{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1GCQ2","uniProtkbId":"A0A8I1GCQ2_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":19,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266133.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Fatty acid oxidation complex subunit alpha"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Enoyl-CoA hydratase/Delta(3)-cis-Delta(2)-trans-enoyl-CoA isomerase/3-hydroxybutyryl-CoA epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"4.2.1.17"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"5.1.2.3"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"5.3.3.8"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"3-hydroxyacyl-CoA dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"1.1.1.35"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266133.1"}],"value":"fadB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266133.1"}],"value":"JHC10_04145"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Involved in the aerobic and anaerobic degradation of long-chain fatty acids via beta-oxidation cycle. Catalyzes the formation of 3-oxoacyl-CoA from enoyl-CoA via L-3-hydroxyacyl-CoA. It can also use D-3-hydroxyacyl-CoA and cis-3-enoyl-CoA as substrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21760"},{"database":"ChEBI","id":"CHEBI:57315"},{"database":"ChEBI","id":"CHEBI:57316"}],"ecNumber":"5.1.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3E)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45228"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:85097"}],"ecNumber":"5.3.3.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22432"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:90726"}],"ecNumber":"1.1.1.35","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049556"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16105"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:58856"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3Z)-enoyl-CoA = a 4-saturated (2E)-enoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45900"},{"database":"ChEBI","id":"CHEBI:85097"},{"database":"ChEBI","id":"CHEBI:85489"}],"ecNumber":"5.3.3.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20724"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:137480"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005005"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Lipid metabolism; fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"Heterotetramer of two alpha chains (FadB) and two beta chains (FadA)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"In the C-terminal section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008750"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"value":"In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007005"}],"value":"In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266133.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase/isomerase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00378"}]},{"type":"Domain","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase NAD binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02737"}]},{"type":"Domain","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":592,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Domain","location":{"start":{"value":625,"modifier":"EXACT"},"end":{"value":709,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase/isomerase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Region","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":718,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Active site","location":{"start":{"value":450,"modifier":"EXACT"},"end":{"value":450,"modifier":"EXACT"}},"description":"For 3-hydroxyacyl-CoA dehydrogenase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":500,"modifier":"EXACT"},"end":{"value":500,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":658,"modifier":"EXACT"},"end":{"value":658,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]},{"type":"Site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022963"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01621"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266133.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266133.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000011","properties":[{"key":"ProteinId","value":"MBJ7266133.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199493929.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXBHZ010000003.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1GCQ2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0036125","properties":[{"key":"GoTerm","value":"C:fatty acid beta-oxidation multienzyme complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008692","properties":[{"key":"GoTerm","value":"F:3-hydroxybutyryl-CoA epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004165","properties":[{"key":"GoTerm","value":"F:delta(3)-delta(2)-enoyl-CoA isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004300","properties":[{"key":"GoTerm","value":"F:enoyl-CoA hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016509","properties":[{"key":"GoTerm","value":"F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070403","properties":[{"key":"GoTerm","value":"F:NAD+ binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006635","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06558","properties":[{"key":"EntryName","value":"crotonase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000009","properties":[{"key":"EntryName","value":"Fatty oxidation complex, alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1040.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01621","properties":[{"key":"EntryName","value":"FadB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006180","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR006176","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR006108","properties":[{"key":"EntryName","value":"3HC_DH_C"}]},{"database":"InterPro","id":"IPR008927","properties":[{"key":"EntryName","value":"6-PGluconate_DH-like_C_sf"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR001753","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra/iso"}]},{"database":"InterPro","id":"IPR050136","properties":[{"key":"EntryName","value":"FA_oxidation_alpha_subunit"}]},{"database":"InterPro","id":"IPR012799","properties":[{"key":"EntryName","value":"FadB"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF008727","properties":[{"key":"EntryName","value":"fadB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02437","properties":[{"key":"EntryName","value":"FadB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612:SF3","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00725","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02737","properties":[{"key":"EntryName","value":"3HCDH_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00378","properties":[{"key":"EntryName","value":"ECH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48179","properties":[{"key":"EntryName","value":"6-phosphogluconate dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00067","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIYQGESIRVDFIEPGFAELQFDAKGSVNKFDQATLEEFSEALTKLQNTDDLRGVIVTSSKSTFIVGADITEFLTLFSDQEKTRSWVAKASRVFDQLEDLPVPTVGAVKGFALGGGCEALLACDYRVADTTATIGLPEVKLGLIPGFGGTMRLPRVIGPDNALEWITTGKNNKAEDAMKVGAIDAIVEPDNLTKAALNLAKAAAAGEQDWKAKRQPKLDPLKANDTELMMTLVTAKGLIAAKAGKHYPAPHKALEAIENGAREHREGALKAENNAFFDLTQTEACQAQVGIFLADQAVKSKSKKYAKAATKEIKTAGVLGAGIMGGGIAYQSASKGIPAVMKDIKQDALDLGMKEAGKILKKGVERGKVNNEKMIKILSSITPTLLNDAVKDVDIVVEAVVENPKVKGSVLAEIEGVISDDAILTSNTSTISITELAKNLKRPEKFCGMHFFNPVHKMPLVEIIRGEKTSDDTVNAVVAYALKLGKTPIVVNDCPGFLVNRVLFPYLAGFAGMVDEGVDFVGIDKVMEKQFGWPMGPAYLSDVVGIDTADHCTVVMEAGFPTRMKRDESSAIAKLAAAERYGQKNGKGFYVYGTDKKGKPTKEADPATYELLGCEQGKKLDADEVIARCMIPMVNEVVRCLEEDIVGSAAEADMALLYGLGFPPFRGGPFRYLETLGMDNFIQLADKYAHLGEIYQVTDGMREMAKAGKSYFDTTSAK","length":718,"molWeight":77387,"crc64":"72FCB754B516162F","md5":"724EC9CF802689811F63E1EFA8E48873"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":4,"Region":2,"Active site":1,"Binding site":9,"Site":2},"uniParcId":"UPI000C53C413"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G487","uniProtkbId":"A0A8I1G487_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":19,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266557.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Xanthine-guanine phosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"XGPRT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"2.4.2.22"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Xanthine phosphoribosyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266557.1"}],"value":"gpt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266557.1"}],"value":"JHC10_06320"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25424"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58115"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17973"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XMP + diphosphate = xanthine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10800"},{"database":"ChEBI","id":"CHEBI:17712"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.22","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Purine metabolism; GMP biosynthesis via salvage pathway; GMP from guanine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266557.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]},{"type":"Binding site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58115"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"GMP","id":"ChEBI:CHEBI:58115"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16235"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"guanine","id":"ChEBI:CHEBI:16235"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17712"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"xanthine","id":"ChEBI:CHEBI:17712"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58115"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"GMP","id":"ChEBI:CHEBI:58115"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16235"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"guanine","id":"ChEBI:CHEBI:16235"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17712"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"xanthine","id":"ChEBI:CHEBI:17712"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022726"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0660","category":"Biological process","name":"Purine salvage"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266557.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266557.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000018","properties":[{"key":"ProteinId","value":"MBJ7266557.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054488237.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXAWT010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G487","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"78252344","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9789690at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004422","properties":[{"key":"GoTerm","value":"F:hypoxanthine phosphoribosyltransferase activity"},{"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:0000310","properties":[{"key":"GoTerm","value":"F:xanthine phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032263","properties":[{"key":"GoTerm","value":"P:GMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032264","properties":[{"key":"GoTerm","value":"P:IMP salvage"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032265","properties":[{"key":"GoTerm","value":"P:XMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01903","properties":[{"key":"EntryName","value":"XGPRT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR023747","properties":[{"key":"EntryName","value":"Xanthine_Guanine_PRibTrfase"}]},{"database":"NCBIfam","id":"NF006613","properties":[{"key":"EntryName","value":"gpt"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39563","properties":[{"key":"EntryName","value":"XANTHINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39563:SF1","properties":[{"key":"EntryName","value":"XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE"},{"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":"MGWHSNREFFVSWEELHRATRELARRQLPAEQYKGIIAVSRGGLVPAAIVARELNIRVVDCVAVSSYDHTEQRDDLQVMKDVTATTDGEGFLVVDDLVDTGNTLKFLRDRLPKAKFVTVYAKPAGMELVDDFVADLAQDTWIHFPWDMHLHYIEPLAGQES","length":161,"molWeight":18298,"crc64":"507772F06C592E94","md5":"0254D853FF6DC1A9D85234BA66ECF902"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":9},"uniParcId":"UPI0006C883C2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G5D4","uniProtkbId":"A0A8I1G5D4_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2022-01-19","entryVersion":18,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266099.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266099.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266099.1"}],"value":"JHC10_03975"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266099.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Domain","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Mannose-1-phosphate guanyltransferase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF25087"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266099.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266099.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000011","properties":[{"key":"ProteinId","value":"MBJ7266099.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199493913.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000005.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G5D4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR056729","properties":[{"key":"EntryName","value":"GMPPB_C"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR018357","properties":[{"key":"EntryName","value":"Hexapep_transf_CS"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25087","properties":[{"key":"EntryName","value":"GMPPB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00101","properties":[{"key":"EntryName","value":"HEXAPEP_TRANSFERASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLRVVILAAGKGTRMRSDLPKVLHKVANKPMVEHVIDTARSLKPDAINLIYGHGGDQLQQAIAGDDLTWVEQREQLGTGHAVQQVIPHLKSNEKVIILYGDVPLLTESTLIKLVTASANTSLGLLTMTLAEPTGYGRIVRNERRSVTGIVEQKDANAQQLAIDEVNTGIMIADSDKLKGWLEQLSNDNAQKEYYLTDIVEMAAQEGVNIATAQPDNAQEVEGANNRQQLASLERALQQRQAEELMTQGVTLIDPARFDCRGKLSAGSDVTIDINAVFEGNVVLGDRVIIEPNCVIRNSVIGDDTVIRANSHIEDAKVAKGCKVGPFARLRPGAELADEAQVGNFVEMKKSRLGKGSKASHLTYLGDTQVGEYANIGAGTITCNYDGVNKALTEIGDGAFVGSNSSLVAPVSIGKNATVGAGSVITRAVADDELAVARGKQRNISGWQRPQSKKGS","length":456,"molWeight":48861,"crc64":"CF6EEFC188C99C8F","md5":"6F9DD8DE373FA87D8FF1996F50A5166C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":20},"uniParcId":"UPI0018F248F5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G8D7","uniProtkbId":"A0A8I1G8D7_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":18,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266873.