,"citation":{"id":"CI-21FJ5ATMAM019","citationType":"submission","authors":["Matsuzawa M.","Hiratani M.","Abe I.","Tsuji Y.","Nakamura J."],"title":"Draft genome sequence of Corynebacterium ammoniagenes strain T-723.","publicationDate":"DEC-2021","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GJN43940.1"}],"value":"T-723","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"GJN43940.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"Y15081","properties":[{"key":"ProteinId","value":"CAA75358.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"BQKK01000009","properties":[{"key":"ProteinId","value":"GJN43940.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"3NE9","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.50 A"},{"key":"Chains","value":"A/B/C=1-153"}]},{"database":"PDB","id":"3NFD","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.89 A"},{"key":"Chains","value":"A/B/C/D/E/F=1-153"}]},{"database":"AlphaFoldDB","id":"O31302","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O31302","properties":[{"key":"Description","value":"-"}]},{"database":"EvolutionaryTrace","id":"O31302","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008897","properties":[{"key":"GoTerm","value":"F:holo-[acyl-carrier-protein] synthase 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:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.90.470.20","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00101","properties":[{"key":"EntryName","value":"AcpS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008278","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom"}]},{"database":"InterPro","id":"IPR037143","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom_sf"}]},{"database":"InterPro","id":"IPR002582","properties":[{"key":"EntryName","value":"ACPS"}]},{"database":"InterPro","id":"IPR050559","properties":[{"key":"EntryName","value":"P-Pant_transferase_sf"}]},{"database":"InterPro","id":"IPR004568","properties":[{"key":"EntryName","value":"Ppantetheine-prot_Trfase_dom"}]},{"database":"NCBIfam","id":"NF000831","properties":[{"key":"EntryName","value":"acpS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00556","properties":[{"key":"EntryName","value":"pantethn_trn"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12215:SF10","properties":[{"key":"EntryName","value":"L-AMINOADIPATE-SEMIALDEHYDE DEHYDROGENASE-PHOSPHOPANTETHEINYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12215","properties":[{"key":"EntryName","value":"PHOSPHOPANTETHEINE TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01648","properties":[{"key":"EntryName","value":"ACPS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56214","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLDNREAMTVGVDLVHIPGFAEQLSRPGSTFEQVFSPLERRHAQTRRDAAADATNSSLAGSRTEHLAGRWAAKEAFIKAWSQAIYGKPPVIEPDLVNFAEIEVLPDRWGRVALQLKGEVAAKLQESIGDVELALSISHDGDYATAQCLLRYQR","length":153,"molWeight":16885,"crc64":"ADE208DDE34EEE00","md5":"810422DBDF2D8156F543BE135812E368"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2},"countByFeatureType":{"Domain":1,"Binding site":14},"uniParcId":"UPI00000B4E79"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"B7UDD1","uniProtkbId":"B7UDD1_CORAM","entryAudit":{"firstPublicDate":"2009-02-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2009-02-10","entryVersion":54,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"submissionNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}],"value":"O-acetylhomoserine sulfhydrylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}],"value":"2.5.1.49"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}],"value":"metY"}}],"comments":[{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362118"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009077"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362118"}],"value":"Belongs to the trans-sulfuration enzymes family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Modified residue","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001434-2"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001434-2"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-1CULPVG0JD9BF","citationType":"submission","authors":["Lee S.-M.","Hwang B.-J.","Lee H.-S."],"publicationDate":"NOV-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}]},{"referenceNumber":2,"citation":{"id":"19383689","citationType":"journal article","authors":["Lee S.M.","Hwang B.J.","Kim Y.","Lee H.S."],"citationCrossReferences":[{"database":"PubMed","id":"19383689"},{"database":"DOI","id":"10.1099/mic.0.024976-0"}],"title":"The cmaR gene of Corynebacterium ammoniagenes performs a novel regulatory role in the metabolism of sulfur-containing amino acids.","publicationDate":"2009","journal":"Microbiology","firstPage":"1878","lastPage":"1889","volume":"155"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58441.