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Fatty acid oxidation complex subunit alpha"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Enoyl-CoA hydratase/3-hydroxybutyryl-CoA epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"4.2.1.17"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"5.1.2.3"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"3-hydroxyacyl-CoA dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"1.1.1.35"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266873.1"}],"value":"fadJ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266873.1"}],"value":"JHC10_07940"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Catalyzes the formation of a hydroxyacyl-CoA by addition of water on enoyl-CoA. Also exhibits 3-hydroxyacyl-CoA epimerase and 3-hydroxyacyl-CoA dehydrogenase activities"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(3S)-3-hydroxybutanoyl-CoA = (3R)-3-hydroxybutanoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21760"},{"database":"ChEBI","id":"CHEBI:57315"},{"database":"ChEBI","id":"CHEBI:57316"}],"ecNumber":"5.1.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA + NAD(+) = a 3-oxoacyl-CoA + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22432"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:90726"}],"ecNumber":"1.1.1.35","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049556"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3S)-3-hydroxyacyl-CoA = a (2E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16105"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57318"},{"database":"ChEBI","id":"CHEBI:58856"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 4-saturated-(3S)-3-hydroxyacyl-CoA = a (3E)-enoyl-CoA + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20724"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58521"},{"database":"ChEBI","id":"CHEBI:137480"}],"ecNumber":"4.2.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005005"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Lipid metabolism; fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Heterotetramer of two alpha chains (FadJ) and two beta chains (FadI)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008750"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"In the N-terminal section; belongs to the enoyl-CoA hydratase/isomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007005"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"value":"In the central section; belongs to the 3-hydroxyacyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266873.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase/isomerase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00378"}]},{"type":"Domain","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":493,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase NAD binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02737"}]},{"type":"Domain","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Domain","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":703,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00725"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"Enoyl-CoA hydratase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]},{"type":"Region","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"3-hydroxyacyl-CoA dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]},{"type":"Site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]},{"type":"Site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022963"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01617"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266873.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266873.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000022","properties":[{"key":"ProteinId","value":"MBJ7266873.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494414.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000009.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G8D7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008692","properties":[{"key":"GoTerm","value":"F:3-hydroxybutyryl-CoA epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004300","properties":[{"key":"GoTerm","value":"F:enoyl-CoA hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016509","properties":[{"key":"GoTerm","value":"F:long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070403","properties":[{"key":"GoTerm","value":"F:NAD+ binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006635","properties":[{"key":"GoTerm","value":"P:fatty acid beta-oxidation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06558","properties":[{"key":"EntryName","value":"crotonase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000011","properties":[{"key":"EntryName","value":"Fatty acid oxidation complex subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000009","properties":[{"key":"EntryName","value":"Fatty oxidation complex, alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1040.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01617","properties":[{"key":"EntryName","value":"FadJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006180","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR006176","properties":[{"key":"EntryName","value":"3-OHacyl-CoA_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR006108","properties":[{"key":"EntryName","value":"3HC_DH_C"}]},{"database":"InterPro","id":"IPR008927","properties":[{"key":"EntryName","value":"6-PGluconate_DH-like_C_sf"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR018376","properties":[{"key":"EntryName","value":"Enoyl-CoA_hyd/isom_CS"}]},{"database":"InterPro","id":"IPR001753","properties":[{"key":"EntryName","value":"Enoyl-CoA_hydra/iso"}]},{"database":"InterPro","id":"IPR050136","properties":[{"key":"EntryName","value":"FA_oxidation_alpha_subunit"}]},{"database":"InterPro","id":"IPR012802","properties":[{"key":"EntryName","value":"FadJ"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF008363","properties":[{"key":"EntryName","value":"fadJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02440","properties":[{"key":"EntryName","value":"FadJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43612:SF3","properties":[{"key":"EntryName","value":"TRIFUNCTIONAL ENZYME SUBUNIT ALPHA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00725","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02737","properties":[{"key":"EntryName","value":"3HCDH_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00378","properties":[{"key":"EntryName","value":"ECH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48179","properties":[{"key":"EntryName","value":"6-phosphogluconate dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00067","properties":[{"key":"EntryName","value":"3HCDH"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00166","properties":[{"key":"EntryName","value":"ENOYL_COA_HYDRATASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQDKAFTMEVRDDGVAVVTIDVPGESMNTLKDSFAEEVGSLMNRLESDDSVKGVVFISGKPGSFIAGADINMIDGCENAVDAESLARKGQAMFDRIEQLNVPVVAAINGACLGGGLELAMACHVRICTDNSKTALGLPEVKLGLLPGSGGTQRLPELVGVQQGLTMILTGKELRAKQAKKAGLVAEVVPQSILLDVAVEHALKRKPKSTKPPLKGMSKVLEATRFGRDIIFKKAGEQAQKKAHGNYPAIDKIIQTVREGVERGREAGLDKEARSFGELAMTPESYQLRQIFFATTEMKKETGADGVEPDSVKRVGVLGGGLMGGGIAYVTAAKAGIPARIKDISEDGISNALHYSYERLNKKVKRRHMRRAELEKTMLMLSGSLDYSGFERTDVVIEAVFEDLNLKQKMVADVEEHAAESTIFATNTSSLPITQIAATAKRPEQVIGLHYFSPVDKMPLAEIITHSGTSDKTIATTVSLAKKQGKTPIVVKDGAGFYVNRILAPYMNEAARLLLAGEPIEHLDKTLVKFGFPVGPITLLDEVGIDVAAKVAPVLVKELGDRFEAPDAFDKLIDDDRKGKKNQKGFYQYGKGVKGKPVDTSVYSLLDIDPKQSKSADEIIDICLLPMLNEAAYCLQEEIIRSPRDGDIGAIFGIGFPPFLGGPFRYMDSQGLETIVNKLEKLASERGERYTPAPLLKQMVENGWSFYQ","length":708,"molWeight":76776,"crc64":"AFC26672817B4BA3","md5":"BFDADAA47A50CAD07DAA408F3867B843"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":4,"Region":2,"Site":2},"uniParcId":"UPI000C099A7F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G910","uniProtkbId":"A0A8I1G910_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":20,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267679.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267679.1"}],"value":"JHC10_12105"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059148"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"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"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267679.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":534,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":515,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":517,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":403,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267679.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267679.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000040","properties":[{"key":"ProteinId","value":"MBJ7267679.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494951.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXAWT010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G910","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"78252241","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"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":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATNYIFVTGGVVSSLGKGIAAASLAAILEARGLNVTIMKLDPYINVDPGTMSPTQHGEVFVTVDGAETDLDLGHYERFIRTRMTSSNNFTTGRVYEDIIRRERKGEFLGATIQVIPHITNEIKRRVIEGSKGFDIAIIEIGGTVGDIESQPFLEAIRQLGTEIGRDHTLFMHLTLVPFLGAAGEVKTKPTQHSVKELRSIGIQPDVLVCRSDRSLPATERSKIALFTNVEERAVIGLRDVDSIYKIPSMLKAQSLDDIVTKRFNLDCPEADLHEWEEVLYQESNPNGEVTVGFVGKYVELPDAYKSVNEALAHAGLKNRLTVNIRYIDSQDLETKGTSKLEDVDAILVPGGFGDRGIEGKLIAAKYARENNIPYLGICLGMQVAMIEFARNVAGLTGANSTEFDENCSDPVVGLITEWMDASGQKELRDKHSDLGGTMRLGSQECHLEKGSKALKMYGKETIEERHRHRYEVNNHYIEPLEKAGLKITGYSHDKQLVEILENPKHRWFVAVQFHPEFTSTPRDGHPLFKGFIEAAGEFHKERLG","length":545,"molWeight":60535,"crc64":"D824443322D80246","md5":"07664055D453556C8A634D7EA93FC16B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":16},"uniParcId":"UPI000C4F145D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G945","uniProtkbId":"A0A8I1G945_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2022-01-19","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267516.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"RecBCD enzyme subunit RecB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"3.1.11.5"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"DNA 3'-5' helicase subunit RecB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Exonuclease V subunit RecB"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"ExoV subunit RecB"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Helicase/nuclease RecBCD subunit RecB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267516.1"}],"value":"recB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267516.1"}],"value":"JHC10_11280"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.","ecNumber":"3.1.11.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Belongs to the helicase family. UvrD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267516.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"UvrD-like helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51198"}]},{"type":"Domain","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":786,"modifier":"EXACT"}},"description":"UvrD-like helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51217"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":906,"modifier":"EXACT"}},"description":"DNA-binding and helicase activity, interacts with RecC","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":937,"modifier":"EXACT"},"end":{"value":1237,"modifier":"EXACT"}},"description":"Nuclease activity, interacts with RecD and RecA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":973,"modifier":"EXACT"},"end":{"value":994,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":978,"modifier":"EXACT"},"end":{"value":987,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":1135,"modifier":"EXACT"},"end":{"value":1135,"modifier":"EXACT"}},"description":"For nuclease activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00560"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1003,"modifier":"EXACT"},"end":{"value":1003,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1122,"modifier":"EXACT"},"end":{"value":1122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1135,"modifier":"EXACT"},"end":{"value":1135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267516.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267516.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000036","properties":[{"key":"ProteinId","value":"MBJ7267516.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494838.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000015.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G945","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009338","properties":[{"key":"GoTerm","value":"C:exodeoxyribonuclease V complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008854","properties":[{"key":"GoTerm","value":"F:exodeoxyribonuclease V activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd22352","properties":[{"key":"EntryName","value":"RecB_C-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.320.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.486.10","properties":[{"key":"EntryName","value":"PCRA, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3170.10","properties":[{"key":"EntryName","value":"Recbcd, chain B, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01485","properties":[{"key":"EntryName","value":"RecB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011604","properties":[{"key":"EntryName","value":"PDDEXK-like_dom_sf"}]},{"database":"InterPro","id":"IPR038726","properties":[{"key":"EntryName","value":"PDDEXK_AddAB-type"}]},{"database":"InterPro","id":"IPR004586","properties":[{"key":"EntryName","value":"RecB"}]},{"database":"InterPro","id":"IPR011335","properties":[{"key":"EntryName","value":"Restrct_endonuc-II-like"}]},{"database":"InterPro","id":"IPR000212","properties":[{"key":"EntryName","value":"UvrD-like"}]},{"database":"InterPro","id":"IPR014016","properties":[{"key":"EntryName","value":"UvrD-like_ATP-bd"}]},{"database":"InterPro","id":"IPR014017","properties":[{"key":"EntryName","value":"UvrD-like_C"}]},{"database":"NCBIfam","id":"TIGR00609","properties":[{"key":"EntryName","value":"recB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070:SF23","properties":[{"key":"EntryName","value":"RECBCD ENZYME SUBUNIT RECB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070","properties":[{"key":"EntryName","value":"UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12705","properties":[{"key":"EntryName","value":"PDDEXK_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00580","properties":[{"key":"EntryName","value":"UvrD-helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13361","properties":[{"key":"EntryName","value":"UvrD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52980","properties":[{"key":"EntryName","value":"Restriction endonuclease-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51198","properties":[{"key":"EntryName","value":"UVRD_HELICASE_ATP_BIND"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51217","properties":[{"key":"EntryName","value":"UVRD_HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQLPSHTSGHTLENPLDFPLNSSRLIEASAGTGKTYTIAALYVRLVIGHGSHNGTEETAFERELVPKNILVMTFTKAATEELSDRIRARLAEAAAYFRDPEAVEGDPFLASLRDDCAAQGQNLMHLARLLDLASQSMDEAAVKTIHGWCQSMLKEHAFASGSLFSQDVETDNEELRLQAAEDYFRRFIYPADAELSARLLEDFKSPEALLGLTYSLSKSGQAPVNGDLHSLLKEAESAHQQRMATIKQEVAPIVQELVDKTSQAKGAATKLKQFQKFADWCADPDLVEPEATAANWKNISTDELQTFAEAKLGGMPESWTVLGELQDRIKRSKVQQQEELAKVKQHAAFWVSSRFAELQNQRAEMGHDDMLTRLRDALKGPSGEALAAAIRKQYPVAMVDEFQDTDPVQYEIFNRIYNLAEPHLGTGIFLIGDPKQAIYSFRNADIYTYLKARRDTEGRHYNLARNFRSSQAMVDGVNALFERAEELPRGAFLFKTEAENQLPFNPVGANGLKRTFKHCLLSSNLKTAPALLWSVSGEEKRNKNDFFRAAANHHANLIASLLNDPQAGYYNEDDKLEQRVKTSDMAVLVNNFNEANAIKKALSDRGLKSVYLSDRESVFAQRVAKDLLALVSACAEPRDPSLIRSALATQLLGLPLSELEHIHSHEREWEERVEQFLSYHDQWQRQGVLAMLHSLLHDHQVPAKLLEDRIHGERQLSDVLHIAELLQQQSLVLDGIPALVNHFAEQVNERHGFGSNSRTQSDEQQLRLESDDELIKIITIHKSKGLQYPLVFMPFVAYTQAETHRIKPPAVYHDENGELQVLWSKDDDNKQRLSNEILAEDLRKMYVAVTRAQYATFIALEAVKEHRNNPLFYLLNGGESLTDELYNEVSERWQQAPHTQLTRLEDDEPLVRALEQEQTTPKLTPRSMPADRKLERWWVASYSALKYEGAVTKSVQAPQSPDEMNLLDERDDDDAEVASAAEPSPDSIHHLPKGAGPGTFLHNLLEESANIGFAKIAGNAAERTELVEGFCVSPYWQEHQNSLEHWLDAYLHNQFPINGSGDRISLSALEQYKAEPEFWFGASEVNAQRLDALVHEHILPGHERPALEPNVLNGMLKGFIDLVFEHNGKYYVADYKSNWLGEDDHAYTEQAMREKILDSRYDLQYVIYTLALHRLLKARLGSDYDYDTYVGGAVYLFLRGHRAETGGAFCDRPARELIEQLDALFSGKDLSDKEPV","length":1237,"molWeight":139529,"crc64":"B78D276D752799E4","md5":"01A9FF5227C428F19FFD87A0DA21FD7D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Compositional bias":1,"Active site":1,"Binding site":4},"uniParcId":"UPI0018F1CD57"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G9A9","uniProtkbId":"A0A8I1G9A9_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":21,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266772.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"tRNA sulfurtransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"2.8.1.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"Sulfur carrier protein ThiS sulfurtransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"Thiamine biosynthesis protein ThiI"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"tRNA 4-thiouridine synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266772.1"}],"value":"thiI"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266772.1"}],"value":"JHC10_07405"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a uridine in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + ATP + H(+) = [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + 2 oxidized [2Fe-2S]-[ferredoxin] + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24176"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:13337"},{"database":"Rhea","id":"RHEA-COMP:13338"},{"database":"Rhea","id":"RHEA-COMP:13339"},{"database":"Rhea","id":"RHEA-COMP:13340"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:61963"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:136798"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.8.1.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[ThiS sulfur-carrier protein]-C-terminal Gly-Gly-AMP + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] + AH2 = [ThiS sulfur-carrier protein]-C-terminal-Gly-aminoethanethioate + L-cysteinyl-[cysteine desulfurase] + A + AMP + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43340"},{"database":"Rhea","id":"RHEA-COMP:12157"},{"database":"Rhea","id":"RHEA-COMP:12158"},{"database":"Rhea","id":"RHEA-COMP:12910"},{"database":"Rhea","id":"RHEA-COMP:19908"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:61963"},{"database":"ChEBI","id":"CHEBI:90618"},{"database":"ChEBI","id":"CHEBI:232372"},{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"Cofactor biosynthesis; thiamine diphosphate biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"Belongs to the ThiI family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266772.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"THUMP","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51165"}]},{"type":"Domain","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":482,"modifier":"EXACT"}},"description":"Rhodanese","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50206"}]},{"type":"Active site","location":{"start":{"value":457,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}]},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023284"}],"id":"KW-0676","category":"Domain","name":"Redox-active center"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022977"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"id":"KW-0784","category":"Biological process","name":"Thiamine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00021"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266772.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266772.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000020","properties":[{"key":"ProteinId","value":"MBJ7266772.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494359.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CDUKHN010000019.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G9A9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"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:0004810","properties":[{"key":"GoTerm","value":"F:CCA tRNA nucleotidyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016722","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on metal ions"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0140741","properties":[{"key":"GoTerm","value":"F:tRNA-uracil-4 sulfurtransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009229","properties":[{"key":"GoTerm","value":"P:thiamine diphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052837","properties":[{"key":"GoTerm","value":"P:thiazole biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0002937","properties":[{"key":"GoTerm","value":"P:tRNA 4-thiouridine biosynthesis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01712","properties":[{"key":"EntryName","value":"PPase_ThiI"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00158","properties":[{"key":"EntryName","value":"RHOD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd11716","properties":[{"key":"EntryName","value":"THUMP_ThiI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.2130.30","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":"Gene3D","id":"3.40.250.10","properties":[{"key":"EntryName","value":"Rhodanese-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00021","properties":[{"key":"EntryName","value":"ThiI"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023188","properties":[{"key":"EntryName","value":"DPS_DNA-bd_CS"}]},{"database":"InterPro","id":"IPR001763","properties":[{"key":"EntryName","value":"Rhodanese-like_dom"}]},{"database":"InterPro","id":"IPR036873","properties":[{"key":"EntryName","value":"Rhodanese-like_dom_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR020536","properties":[{"key":"EntryName","value":"ThiI_AANH"}]},{"database":"InterPro","id":"IPR054173","properties":[{"key":"EntryName","value":"ThiI_fer"}]},{"database":"InterPro","id":"IPR049961","properties":[{"key":"EntryName","value":"ThiI_N"}]},{"database":"InterPro","id":"IPR026340","properties":[{"key":"EntryName","value":"THII_Thiazole_biosynth_dom"}]},{"database":"InterPro","id":"IPR004114","properties":[{"key":"EntryName","value":"THUMP_dom"}]},{"database":"InterPro","id":"IPR049962","properties":[{"key":"EntryName","value":"THUMP_ThiI"}]},{"database":"InterPro","id":"IPR003720","properties":[{"key":"EntryName","value":"tRNA_STrfase"}]},{"database":"NCBIfam","id":"TIGR04271","properties":[{"key":"EntryName","value":"ThiI_C_thiazole"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00342","properties":[{"key":"EntryName","value":"tRNA uracil 4-sulfurtransferase ThiI"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43209","properties":[{"key":"EntryName","value":"TRNA SULFURTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43209:SF1","properties":[{"key":"EntryName","value":"TRNA SULFURTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00581","properties":[{"key":"EntryName","value":"Rhodanese"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02568","properties":[{"key":"EntryName","value":"ThiI"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22025","properties":[{"key":"EntryName","value":"ThiI_fer"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02926","properties":[{"key":"EntryName","value":"THUMP"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00981","properties":[{"key":"EntryName","value":"THUMP"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52821","properties":[{"key":"EntryName","value":"Rhodanese/Cell cycle control phosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF143437","properties":[{"key":"EntryName","value":"THUMP domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00819","properties":[{"key":"EntryName","value":"DPS_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50206","properties":[{"key":"EntryName","value":"RHODANESE_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51165","properties":[{"key":"EntryName","value":"THUMP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKFVVRLHAEITIKSRSVRKRYGKVLTNNLRKILAPIDDSVYAKWLWDRIEVSADGDDSEVRNQIKEVLQNTPGISWFAEVIEQPLTDFDAIAELVGEHWLQRLPGKTFAMRVKRKGHHEFNSQQLERYIGGYLLQRVPDASVNLSKPDLEIALQITNKVVHLVGERINGLGGFPIPTQETVLSLLSGGFDSGVATYEFIRRGARTHFCFFNLGGDAHEVAVRQIAYYLWKRYSASHPIKFISVDFAPIVDDILTNVENGQMGVVLKRQMLRAADKVARYVKAQALVTGEAMGQVSSQTLANLRVIDQATDALVLRPLITKDKQEIVDEAKRIGTEPLAKSIPEYCGVISNKPTVKAIPAVIEAEEAKLNKDLLDQVVQASNVLSMQDIATQTDKELELPDTTTELKSHTTIIDIRNDEEIEAAPLSVDVEVIEIPFFKLATQFAELDQSREYLLYCDQGIMSRMQALLLHENGYSNVSVYKP","length":483,"molWeight":54229,"crc64":"B5AD69C87E44D73D","md5":"5983EC011C46182C21B857A6C46F79A6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":4},"uniParcId":"UPI000C58B166"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1GAB3","uniProtkbId":"A0A8I1GAB3_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2022-01-19","entryVersion":21,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266321.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional NAD(P)H-hydrate repair enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Nicotinamide nucleotide repair protein"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"NAD(P)H-hydrate epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"5.1.99.6"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266321.1"}],"value":"JHC10_05105"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025153"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADHX = (6S)-NADHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32215"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:64075"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000013"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADPHX = (6S)-NADPHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32227"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:64077"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000909"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADHX + ADP = AMP + phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32223"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32235"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009524"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the C-terminal section; belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006001"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the N-terminal section; belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266321.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":442,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266321.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266321.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000012","properties":[{"key":"ProteinId","value":"MBJ7266321.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494049.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000005.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1GAB3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTNTDGSRYENCLYRVEQLQKGEKKAAEASAMNMMQLMSAAGKAVFKQLQRRFPAPARIAVCCGEGNNGGDGYIVARLAQEAGYQVQVFALKPNAELSDPLESDAHRARSAWREQGGNEKALLDCAPDQFDLVVDALFGVGLNRALEGDPVTWVQHVNASSTPVISVDVPSGLNADNGHVPGAAVRAHLTVSLVALKRGLLTGKAQNHTGELVLEDLGIGETFKQQNDADWFRVDAGGLGNWLPARARCTHKGEQGHVLIVGGQPGMSGAVILAMKSALRAGAGKVSVACHPDVQAIVAAAQPEAMVHSIKDEDTLKPLLRDASAIALGPGLGQSRWSHDVFSQVMKADALKVIDADGLNLLASYPARSSKLLLTPHPGEAARLLQTTADEVEADRFLAVTQLREKYGAQVLLKGAGSLLVTDRGRCLIDRGSPAMASGGMGDLLTGLISGLLAQRMAPAQALIAGALWHAMAGEEAGKDGERGTLASDLLPYIRRLVNGYGRDDD","length":506,"molWeight":53477,"crc64":"EDDB3BE0B2BB7391","md5":"B3A4B5CCA945A09DE0206AD0EF98DB1D"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI0018F27596"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1GAB6","uniProtkbId":"A0A8I1GAB6_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":20,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266886.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266886.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266886.1"}],"value":"JHC10_08005"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266886.