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FJ483537","properties":[{"key":"ProteinId","value":"ACK58441.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"B7UDD1","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004124","properties":[{"key":"GoTerm","value":"F:cysteine synthase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003961","properties":[{"key":"GoTerm","value":"F:O-acetylhomoserine aminocarboxypropyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0071269","properties":[{"key":"GoTerm","value":"P:L-homocysteine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019346","properties":[{"key":"GoTerm","value":"P:transsulfuration"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00614","properties":[{"key":"EntryName","value":"CGS_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000035","properties":[{"key":"EntryName","value":"O-succinylhomoserine sulfhydrylase"},{"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":"IPR000277","properties":[{"key":"EntryName","value":"Cys/Met-Metab_PyrdxlP-dep_enz"}]},{"database":"InterPro","id":"IPR006235","properties":[{"key":"EntryName","value":"OAc-hSer/O-AcSer_sulfhydrylase"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR01326","properties":[{"key":"EntryName","value":"OAH_OAS_sulfhy"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004125","properties":[{"key":"EntryName","value":"PRK05613.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43797","properties":[{"key":"EntryName","value":"HOMOCYSTEINE/CYSTEINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43797:SF2","properties":[{"key":"EntryName","value":"HOMOCYSTEINE_CYSTEINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01053","properties":[{"key":"EntryName","value":"Cys_Met_Meta_PP"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001434","properties":[{"key":"EntryName","value":"CGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPHLTGTVPDMTKYDNSNFENWSLETRALHVGQDLDGNSNSRNVPIHQTTSYVFDSAEHAANRFNLSDAGPIYTRLTNPTTGALEARIASLEGGVDAVAFASGQAAQTAALINLASAGDHIVSSPRLYGGTNTLFTITLARLGIEVTLVDNPDDPQSWADAVKPNTRAFYAETFGNPIADILDIPAVAEVAHNNQVPLIVDNTIATAAVARPLELGADIVVASTTKFYSGNGSSIGGILVDGGKFDWTVERDGKPVFPYFVTPDAAYHGLKYADLGAPAFALKARAGILRDTGAALSPFNAWVTLTGLETLQLRIDKHGENAQKVAEYLEAHDKVTKVNYAGLDSSPYKEVKERLGYTSTGSVLSFEIDGGKDEAWAFIDALKLHSNLANIGDTRSLVVHPATTTHSQSDEEGLRVAGITQSTVRLSVGIENIADIIADLELGFTAI","length":447,"molWeight":47609,"crc64":"9BB4F7A3897E693D","md5":"5297125E284620B8E68763F6B483417A"},"extraAttributes":{"countByCommentType":{"COFACTOR":1,"SIMILARITY":1},"countByFeatureType":{"Modified residue":1},"uniParcId":"UPI000188F446"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"B7UDD3","uniProtkbId":"B7UDD3_CORAM","entryAudit":{"firstPublicDate":"2009-02-10","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2009-02-10","entryVersion":61,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58443.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003862"}],"value":"Methylenetetrahydrofolate reductase"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58443.1"}],"value":"metF"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-5-methyl-5,6,7,8-tetrahydrofolate + NAD(+) = (6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19821"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:18608"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.5.1.54","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048628"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:19823"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048628"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003862"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004777"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003862"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006743"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003862"}],"value":"Belongs to the methylenetetrahydrofolate reductase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"Methylenetetrahydrofolate reductase-like catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02219"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003862"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003862"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003862"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-6DF73KE275EVD","citationType":"submission","authors":["Lee S.-M.","Hwang B.-J.","Kim Y.","Lee H.-S."],"publicationDate":"NOV-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58443.