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1074,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5048499159"},{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":678,"modifier":"EXACT"},"end":{"value":869,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":936,"modifier":"EXACT"},"end":{"value":1074,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":553,"modifier":"EXACT"}},"description":"Oligomerization domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":936,"modifier":"EXACT"},"end":{"value":1074,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":714,"modifier":"EXACT"},"end":{"value":714,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":753,"modifier":"EXACT"},"end":{"value":753,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":755,"modifier":"EXACT"},"end":{"value":755,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":760,"modifier":"EXACT"},"end":{"value":760,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":785,"modifier":"EXACT"},"end":{"value":785,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":786,"modifier":"EXACT"},"end":{"value":786,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":787,"modifier":"EXACT"},"end":{"value":787,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":788,"modifier":"EXACT"},"end":{"value":788,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":828,"modifier":"EXACT"},"end":{"value":828,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":828,"modifier":"EXACT"},"end":{"value":828,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":828,"modifier":"EXACT"},"end":{"value":828,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":840,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":840,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":840,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":840,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":840,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Binding site","location":{"start":{"value":842,"modifier":"EXACT"},"end":{"value":842,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"4"}},{"type":"Binding site","location":{"start":{"value":842,"modifier":"EXACT"},"end":{"value":842,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266886.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266886.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000022","properties":[{"key":"ProteinId","value":"MBJ7266886.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054487038.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXAWT010000003.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1GAB6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804197at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRTDIKSILILGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPEMADATYIEPIHWEVVEKIIERERPDAVLPTMGGQTALNCALDLDRHGVLERYKVEMIGANADAIDKAENRDRFDKAMKAIGLETPNAEMAHSLDEAFDVLSRLGFPCIIRPSFTMGGSGGGIAYNREEFEEICRRGLDLSPTNELLIDESLLGWKEYEMEVVRDKSDNCIIVCTIENFDPMGIHTGDSITVAPAQTLTDKEFQIMRDAAMAVLREIGVETGGSNVQFGVNPDTGRMVIIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELENEITGGRTPASFEPALDYVVTKIPRFNFEKFANCNDRLTTQMKSVGEVMAIGRNFQESMQKALRGLELGASGFDPIVEIDSKDARSKVIRELKEPGAERIWYIADAFRLGMTVREVFELTRIDEWYLIQIEELVNLEKEVDELGLAGLTSEVMTVLKRRGFADSRIADVLHVSEAEVRKKRHKFKIHPVYKRVDTCAAEFASGTAYMYSSYDEECESAPSDKDKIMVIGGGPNRIGQGIEFDYCCVHASLALREDGYETIMVNCNPETVSTDYDTSDRLYFEPITLEDVLEIVRIEKPKGVIVQYGGQTPLKLARELEANGVPIIGTSPDAIDRAEDRSRFQTAVRRLGLKQPENSTVTGFNEALTEAKRIGYPLVVRPSYVLGGRAMEIVYDEADLQRYLTDAVKVSNDAPVLLDRFLDNAVEVDVDAICDGKDVLIGGIMQHIEEAGVHSGDSACSLPPYSLSDIIQAQLREQMRKLAFELNVNGLMNAQFAVKDEEIYLIEVNPRAARTVPFVSKATGVPLAKVAARVMVGQSLQQQGYVKEIIPPYYSVKEVVIPFAKFQGVDPIRGPEMRSTGEVMGVGESFEEAYAKANLGAGEALAKKGKALISVKDSDKQRLMDLARGLLALGFSLEATRGTAKMLGEEGIDCSIVNKLQEGRPNIVDAIKNGEYSYIINTVEGRRAIEDSVYIRREALLNKVIYTTTLNAAFATVKANTADDRARVSSVQELHKRVSLI","length":1074,"molWeight":118507,"crc64":"F4C569F7434F322C","md5":"CA7EA3F41DFDEC23B33791D97470841C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Chain":1,"Domain":3,"Region":3,"Binding site":38,"Lipidation":2},"uniParcId":"UPI0006C89911"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1GBD7","uniProtkbId":"A0A8I1GBD7_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":17,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267274.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267274.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267274.1"}],"value":"JHC10_10030"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267274.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]},{"type":"Chain","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":751,"modifier":"EXACT"}},"description":"Catalase-peroxidase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"featureId":"PRO_5047561053"},{"type":"Domain","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Active site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":279,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-115)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267274.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267274.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000030","properties":[{"key":"ProteinId","value":"MBJ7267274.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494679.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_DFTL01000002.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1GBD7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.520.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF0","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFNKTVPLLSTVAIAISLSVGSGVANAQENSSYEVNSPEPKSNEFWWPNKLNLEPLRQHSPESDPYGDDFDYAEAFSQLDLEQVKKDIEELMTSDQDWWPADYGHYGPFFIRMAWHGAGTYRVQDGRGGAAGAQQRFEPLNSWPDNVSLDKARRLLWPVKQKYGRDISWADLMVLTGNVALESMGFETFGFAGGREDAWEPDIVYWGPEKEWLAGDERYSGDRELENPLAAVQMGLIYVNPEGPNGKPDPLLAAKDIRDTFGRMAMNDEETVALIAGGHTFGKAHGAHKPEDCLGAEPAAAGVEEQGLGWKNKCGKGNAEDTITSGLEGAWSVNPTAWTTQYLDNLFGFEWEQTKSPAGAIQWIPVDGQASELVPDAHVEGKRHAPIMFTTDLSLKEDPEYRKIAKRFHEDPKEFELAFAKAWFKLTHRDMGPKQRYLGDMAPQEDLLWQDPIPEVDFELINDGEIEQLKAVILDSGLSVPQLVRTAWASASSFRGTDMRGGANGARIALEPQVSWEANNPTELKKALNTLKGVQEDFNEELSGDKQVSLADVIVLGGAAAIEKAAKDAGYDVTVPFEPGRTDASQEMTDVNSFSFLEPKADAFRNYYAEGNRVPPAQHMVDKADQLTLTVPEMTVLVGGLRSLDANYDGSDHGVFTDKPGTLSNDFFVNLLSMDNEWKQSSDNEAIYEGYDRKTGEQKYTATPVDLIFGSNSELRAVAEVYAMSDADQKFVGDFVQAWTKVMQLDRFDLK","length":751,"molWeight":83294,"crc64":"A2D115F4FBD9F616","md5":"46541AA79CCDCA7EA8D9718FD4E821A1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI0018F25610"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1KGK0","uniProtkbId":"A0A8I1KGK0_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":20,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266597.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072883"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066633"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075482"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076158"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081560"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-tripeptide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramyl-tripeptide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266597.1"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266597.1"}],"value":"JHC10_06520"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050251"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266597.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266597.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266597.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266597.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000019","properties":[{"key":"ProteinId","value":"MBJ7266597.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A8I1KGK0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.90.190.20:FF:000006","properties":[{"key":"EntryName","value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"NF001123","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLAELLTMLPASFAIPDVTVSGIKLDSRQVANGDVFVAIPGYETDGRAYIDAAIDAGAVAVIAEAPGLALEHRRGAVVVGFSGVREHLSHIAGTFFGHPSEKMQLVGVTGTNGKTSVTHIMAQLAKALGTEAAVIGTTGSGLIGRLLPERHTTPDAVTVQHRLATLLAEGAELVAMEVSSHALIQRRVEALHFSAAAITNISRDHLDYHGTMENYVAAKQRLFADFGVQNRIVNADDDTLSQWHKDNLADLWISLNDSSVEPCLRATGLQFHEQGSVFQINWQGESCTVETPLLGRFNVYNLLCAVAVLLKFNKPLAEIGQACRNLLPVPGRMEAFHNKQSPLVVVDYAHTPDALHQVLSALRLHCKGRLWCVFGCGGDRDRGKRPQMGKVAADYADVVVVTDDNPRTEPAQQIIEDILTGIADKERVKVWPGRREAVIKAMQEAAQDDVVLLAGKGHEDYQVIGTQRVDYNERAVVSEWLQGDCA","length":487,"molWeight":52835,"crc64":"FACBDE6FB24382CB","md5":"56778D2F9F06662CA94C61FDE21153F2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":11,"Modified residue":1},"uniParcId":"UPI0018F1F1F3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1KGK1","uniProtkbId":"A0A8I1KGK1_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":19,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266891.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ATP-dependent zinc metalloprotease FtsH"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"3.4.24.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266891.1"}],"value":"ftsH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266891.1"}],"value":"JHC10_08030"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Multi-pass membrane protein","id":"SL-9909"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003651"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010044"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the C-terminal section; belongs to the peptidase M41 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the central section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266891.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"ATP-dependent zinc metalloprotease FtsH","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5052621638"},{"type":"Transmembrane","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":598,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":598,"modifier":"EXACT"},"end":{"value":615,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":633,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266891.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266891.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000022","properties":[{"key":"ProteinId","value":"MBJ7266891.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054487048.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXAWT010000003.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1KGK1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9809379at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004222","properties":[{"key":"GoTerm","value":"F:metalloendopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19501","properties":[{"key":"EntryName","value":"RecA-like_FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.760:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.720.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.760","properties":[{"key":"EntryName","value":"Peptidase M41"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01458","properties":[{"key":"EntryName","value":"FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR041569","properties":[{"key":"EntryName","value":"AAA_lid_3"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR003960","properties":[{"key":"EntryName","value":"ATPase_AAA_CS"}]},{"database":"InterPro","id":"IPR005936","properties":[{"key":"EntryName","value":"FtsH"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011546","properties":[{"key":"EntryName","value":"Pept_M41_FtsH_extracell"}]},{"database":"InterPro","id":"IPR000642","properties":[{"key":"EntryName","value":"Peptidase_M41"}]},{"database":"InterPro","id":"IPR037219","properties":[{"key":"EntryName","value":"Peptidase_M41-like"}]},{"database":"NCBIfam","id":"NF008004","properties":[{"key":"EntryName","value":"ftsH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01241","properties":[{"key":"EntryName","value":"FtsH_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076:SF97","properties":[{"key":"EntryName","value":"ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076","properties":[{"key":"EntryName","value":"METALLOPROTEASE M41 FTSH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17862","properties":[{"key":"EntryName","value":"AAA_lid_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06480","properties":[{"key":"EntryName","value":"FtsH_ext"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01434","properties":[{"key":"EntryName","value":"Peptidase_M41"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140990","properties":[{"key":"EntryName","value":"FtsH protease domain-like"},{"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":"PS00674","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDMAKNLILWLVIAVVLMSVFQSFSPSGTTSATMTYNEFVSQVNNGNIRRAEFGDDGRTISGMTRNGQSYKTVVPTQYDPKILDDLLANDVETQGTPPEEQSILASIFISWFPMLLLIGVWIFFMRQMQGGGGRGAMSFGKSKAKLMNEEQSKTTFKDVAGCDEAKEEVSELVDYLKDPSKFQRLGGKIPKGVLMVGPPGTGKTLLAKAISGEAKVPFFSISGSDFVEMFVGVGASRVRDMFEQAKKSAPCIIFIDELDAVGRQRGAGLGGGHDEREQTLNQMLVEMDGFEGNEGIIVIAATNRPDVLDPALLRPGRFDRQVVVGLPDVRGREQILKVHMRKVPLGDDVKPELIARGTPGFSGADLANLVNEAALFAARGDRRVVSMEEFDKAKDKIMMGAERRSMVMTDDEKAMTAYHEAGHAIVGRLVPEHDPVYKVSIIPRGRALGVTMYLPEQDRVSHSKQHLESMISSLFGGRLAEAIIFGDEKVTTGASNDIERATEIARKMVTQWGLSEKMGPLLYAEDENEVFLGRSVTQHKHMSDDTARAIDEEVKSVIDRNYQRAKKLLEENVDILHSMKDALVRYETIDADQIDDLMNRRDVRQPKDWDDRDSGGNGSDGGAAKADETEERPERPINVDKPGDATS","length":648,"molWeight":71402,"crc64":"3D828133BFCBBEB6","md5":"C72B80707F725A174269510B3EC8DB4E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":2},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":2,"Active site":1,"Binding site":4},"uniParcId":"UPI0006C86CCE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1KHY8","uniProtkbId":"A0A8I1KHY8_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":18,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266196.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266196.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266196.1"}],"value":"JHC10_04475"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266196.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-96)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266196.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266196.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000011","properties":[{"key":"ProteinId","value":"MBJ7266196.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199493978.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000005.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1KHY8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF6","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSSSGGGKCPIMHGSMTSEKKTNTHWWPNSLKLEILRQHDTKANPMDDDFNYAEEFKKINLEELKQDLKDLMTDSQDWWPADWGHYGGLMIRMAWHSAGSYRLADGRGGGGTGNQRFAPLNSWPDNVSLDKARRLLWPIKKKYGNKLSWADLFILAGNMAYESMGLKTFGFAGGREDIWHPEEDTYWGSEKEWLAETKNRYSSDDERESLENPLAAVQMGLIYVNPEGVDGNPDPLRTAKDVRETFKRMAMNDEETCALTAGGHTVGKCHGNGKEENLGPEPEAADVEEQGFGWRNSGGKGVGRDTMSSGIEGAWTTNPTQWDNGYFYLLFNYEWELKKSPAGAWQWEPVDIKEEDKPVDVEDPSIRHNPIMTDADMAMKMDPDYRKIAEKFYKDPEYFADVFARAWFKLTHRDLGPKDRYLGADVPEEDLIWQDPIPKVDYTLSETEIADLKDKLLNTGLTSYELISTAWDSARNFRCSDFRGGANGARIRLAPQKDWHGNEPEKLHKVLRVLEELQSTLDKKVSLADLIVLGGTAAVEKAVKDAGYNLTVPFAPGRGDATDEQTDVESFEPLEPLHDGYRNYLKKDYAVPAEELMLDRTHLMGLTAPEMTVLVGGMRALGANYGESKHGVFTDRAGTLTNDFFVNLTDMNNVWKKADDHYEVRDRKTDELKWTASRIDLVFGSNSILRSYSELYAQDDNQEKFVKDFVKAWTKVMNADRFDLA","length":726,"molWeight":82250,"crc64":"965CEC3A6728AEFA","md5":"FD535B7E0BBD5C7EC03350916A5D08BB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI0018F16871"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1KIU1","uniProtkbId":"A0A8I1KIU1_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":19,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267628.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267628.1"}],"value":"trmG/rlmN"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"rlmN"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267628.1"}],"value":"JHC10_11845"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267628.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267628.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267628.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000039","properties":[{"key":"ProteinId","value":"MBJ7267628.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054489338.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXAWT010000004.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1KIU1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.530:FF:000003","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000008","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"NF008396","properties":[{"key":"EntryName","value":"rlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTNAIDKKVNLLDLNREGIKEFFREMGEKPFRAEQVMKWLYHFCVDDFDEMTNLNKALREKLKQVAEIRAPEIREQQQSSDGTIKFAMTLFDGQDVETVWIPEGDRATLCVSSQVGCALECTFCSTGAQGFNRNLSVAEIIGQVWRVNQLLGAYGKTGIKPVTNVVMMGMGEPLLNLNNVVPAMELMLDDLGFGLSKRRVTLSTSGVVPALEKLRERIDVMLAISLHAPDDELRNEIVPVNKKYNIEEFLASSRRYVEQSKAQRKVTVEYVMLDHVNDSTDQAHALAKTLKDTPSKINLIPFNPFPGSDYGRSSNSRIDRFAKVLMEYGFTVMVRKTRGDDIDAACGQLVGDVIDRTKRILKRQQKQRGGEAIAVKTA","length":378,"molWeight":42500,"crc64":"6FF27D8FB71A3811","md5":"E9AFD3B5FAB2FF4CC7795C7D3BD2AB5E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI0006C8C2C1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1KJV6","uniProtkbId":"A0A8I1KJV6_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2022-01-19","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266968.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266968.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266968.1"}],"value":"JHC10_08425"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266968.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"DNA/pantothenate metabolism flavoprotein C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04127"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266968.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266968.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000023","properties":[{"key":"ProteinId","value":"MBJ7266968.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494468.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000005.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1KJV6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAQLQNKHILLGITGGIAAYKAPDLVRRLREQGAEVRVVMTDSAKAFVTPLSLQAVSGFTVSDDLLDPTAEAAMGHIELARWADIILVAPATANTIARITHGFADDLLSTLVLASKAPVVIAPAMNQQMWAATSVQKNIETLLSRGVQMIGPESGEQACGDVGYGRMSDPTQIVQALIEKQPKTPQTWQGKTFVITAGPTREAIDPVRYISNHSSGKMGYALAEAAAHAGANVILVSGPTQLATPAGVQRIDVETAEQMLNAVQQQLQQCDVFIGCAAVSDYRIAEIASQKIKKEQNDEPPQLKLVQNPDILQQVASSEKPPFTVGFAAETENLKANALRKLERKQLKMIVANDVSQTGLGFNSDSNNAIIFSQDSEQSLPTMSKHDMAVAIIDAIAKRYFDNTTPEIRAN","length":411,"molWeight":44193,"crc64":"24008434F39FD931","md5":"87271408A69F2DE51118F897D9E409CD"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":7},"uniParcId":"UPI0018F19D4F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G1Z7","uniProtkbId":"A0A8I1G1Z7_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2022-01-19","entryVersion":17,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00020605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Phosphoribosylamine--glycine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013255"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"value":"6.3.4.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00079592"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"value":"GARS"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Glycinamide ribonucleotide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042864"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Phosphoribosylglycinamide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265702.1"}],"value":"purD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265702.1"}],"value":"JHC10_01965"}]}],"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:0000256","source":"HAMAP-Rule","id":"MF_00138"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005174"},{"evidenceCode":"ECO:0000256","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:0000256","source":"ARBA","id":"ARBA00038345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"value":"Belongs to the GARS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265702.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Region","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00138"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000004","properties":[{"key":"ProteinId","value":"MBJ7265702.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199493635.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000014.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G1Z7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO: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":"FunFam","id":"3.30.470.20:FF:000031","properties":[{"key":"EntryName","value":"Phosphoribosylamine--glycine ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000006","properties":[{"key":"EntryName","value":"Phosphoribosylamine--glycine ligase, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1490.20:FF:000006","properties":[{"key":"EntryName","value":"phosphoribosylamine--glycine ligase, chloroplastic-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.600.10:FF:000001","properties":[{"key":"EntryName","value":"Trifunctional purine biosynthetic protein adenosine-3"},{"key":"MatchStatus","value":"1"}]},{"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":"MKVLVVGGGGREHALAWKAAQSQQVECVYVAPGNAGTEREPNLTNVAISAEDIECLLNFAKSEGVELTIVGPEAPLVAGIVDRFSEAGLAAFGPTAKAAQLEGSKAFSKDFLQRHNIPTADYQNFTEVEAAKAYVAEKGVPIVIKADGLAAGKGVIIAESQEQADAAIDDMLAGNRFGDAGHRVVIEEFLRGEEASFIVMVDGEHAVPFASSQDHKARDNGDKGPNTGGMGAYSPAPVVSPSIHKWVMEHVIKPTVDGMAAEGAPYKGFLYAGLMIAEDGTAKVLEYNCRFGDPETQPIMMRLKSDLVELCQQAIEGKLNQAPIDFDERAAVGVVMAAGGYPESYNKGDLIHGLPEQASENQKVFHAGTKMDDGNVVTSGGRVLCCTALGKTVTEAQQLAYQLVDKINWNDAYYRTDIAHRAIKRES","length":427,"molWeight":45552,"crc64":"B44C3463F676A16C","md5":"6A11FB1D507247401BCA3819909D8C97"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI0018F17152"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G255","uniProtkbId":"A0A8I1G255_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":19,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265937.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"2.1.1.163"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"2.1.1.201"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"2-methoxy-6-polyprenyl-1,4-benzoquinol methylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"Demethylmenaquinone methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265937.1"}],"value":"ubiE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265937.1"}],"value":"JHC10_03145"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"Methyltransferase required for the conversion of demethylmenaquinol (DMKH2) to menaquinol (MKH2) and the conversion of 2-polyprenyl-6-methoxy-1,4-benzoquinol (DDMQH2) to 2-polyprenyl-3-methyl-6-methoxy-1,4-benzoquinol (DMQH2)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2-demethylmenaquinol + S-adenosyl-L-methionine = a menaquinol + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42640"},{"database":"Rhea","id":"RHEA-COMP:9539"},{"database":"Rhea","id":"RHEA-COMP:9563"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:18151"},{"database":"ChEBI","id":"CHEBI:55437"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"}],"ecNumber":"2.1.1.163","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2-methoxy-6-(all-trans-polyprenyl)benzene-1,4-diol + S-adenosyl-L-methionine = a 5-methoxy-2-methyl-3-(all-trans-polyprenyl)benzene-1,4-diol + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28286"},{"database":"Rhea","id":"RHEA-COMP:10858"},{"database":"Rhea","id":"RHEA-COMP:10859"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:84166"},{"database":"ChEBI","id":"CHEBI:84167"}],"ecNumber":"2.1.1.201","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"Cofactor biosynthesis; ubiquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"Quinol/quinone metabolism; menaquinone biosynthesis; menaquinol from 1,4-dihydroxy-2-naphthoate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. MenG/UbiE family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265937.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"id":"KW-0474","category":"Biological process","name":"Menaquinone biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022688"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01813"}],"id":"KW-0831","category":"Biological process","name":"Ubiquinone biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265937.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265937.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000009","properties":[{"key":"ProteinId","value":"MBJ7265937.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199493793.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXBHZ010000013.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G255","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008425","properties":[{"key":"GoTerm","value":"F:2-methoxy-6-polyprenyl-1,4-benzoquinol methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043770","properties":[{"key":"GoTerm","value":"F:demethylmenaquinone methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009234","properties":[{"key":"GoTerm","value":"P:menaquinone biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.150:FF:000014","properties":[{"key":"EntryName","value":"Ubiquinone/menaquinone biosynthesis C-methyltransferase UbiE"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01813","properties":[{"key":"EntryName","value":"MenG_UbiE_methyltr"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR004033","properties":[{"key":"EntryName","value":"UbiE/COQ5_MeTrFase"}]},{"database":"InterPro","id":"IPR023576","properties":[{"key":"EntryName","value":"UbiE/COQ5_MeTrFase_CS"}]},{"database":"NCBIfam","id":"TIGR01934","properties":[{"key":"EntryName","value":"MenG_MenH_UbiE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001240","properties":[{"key":"EntryName","value":"ubiE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001242","properties":[{"key":"EntryName","value":"ubiE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001244","properties":[{"key":"EntryName","value":"ubiE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43591:SF24","properties":[{"key":"EntryName","value":"2-METHOXY-6-POLYPRENYL-1,4-BENZOQUINOL METHYLASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43591","properties":[{"key":"EntryName","value":"METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01209","properties":[{"key":"EntryName","value":"Ubie_methyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51608","properties":[{"key":"EntryName","value":"SAM_MT_UBIE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01183","properties":[{"key":"EntryName","value":"UBIE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01184","properties":[{"key":"EntryName","value":"UBIE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNDKNEESIDFGYQKVARSQKKSLVADVFQSVAAKYDVMNDLMSFGIHRLWKRYTIDCSGVRRGMKVLDIAGGTGDLTAQFSRRVGAEGEVVLADINDAMLKVGRDKLRDSGVIGNVRYVQADAEELPFDDNTFDVITIAFGLRNVTDKDRALRSMLRVLKPGGRVLILEFSKPVSATLNQVYDFYSFNILPKMGQVVANDSDSYQYLAESIRMHPDQETLKSMMSTAGYEKVDYQNMTGGVVALHRGYKF","length":251,"molWeight":28140,"crc64":"7D0CB9F943423F42","md5":"CFE192546B58263CA3BD30D3C9CC02D0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Binding site":3},"uniParcId":"UPI000C52AD20"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2C8","uniProtkbId":"A0A8I1G2C8_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2022-01-19","entryVersion":18,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265686.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00014308"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Uroporphyrinogen decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"UPD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"URO-D"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012288"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"4.1.1.37"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265686.1"}],"value":"hemE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265686.1"}],"value":"JHC10_01875"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uroporphyrinogen III + 4 H(+) = coproporphyrinogen III + 4 CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19865"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57308"},{"database":"ChEBI","id":"CHEBI:57309"}],"ecNumber":"4.1.1.37","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000554"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004804"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000554"}],"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009935"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004169"}],"value":"Belongs to the uroporphyrinogen decarboxylase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265686.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Uroporphyrinogen decarboxylase (URO-D)","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00906"}]},{"type":"Domain","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Uroporphyrinogen decarboxylase (URO-D)","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00907"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265686.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7265686.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000004","properties":[{"key":"ProteinId","value":"MBJ7265686.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054490234.