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58443.1"}]},{"referenceNumber":2,"citation":{"id":"19383689","citationType":"journal article","authors":["Lee S.M.","Hwang B.J.","Kim Y.","Lee H.S."],"citationCrossReferences":[{"database":"PubMed","id":"19383689"},{"database":"DOI","id":"10.1099/mic.0.024976-0"}],"title":"The cmaR gene of Corynebacterium ammoniagenes performs a novel regulatory role in the metabolism of sulfur-containing amino acids.","publicationDate":"2009","journal":"Microbiology","firstPage":"1878","lastPage":"1889","volume":"155"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58443.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58443.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FJ483538","properties":[{"key":"ProteinId","value":"ACK58443.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"B7UDD3","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00193","properties":[{"key":"RectionId","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0071949","properties":[{"key":"GoTerm","value":"F:FAD binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0106312","properties":[{"key":"GoTerm","value":"F:methylenetetrahydrofolate reductase (NADH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006555","properties":[{"key":"GoTerm","value":"P:L-methionine metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd00537","properties":[{"key":"EntryName","value":"MTHFR"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.220","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029041","properties":[{"key":"EntryName","value":"FAD-linked_oxidoreductase-like"}]},{"database":"InterPro","id":"IPR003171","properties":[{"key":"EntryName","value":"Mehydrof_redctse-like"}]},{"database":"PANTHER","id":"PTHR45754","properties":[{"key":"EntryName","value":"METHYLENETETRAHYDROFOLATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45754:SF3","properties":[{"key":"EntryName","value":"METHYLENETETRAHYDROFOLATE REDUCTASE (NADPH)"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02219","properties":[{"key":"EntryName","value":"MTHFR"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51730","properties":[{"key":"EntryName","value":"FAD-linked oxidoreductase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVPRISASAPLDYLELDPAGHPRVENKEQAFSRTALSFEVIPPRHDADQAKIANLLQVLGSYNPDYIAVTSSKRSGWLEGTAKFIEQISSTTTMRPLAHLACTAGDKRELISWINVLVDAGVRGFLALRGDLEPGQTSLPEGYLQHGDELVRLIRQLEGEQAARFAAGRLAVAVACYPNGHAESANDDEDFDVLLSKQRSGADLAITQLFFDAEDYLKFSQRAQLAGTKMPLIPGIMPITSLKRAQRMGELSGLEVPPKLIDKLSRARSPDEEYAIGMAHTVELAQAVIAAGAGCLHIYTHNNADITQELLAEIGISASIKN","length":322,"molWeight":34955,"crc64":"3C76A32287C40ABD","md5":"2D4182B07AD4823A7089F147C26C238E"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI000188F448"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"B7UDD4","uniProtkbId":"B7UDD4_CORAM","entryAudit":{"firstPublicDate":"2009-02-10","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2009-02-10","entryVersion":54,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Corynebacterium ammoniagenes","commonName":"Brevibacterium ammoniagenes","taxonId":1697,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Mycobacteriales","Corynebacteriaceae","Corynebacterium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012034"}],"value":"5-methyltetrahydropteroyltriglutamate--homocysteine S-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012034"}],"value":"2.1.1.14"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}],"value":"metE"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002777"}],"value":"Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004681"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009553"}],"value":"Belongs to the vitamin-B12 independent methionine synthase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"Cobalamin-independent methionine synthase MetE N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08267"}]},{"type":"Domain","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":754,"modifier":"EXACT"}},"description":"Cobalamin-independent methionine synthase MetE C-terminal/archaeal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01717"}]},{"type":"Active site","location":{"start":{"value":702,"modifier":"EXACT"},"end":{"value":702,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-3"}]},{"type":"Binding site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58199"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-homocysteine","id":"ChEBI:CHEBI:58199"}},{"type":"Binding site","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57844"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-methionine","id":"ChEBI:CHEBI:57844"}},{"type":"Binding