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXBHZ010000019.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2C8","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9806656at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004853","properties":[{"key":"GoTerm","value":"F:uroporphyrinogen decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00717","properties":[{"key":"EntryName","value":"URO-D"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.210:FF:000001","properties":[{"key":"EntryName","value":"Uroporphyrinogen decarboxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00218","properties":[{"key":"EntryName","value":"URO_D"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR038071","properties":[{"key":"EntryName","value":"UROD/MetE-like_sf"}]},{"database":"InterPro","id":"IPR006361","properties":[{"key":"EntryName","value":"Uroporphyrinogen_deCO2ase_HemE"}]},{"database":"InterPro","id":"IPR000257","properties":[{"key":"EntryName","value":"Uroporphyrinogen_deCOase"}]},{"database":"NCBIfam","id":"TIGR01464","properties":[{"key":"EntryName","value":"hemE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21091","properties":[{"key":"EntryName","value":"METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21091:SF169","properties":[{"key":"EntryName","value":"UROPORPHYRINOGEN DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01208","properties":[{"key":"EntryName","value":"URO-D"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51726","properties":[{"key":"EntryName","value":"UROD/MetE-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00906","properties":[{"key":"EntryName","value":"UROD_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00907","properties":[{"key":"EntryName","value":"UROD_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAPALKNDRYLRALAKQPVDRTPVWMMRQAGRYLPEYKEVRAQAGDFMSLCRNTELACEVTMQPLRRFDLDAAILFSDILTIPDAMGLGLYFETGEGPKFKDPVRSMAAIKNLAVPDMEDELGYVMDAVRAIRHELNGSVPLIGFSGSPWTLATYMVEGGSTKNFSKVKQLMFADPEAMHTLLSVLAESVTQYLNAQIAAGAQSVMIFDTWGGVLSPRDYKAFSLAYMEKIVAGLTREADGRKVPVTLFTKNGGQWLEAMAATGADALGVDWTTDLGDARGRVGGQVALQGNMDPSVLYAKPERIEEEVQTILQSYGSGTGHVFNLGHGIHPEVDPEHAAAFINAIHKYSPAFHSND","length":358,"molWeight":39183,"crc64":"BC05649DE9840BFC","md5":"7BBCF957824D40F0FFD4A9BB6618C600"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":5,"Site":1},"uniParcId":"UPI0006C8AF42"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2E0","uniProtkbId":"A0A8I1G2E0_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2022-01-19","entryVersion":19,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017068"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Enolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012058"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"4.2.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"2-phospho-D-glycerate hydro-lyase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"2-phosphoglycerate dehydratase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267678.1"}],"value":"eno"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267678.1"}],"value":"JHC10_12100"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10164"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58289"},{"database":"ChEBI","id":"CHEBI:58702"}],"ecNumber":"4.2.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Binds a second Mg(2+) ion via substrate during catalysis."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-3"}],"value":"Mg(2+) is required for catalysis and for stabilizing the dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005031"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Component of the RNA degradosome, a multiprotein complex involved in RNA processing and mRNA degradation"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Fractions of enolase are present in both the cytoplasm and on the cell surface"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Secreted","id":"SL-0243"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Cell surface","id":"SL-0310"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009604"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"value":"Belongs to the enolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267678.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"Enolase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01193"}]},{"type":"Domain","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Enolase C-terminal TIM barrel","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01192"}]},{"type":"Active site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-1"}]},{"type":"Active site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-1"}]},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58289"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"ligand":{"name":"(2R)-2-phosphoglycerate","id":"ChEBI:CHEBI:58289"}},{"type":"Binding site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001400-2"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022525"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00318"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267678.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000040","properties":[{"key":"ProteinId","value":"MBJ7267678.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494950.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000024.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2E0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009986","properties":[{"key":"GoTerm","value":"C:cell surface"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000015","properties":[{"key":"GoTerm","value":"C:phosphopyruvate hydratase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004634","properties":[{"key":"GoTerm","value":"F:phosphopyruvate hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03313","properties":[{"key":"EntryName","value":"enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.120:FF:000001","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.390.10:FF:000001","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.120","properties":[{"key":"EntryName","value":"Enolase-like C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.390.10","properties":[{"key":"EntryName","value":"Enolase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00318","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000941","properties":[{"key":"EntryName","value":"Enolase"}]},{"database":"InterPro","id":"IPR036849","properties":[{"key":"EntryName","value":"Enolase-like_C_sf"}]},{"database":"InterPro","id":"IPR029017","properties":[{"key":"EntryName","value":"Enolase-like_N"}]},{"database":"InterPro","id":"IPR020810","properties":[{"key":"EntryName","value":"Enolase_C"}]},{"database":"InterPro","id":"IPR020809","properties":[{"key":"EntryName","value":"Enolase_CS"}]},{"database":"InterPro","id":"IPR020811","properties":[{"key":"EntryName","value":"Enolase_N"}]},{"database":"NCBIfam","id":"TIGR01060","properties":[{"key":"EntryName","value":"eno"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11902","properties":[{"key":"EntryName","value":"ENOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11902:SF1","properties":[{"key":"EntryName","value":"ENOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00113","properties":[{"key":"EntryName","value":"Enolase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03952","properties":[{"key":"EntryName","value":"Enolase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001400","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00148","properties":[{"key":"EntryName","value":"ENOLASE"}]},{"database":"SFLD","id":"SFLDF00002","properties":[{"key":"EntryName","value":"enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG00178","properties":[{"key":"EntryName","value":"enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00001","properties":[{"key":"EntryName","value":"Enolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01192","properties":[{"key":"EntryName","value":"Enolase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01193","properties":[{"key":"EntryName","value":"Enolase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51604","properties":[{"key":"EntryName","value":"Enolase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54826","properties":[{"key":"EntryName","value":"Enolase N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00164","properties":[{"key":"EntryName","value":"ENOLASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNIVKVIGREIMDSRGNPTVEADVYLESGHMGRAAAPSGASTGSREALELRDGDKSRYLGKGVETAVANINGAIAEALSGIDATNQDAVDNIMLKLDGTDNKEKLGANAILAVSLAVAKAAALSKGIELYEHIANLNNTSGKYSMPLPMMNILNGGEHADNNVDIQEFMIQPVGAESFKEGLRMGAEVFYALKKVLQKRGLSTAVGDEGGFAPNLASNEEALQVIVEAVENAGYKMGSDITLALDCAASEFYRDGKYELSGEGKSFTAEEFADYLAELCDRYPIISIEDGLDESDWDGWKVLTEKLGSKVQLVGDDLFVTNTRILKEGIDKSIANSILIKFNQIGSLTETLAAIAMAREAGYSAVISHRSGETEDATIADLAVGTAAGQIKTGSLCRSDRVAKYNQLLRIEGDLNGQAPYRGRQEVNAG","length":430,"molWeight":45816,"crc64":"BCF9B833F61DC983","md5":"1B914870D89248F63E7D3804DEAD8E4C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":14},"uniParcId":"UPI0018F23133"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2G7","uniProtkbId":"A0A8I1G2G7_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267515.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"RecBCD enzyme subunit RecD"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"5.6.2.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"DNA 5'-3' helicase subunit RecD"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"Exonuclease V subunit RecD"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"ExoV subunit RecD"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"Helicase/nuclease RecBCD subunit RecD"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267515.1"}],"value":"recD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267515.1"}],"value":"JHC10_11275"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit has ssDNA-dependent ATPase and 5'-3' helicase activity. When added to pre-assembled RecBC greatly stimulates nuclease activity and augments holoenzyme processivity. Negatively regulates the RecA-loading ability of RecBCD"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"value":"Belongs to the RecD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267515.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"RecBCD enzyme subunit RecD N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF21185"}]},{"type":"Domain","location":{"start":{"value":587,"modifier":"EXACT"},"end":{"value":634,"modifier":"EXACT"}},"description":"UvrD-like helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13538"}]},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01487"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267515.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267515.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000036","properties":[{"key":"ProteinId","value":"MBJ7267515.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494837.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_DFMD01000031.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2G7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009338","properties":[{"key":"GoTerm","value":"C:exodeoxyribonuclease V complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008854","properties":[{"key":"GoTerm","value":"F:exodeoxyribonuclease V activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0017116","properties":[{"key":"GoTerm","value":"F:single-stranded DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd17933","properties":[{"key":"EntryName","value":"DEXSc_RecD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18809","properties":[{"key":"EntryName","value":"SF1_C_RecD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"3"}]},{"database":"Gene3D","id":"1.10.10.1020","properties":[{"key":"EntryName","value":"RecBCD complex, subunit RecD, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01487","properties":[{"key":"EntryName","value":"RecD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050534","properties":[{"key":"EntryName","value":"1ab-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR006344","properties":[{"key":"EntryName","value":"RecD"}]},{"database":"InterPro","id":"IPR049550","properties":[{"key":"EntryName","value":"RecD_N"}]},{"database":"InterPro","id":"IPR041851","properties":[{"key":"EntryName","value":"RecD_N_sf"}]},{"database":"InterPro","id":"IPR027785","properties":[{"key":"EntryName","value":"UvrD-like_helicase_C"}]},{"database":"NCBIfam","id":"TIGR01447","properties":[{"key":"EntryName","value":"recD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43788:SF6","properties":[{"key":"EntryName","value":"DNA HELICASE B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43788","properties":[{"key":"EntryName","value":"DNA2/NAM7 HELICASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13245","properties":[{"key":"EntryName","value":"AAA_19"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21185","properties":[{"key":"EntryName","value":"RecD_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13538","properties":[{"key":"EntryName","value":"UvrD_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTEVTSNTLFDALREWRDTGWIRSIDLAFVEFLQQAGETRSDVLLAALCASHEAGRGHTSIDIKALQNEPESVLNLPPENRYSPNCDTPSALFRQFGTDVEAALTQSHCVDADGKGNQPLVLSGGKLYLRRYWQYEAFIESDLQARMRDRPITNDDLLKSTLAKLFDKAEDEKTDDINWQRVACANTVRNRFSVITGGPGTGKTYTVVRLLTALQHQTLFLGLPPLRVSLAAPTGKAAARLTESIESELNTLRGDAKLATLKDALDAIKPEGKTLHRLLGVKPNSRAFKHHADNPLRTDVVIVDEASMIDIEMMTALLKATPKNARLVLIGDKDQLASVEAGAVLGNLCEGADEGHYHTEIAQWLQQVADTPAFPSDLIDDSGKQRLQHVVKFRKSYRFKGPIADLANAINRQDNVATKQELEKAKSAGEDYPVSLYEVSSLDDPAFEALVKRNLTASGSLTFHVRTNTETTNDANNINDIAQEALQNLSNFQILTALREGPWGVKAVNQKVGDILGVNANTWYEGRPVMVTKNDYGLKLNNGDIGLTFKDPEHGHLRVAFPDQANKSENKGVRWVLPSRLTHIETVYAMTVHKSQGSEFKHTVMVLPDHDSPVLSKELLYTGITRAKERLSLVGVTKVENR","length":642,"molWeight":70989,"crc64":"84D6EDB9BD3E64D3","md5":"70DF7F36494A43A90489C6813756BAB0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":1},"uniParcId":"UPI000C51F9E8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2N0","uniProtkbId":"A0A8I1G2N0_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266401.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"value":"Argininosuccinate lyase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"value":"ASAL"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"value":"4.3.2.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"value":"Arginosuccinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266401.1"}],"value":"argH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266401.1"}],"value":"JHC10_05505"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-(N(omega)-L-arginino)succinate = fumarate + L-arginine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24020"},{"database":"ChEBI","id":"CHEBI:29806"},{"database":"ChEBI","id":"CHEBI:32682"},{"database":"ChEBI","id":"CHEBI:57472"}],"ecNumber":"4.3.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000985"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24292"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"}],"ecNumber":"2.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048372"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004941"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR036456"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine from L-ornithine and carbamoyl phosphate: step 3/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004925"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR036456"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"value":"Belongs to the lyase 1 family. Argininosuccinate lyase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060819"}],"value":"In the C-terminal section; belongs to the acetyltransferase family. ArgA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005552"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR036456"}],"value":"In the N-terminal section; belongs to the lyase 1 family. Argininosuccinate lyase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266401.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":458,"modifier":"EXACT"},"end":{"value":608,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51186"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR036456"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00006"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR036456"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266401.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266401.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000015","properties":[{"key":"ProteinId","value":"MBJ7266401.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494109.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000020.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2N0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016407","properties":[{"key":"GoTerm","value":"F:acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004056","properties":[{"key":"GoTerm","value":"F:argininosuccinate lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01359","properties":[{"key":"EntryName","value":"Argininosuccinate_lyase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04301","properties":[{"key":"EntryName","value":"NAT_SF"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.40.30:FF:000001","properties":[{"key":"EntryName","value":"Argininosuccinate lyase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.200.10:FF:000006","properties":[{"key":"EntryName","value":"Argininosuccinate lyase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.40.30","properties":[{"key":"EntryName","value":"Fumarase/aspartase (C-terminal domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.200.10","properties":[{"key":"EntryName","value":"Fumarase/aspartase (Central domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.275.10","properties":[{"key":"EntryName","value":"Fumarase/aspartase (N-terminal domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00006","properties":[{"key":"EntryName","value":"Arg_succ_lyase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR029419","properties":[{"key":"EntryName","value":"Arg_succ_lyase_C"}]},{"database":"InterPro","id":"IPR009049","properties":[{"key":"EntryName","value":"Argininosuccinate_lyase"}]},{"database":"InterPro","id":"IPR011244","properties":[{"key":"EntryName","value":"ASAL_AGS_AcTrfase"}]},{"database":"InterPro","id":"IPR024083","properties":[{"key":"EntryName","value":"Fumarase/histidase_N"}]},{"database":"InterPro","id":"IPR022761","properties":[{"key":"EntryName","value":"Fumarate-Lyase-like_N"}]},{"database":"InterPro","id":"IPR020557","properties":[{"key":"EntryName","value":"Fumarate_lyase_CS"}]},{"database":"InterPro","id":"IPR000362","properties":[{"key":"EntryName","value":"Fumarate_lyase_fam"}]},{"database":"InterPro","id":"IPR000182","properties":[{"key":"EntryName","value":"GNAT_dom"}]},{"database":"InterPro","id":"IPR008948","properties":[{"key":"EntryName","value":"L-Aspartase-like"}]},{"database":"NCBIfam","id":"NF008964","properties":[{"key":"EntryName","value":"argH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00838","properties":[{"key":"EntryName","value":"argH"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43814","properties":[{"key":"EntryName","value":"ARGININOSUCCINATE LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43814:SF1","properties":[{"key":"EntryName","value":"ARGININOSUCCINATE LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00583","properties":[{"key":"EntryName","value":"Acetyltransf_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14698","properties":[{"key":"EntryName","value":"ASL_C2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00206","properties":[{"key":"EntryName","value":"Lyase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF036456","properties":[{"key":"EntryName","value":"ASAL_AGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00145","properties":[{"key":"EntryName","value":"ARGSUCLYASE"}]},{"database":"PRINTS","id":"PR00149","properties":[{"key":"EntryName","value":"FUMRATELYASE"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48557","properties":[{"key":"EntryName","value":"L-aspartase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00163","properties":[{"key":"EntryName","value":"FUMARATE_LYASES"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51186","properties":[{"key":"EntryName","value":"GNAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALWGGRFAAGPDAAFQQFNDSLPFDYVLAEQDITGSKVWANALHKVGVLNRDECQQLKQALSELLSEVREDPTAVAVGGDEDIHSFVEAALIAKVGDLAKKLHTGRSRNDQVATDLRLWCREQVGVLQQSLKQTQQALLDLAQREKDTVIPGYTHLQRAQPVLLAHWCLAYVEMLQRDSERLQDATDRLNKSPLGCGALAGTAYAVDREAIASELGFSEATRNSLDSVSDRDFVVELLSIASLSMLHLSRLAEDLIFYNSGEAGFIELADNVTSGSSLMPQKKNPDALELVRGKSGRVVGSLTGLMMTLKALPLAYNKDMQEDKEGLFDAFTTWQASLAMVTSSLNGLTVNHEACCKAAQGGYANATELADYMVSKGIPFRQAHHNVGELVQQAIQAKKPLEDMPLEAFQAVAPVIEQDVYDWLTLDALLEKRCALGGTSPQRVNEALKAAQQQQQIQVRDANLGDIGAILDLVQHWAGAGENLPRAKDDIVHSINEFAVTEVDGKVMGCASLYIYTTGLAEIRSLGVNPKTEVRGQGRMLVAYLLKKARLLQLNRVIVLTRVPDFFEQRGFSHCSKDTLPEKVMKDCEICPRLANCDELAMEYHLEQPNEQLIFRSSC","length":620,"molWeight":68199,"crc64":"3330C94B3355D28D","md5":"5CA967C8909BC96845715923942088F5"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0018F22F0D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2N7","uniProtkbId":"A0A8I1G2N7_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267822.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Bifunctional aspartokinase/homoserine dehydrogenase"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Aspartokinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"2.7.2.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Homoserine dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"1.1.1.3"}]}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267822.1"}],"value":"JHC10_12835"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate + ATP = 4-phospho-L-aspartate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23776"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57535"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-homoserine + NAD(+) = L-aspartate 4-semialdehyde + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15757"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57476"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:537519"}],"ecNumber":"1.1.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049031"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:15759"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049031"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-homoserine + NADP(+) = L-aspartate 4-semialdehyde + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15761"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57476"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:537519"}],"ecNumber":"1.1.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048841"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:15763"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048841"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"a metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001920"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:25213"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004766"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004986"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005062"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 3/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005139"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005056"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"In the C-terminal section; belongs to the homoserine dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"value":"In the N-terminal section; belongs to the aspartokinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267822.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"Aspartate/glutamate/uridylate kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00696"}]},{"type":"Domain","location":{"start":{"value":462,"modifier":"EXACT"},"end":{"value":594,"modifier":"EXACT"}},"description":"Aspartate/homoserine dehydrogenase NAD-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03447"}]},{"type":"Domain","location":{"start":{"value":608,"modifier":"EXACT"},"end":{"value":802,"modifier":"EXACT"}},"description":"Homoserine dehydrogenase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00742"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267822.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"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":"ARBA00023027"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023053"}],"id":"KW-0915","category":"Ligand","name":"Sodium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022697"}],"id":"KW-0791","category":"Biological process","name":"Threonine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000727"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267822.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267822.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000047","properties":[{"key":"ProteinId","value":"MBJ7267822.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199495059.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000013.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2N7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0004072","properties":[{"key":"GoTerm","value":"F:aspartate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004412","properties":[{"key":"GoTerm","value":"F:homoserine dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009090","properties":[{"key":"GoTerm","value":"P:L-homoserine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009088","properties":[{"key":"GoTerm","value":"P:L-threonine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04257","properties":[{"key":"EntryName","value":"AAK_AK-HSDH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.360.10:FF:000006","properties":[{"key":"EntryName","value":"Bifunctional aspartokinase/homoserine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1160.10","properties":[{"key":"EntryName","value":"Acetylglutamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.1320","properties":[{"key":"EntryName","value":"Aspartokinase, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036393","properties":[{"key":"EntryName","value":"AceGlu_kinase-like_sf"}]},{"database":"InterPro","id":"IPR049638","properties":[{"key":"EntryName","value":"AK-HD"}]},{"database":"InterPro","id":"IPR041743","properties":[{"key":"EntryName","value":"AK-HSDH_N"}]},{"database":"InterPro","id":"IPR001048","properties":[{"key":"EntryName","value":"Asp/Glu/Uridylate_kinase"}]},{"database":"InterPro","id":"IPR005106","properties":[{"key":"EntryName","value":"Asp/hSer_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR042199","properties":[{"key":"EntryName","value":"AsparK_Bifunc_asparK/hSer_DH"}]},{"database":"InterPro","id":"IPR018042","properties":[{"key":"EntryName","value":"Aspartate_kinase_CS"}]},{"database":"InterPro","id":"IPR011147","properties":[{"key":"EntryName","value":"Bifunc_Aspkin/hSer_DH"}]},{"database":"InterPro","id":"IPR001342","properties":[{"key":"EntryName","value":"HDH_cat"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF007003","properties":[{"key":"EntryName","value":"metL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43070","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43070:SF5","properties":[{"key":"EntryName","value":"HOMOSERINE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00696","properties":[{"key":"EntryName","value":"AA_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00742","properties":[{"key":"EntryName","value":"Homoserine_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03447","properties":[{"key":"EntryName","value":"NAD_binding_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000727","properties":[{"key":"EntryName","value":"ThrA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53633","properties":[{"key":"EntryName","value":"Carbamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00324","properties":[{"key":"EntryName","value":"ASPARTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTTQLTEEQKQAVADSVQVHKFGGSSLADAFCYRRVARIVTEYAGASDLVVVSAAGDTTNRILAIINAKPQPGDTASILLDQLENFQQGLITELLSGDLQQQLLQQSQQDFTRWRRWLAGDEDIAHNAELLSYGELWSARLLSALLQKQGTRADHIDARDFLLAADAPEPVIQVEHSREKLLLRVAPHSGTRFIVTGFIARGLNGESLTLGRNGSDYSATLVGSLLDARQVTIWKDVAGVYSADPRKVERVVSLPTLDWTEAEELARLGSPVLHPRTFQPVDRQRMVISVRSSLKVENQQTRIGQFQNTQPRGKVFTSLSEVVLFKVELQDKALVKRLDELELEPLVSWTEPENHQQYLVFHQNHLDYLTGWLDSLDAGDAITQIRGYSMVAIVGNRIQETDQFSTFKLQLSEQKVRRFALTQNGDSAVAILEQKLDNRLLNRLHSQLFNYRRSLGVLVIGRGNIGTAWLELFRQQRDRINQVMDVRVIGIANSRRLWLDYNGVELTQWADDFDRLARPYVLTELLRELPNAPYDELVVIDLTDAKQVAQLYPSLFANGLHIISANKRAGSADEALYREIRTIQHEYEREWLYNTTVGAGLPLNYAINDLRNSGDEIRSISGIFSGTMSWLFENFTKGVAFSSLVKEAKERGYSEPDPREDLSCQDLVRKLLILAREIGLNLDWQDIQVQSLVPENLRDIPLKDFMQRISELDEPMAAMLDEAAKDGKVPRLLASFTVSDEQRVTAQVGIEYIPEGDMLANLIPGENIFVIYTDWYSEMPLVISGPGAGKHVTAGGVQSDLNQLLGKLAVGA","length":813,"molWeight":91246,"crc64":"E32735F91259D0F5","md5":"C1F22566F42BFC48091CFBC3D9FBAE2A"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0018F215C4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2Q0","uniProtkbId":"A0A8I1G2Q0_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":17,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"Membrane-bound