site","location":{"start":{"value":493,"modifier":"EXACT"},"end":{"value":493,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57844"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-methionine","id":"ChEBI:CHEBI:57844"}},{"type":"Binding site","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":570,"modifier":"EXACT"},"end":{"value":570,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":608,"modifier":"EXACT"},"end":{"value":608,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58199"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-homocysteine","id":"ChEBI:CHEBI:58199"}},{"type":"Binding site","location":{"start":{"value":608,"modifier":"EXACT"},"end":{"value":608,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57844"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-methionine","id":"ChEBI:CHEBI:57844"}},{"type":"Binding site","location":{"start":{"value":650,"modifier":"EXACT"},"end":{"value":650,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":652,"modifier":"EXACT"},"end":{"value":652,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":674,"modifier":"EXACT"},"end":{"value":674,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":734,"modifier":"EXACT"},"end":{"value":734,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-6DF73KE275EVD","citationType":"submission","authors":["Lee S.-M.","Hwang B.-J.","Kim Y.","Lee H.-S."],"publicationDate":"NOV-2008","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}]},{"referenceNumber":2,"citation":{"id":"19383689","citationType":"journal article","authors":["Lee S.M.","Hwang B.J.","Kim Y.","Lee H.S."],"citationCrossReferences":[{"database":"PubMed","id":"19383689"},{"database":"DOI","id":"10.1099/mic.0.024976-0"}],"title":"The cmaR gene of Corynebacterium ammoniagenes performs a novel regulatory role in the metabolism of sulfur-containing amino acids.","publicationDate":"2009","journal":"Microbiology","firstPage":"1878","lastPage":"1889","volume":"155"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}],"value":"ATCC 6872","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ACK58444.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"FJ483538","properties":[{"key":"ProteinId","value":"ACK58444.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"B7UDD4","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00051","properties":[{"key":"RectionId","value":"UER00082"}]},{"database":"GO","id":"GO:0003871","properties":[{"key":"GoTerm","value":"F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008652","properties":[{"key":"GoTerm","value":"P:amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03311","properties":[{"key":"EntryName","value":"CIMS_C_terminal_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR013215","properties":[{"key":"EntryName","value":"Cbl-indep_Met_Synth_N"}]},{"database":"InterPro","id":"IPR006276","properties":[{"key":"EntryName","value":"Cobalamin-indep_Met_synthase"}]},{"database":"InterPro","id":"IPR002629","properties":[{"key":"EntryName","value":"Met_Synth_C/arc"}]},{"database":"InterPro","id":"IPR038071","properties":[{"key":"EntryName","value":"UROD/MetE-like_sf"}]},{"database":"NCBIfam","id":"NF003556","properties":[{"key":"EntryName","value":"metE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30519","properties":[{"key":"EntryName","value":"5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08267","properties":[{"key":"EntryName","value":"Meth_synt_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01717","properties":[{"key":"EntryName","value":"Meth_synt_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000382","properties":[{"key":"EntryName","value":"MeTrfase_B12_ind"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51726","properties":[{"key":"EntryName","value":"UROD/MetE-like"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTNQPTSFPKATIEGYPRVGPQRELKKALEAFWAGKIDQETFESAAHSLRVDTYARLKDLGLNEDYAIPADVAYYDQVLETSLTVGAVGGDAAEVSLEEEFALARGNSERAPLEMTKWFDTNYHYIVPEIADGQKFVARPQRIVKLVEEARAQGHAVRPYLVGPVTVLALSKQAEGSNGQPLERLDELVESYIHVLAALADAGVAWVQLAEPATVADLAVADDTQIAAHLEAAYTKILAAENRPQVYLTTPYGSARAGLDALAKVAPEALHVDLSVGTQALDSDYVNRVKNTVDTAKTQLVAGLVDGRNVWAGNLRALRETFEQFDGASVSTSVSLQHVPHTVEAEPNLPVDVAAWFSFANEKIGEVVALAAGPLDAAEAYARADRAVRTRAESTRTHNQQVADRTAALPKGQVQREPAFAERQEAQKALGLPALPTTTIGSFPQTSDIRKARADHRAGNLTDEQYVEELRKEVASVIELQERLGLDVLVHGEPERNDMVQYFAELLDGFVVTENGWVQSYGSRCTRPPIVVGDVSRPKAMTVEWAKYAQSLSQKHVKGMLTGPVTILAWSFVRDDVHQSVSADQIGVALADEVKDLEEAGIEIIQIDEPALRELLPLREEDRPSYLDWAVRSFRLVSLDAAPTTQIHTHLCYSEFGQIIDAVAGLDADVTSIEAARSRMELLQDIDEKFHSEIGPGIYDIHSPRIPSVAEMAELIRAALKHVPLERLWVNPDCGLKTRGYEETEQSLRNMVLARDEVAANLKVSVNA","length":768,"molWeight":84160,"crc64":"6B282ABA190E18A7","md5":"1D34E0C1C96D763609B925068030BAAD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":13},"uniParcId":"UPI000188F449"}}]}