lytic murein transglycosylase F"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"4.2.2.n1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"Murein lyase F"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266371.1"}],"value":"mltF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266371.1"}],"value":"JHC10_05355"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"Murein-degrading enzyme that degrades murein glycan strands and insoluble, high-molecular weight murein sacculi, with the concomitant formation of a 1,6-anhydromuramoyl product. Lytic transglycosylases (LTs) play an integral role in the metabolism of the peptidoglycan (PG) sacculus. Their lytic action creates space within the PG sacculus to allow for its expansion as well as for the insertion of various structures such as secretion systems and flagella"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Exolytic cleavage of the (1->4)-beta-glycosidic linkage between N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc) residues in peptidoglycan, from either the reducing or the non-reducing ends of the peptidoglycan chains, with concomitant formation of a 1,6-anhydrobond in the MurNAc residue.","ecNumber":"4.2.2.n1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}]}},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"Attached to the inner leaflet of the outer membrane"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"Cell outer membrane","id":"SL-0040"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"The N-terminal domain does not have lytic activity and probably modulates enzymatic activity. The C-terminal domain is the catalytic active domain"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007734"}],"value":"Belongs to the transglycosylase Slt family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"In the C-terminal section; belongs to the transglycosylase Slt family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"In the N-terminal section; belongs to the bacterial solute-binding protein 3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266371.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}]},{"type":"Chain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"Membrane-bound lytic murein transglycosylase F","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5047559089"},{"type":"Domain","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"Solute-binding protein family 3/N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00062"}]},{"type":"Region","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"LT domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}]},{"type":"Active site","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10071"}]},{"type":"Lipidation","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023237"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"id":"KW-0998","category":"Cellular component","name":"Cell outer membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02016"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7266371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000015","properties":[{"key":"ProteinId","value":"MBJ7266371.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199494087.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAEMOO010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2Q0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009279","properties":[{"key":"GoTerm","value":"C:cell outer membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008933","properties":[{"key":"GoTerm","value":"F:peptidoglycan lytic transglycosylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016998","properties":[{"key":"GoTerm","value":"P:cell wall macromolecule catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000270","properties":[{"key":"GoTerm","value":"P:peptidoglycan metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd13403","properties":[{"key":"EntryName","value":"MLTF-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01009","properties":[{"key":"EntryName","value":"PBP2_YfhD_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.530.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_02016","properties":[{"key":"EntryName","value":"MltF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023346","properties":[{"key":"EntryName","value":"Lysozyme-like_dom_sf"}]},{"database":"InterPro","id":"IPR023703","properties":[{"key":"EntryName","value":"MltF"}]},{"database":"InterPro","id":"IPR001638","properties":[{"key":"EntryName","value":"Solute-binding_3/MltF_N"}]},{"database":"InterPro","id":"IPR000189","properties":[{"key":"EntryName","value":"Transglyc_AS"}]},{"database":"InterPro","id":"IPR008258","properties":[{"key":"EntryName","value":"Transglycosylase_SLT_dom_1"}]},{"database":"NCBIfam","id":"NF008112","properties":[{"key":"EntryName","value":"mltF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR35936","properties":[{"key":"EntryName","value":"MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR35936:SF32","properties":[{"key":"EntryName","value":"MEMBRANE-BOUND LYTIC MUREIN TRANSGLYCOSYLASE F"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00497","properties":[{"key":"EntryName","value":"SBP_bac_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01464","properties":[{"key":"EntryName","value":"SLT"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00062","properties":[{"key":"EntryName","value":"PBPb"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53955","properties":[{"key":"EntryName","value":"Lysozyme-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00922","properties":[{"key":"EntryName","value":"TRANSGLYCOSYLASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKSAVSLFVLLLLAVSLITACSPQTRPDAMTVVKERQVLRVGTLMNPTSYYFDHDREQGFEYDLAKRFADRLGVELEMVPRFDVNDLFTMLRRGEIDIVAAGIDRTSTRARLFRFGPPYDVISQKVVFKQGSRQRPRDLQQITDGEIVVVEGSSHHEFLKSLGDSIPTLNWRATRDHDAVELLQMVINEEIDYTITDSTALDIQRRFHPDLSVAFTVKHDQDIAWALPQGEDDSLFSAVVEYFGEIRASGRLAHIKEQHFGHVKQFNYVTTSLFIEAVDKILPIYQETFKEHSGSLDWRLLAAISYQESLWNPRAVSPTGVRGMMMLTLPTAKAMGVKSRLNAEQSIRGGARYLERMLNRVPARIPQPDRTWFALAAYNIGFGHLEDARIITERQGGNPDRWVDVKKRLPLLRQKQFYRHTRYGFARGDEPVTYVGNIRRFYDTLKYLDEQGRL","length":455,"molWeight":52228,"crc64":"99753641821D8DCD","md5":"E750B8E2A25EA661510DBE075F2C12AF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":3,"CAUTION":2},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Region":1,"Active site":1,"Lipidation":2},"uniParcId":"UPI0018F16B9B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2Q5","uniProtkbId":"A0A8I1G2Q5_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":18,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267852.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00021726"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Phospholipase A1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013179"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"3.1.1.32"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013278"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"3.1.1.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Phosphatidylcholine 1-acylhydrolase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267852.1"}],"value":"JHC10_12985"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15801"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28868"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:58168"}],"ecNumber":"3.1.1.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001604"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18689"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28868"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:57875"}],"ecNumber":"3.1.1.32","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000111"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer. The Ca(2+) ion may have a role in catalysis."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011702"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Homodimer; dimerization is reversible, and the dimeric form is the active one"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"One of the very few enzymes located there"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Cell outer membrane","id":"SL-0040"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010525"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Belongs to the phospholipase A1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267852.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}]},{"type":"Chain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Phospholipase A1","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"featureId":"PRO_5047585026"},{"type":"Active site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-1"}]},{"type":"Active site","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-1"}]},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023237"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0998","category":"Cellular component","name":"Cell outer membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022963"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022452"}],"id":"KW-1134","category":"Domain","name":"Transmembrane beta strand"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267852.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267852.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000047","properties":[{"key":"ProteinId","value":"MBJ7267852.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_199495088.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CDUKHN010000009.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2Q5","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009279","properties":[{"key":"GoTerm","value":"C:cell outer membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004623","properties":[{"key":"GoTerm","value":"F:A2-type glycerophospholipase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008970","properties":[{"key":"GoTerm","value":"F:glycerophospholipid phospholipase A1 activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006629","properties":[{"key":"GoTerm","value":"P:lipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00541","properties":[{"key":"EntryName","value":"OMPLA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.230.10","properties":[{"key":"EntryName","value":"Phospholipase A1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003187","properties":[{"key":"EntryName","value":"PLipase_A1"}]},{"database":"InterPro","id":"IPR036541","properties":[{"key":"EntryName","value":"PLipase_A1_sf"}]},{"database":"PANTHER","id":"PTHR40457","properties":[{"key":"EntryName","value":"PHOSPHOLIPASE A1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR40457:SF1","properties":[{"key":"EntryName","value":"PHOSPHOLIPASE A1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02253","properties":[{"key":"EntryName","value":"PLA1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01486","properties":[{"key":"EntryName","value":"PHPHLIPASEA1"}]},{"database":"SUPFAM","id":"SSF56931","properties":[{"key":"EntryName","value":"Outer membrane phospholipase A (OMPLA)"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRKWIWIFATGVSAIAVNVQAQELSNMQQCLLGKMNDANAEVTIADVRAQCEEELRSAEDEDIVEVDAVEQPGALTNRMKSEQVTQFDPYVLTPHRRNYLLPVITSNNINREQYASVDGYEQNLEDYEAKFQFSFKVPFNRESLLFEEDKLFFGLTVQSWWQVYSDDISKPFRETNYMPEIFYATPTGWHPFGTNTGVVFGAEHLSNGRSQPLSRSWNRFYAQFFVEKGRFVFSLKPWIRLQENRKTDPMQSSGDDNPNITDYVGDYEFTTAYSDGDFEYILRLRHAIDTGRGSAELNWTFPIGGKFIGYTSIFTGYGESLIDYNHKQTRFGIGIALNNIL","length":341,"molWeight":39292,"crc64":"C5BFBE721D5C4850","md5":"5DB3D19E6FB0F46B17052DA20F6CFC88"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Active site":2,"Binding site":4},"uniParcId":"UPI000C0AF30E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A8I1G2T1","uniProtkbId":"A0A8I1G2T1_9GAMM","entryAudit":{"firstPublicDate":"2022-01-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2022-01-19","entryVersion":19,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Idiomarina abyssalis","taxonId":86102,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267544.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Alteromonadales","Idiomarinaceae","Idiomarina"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Porphobilinogen deaminase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"PBG"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"2.5.1.61"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Hydroxymethylbilane synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"HMBS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Pre-uroporphyrinogen synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267544.1"}],"value":"hemC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267544.1"}],"value":"JHC10_11420"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002869"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13185"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57845"},{"database":"ChEBI","id":"CHEBI:58126"}],"ecNumber":"2.5.1.61","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048169"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"dipyrromethane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60342"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Binds 1 dipyrromethane group covalently."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004735"}],"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"The porphobilinogen subunits are added to the dipyrromethane group"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005638"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Belongs to the HMBS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267544.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01379"}]},{"type":"Domain","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03900"}]},{"type":"Modified residue","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"S-(dipyrrolylmethanemethyl)cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CTMHDEC1PE3UV","citationType":"submission","authors":["Kiel Reese B.","Mullis M.","Weisend R.E."],"title":"Draft Genomes of Bacterial Isolates from North Pond Shallow Sediments.","publicationDate":"SEP-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267544.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}],"value":"KJE-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBJ7267544.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000655994"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAEMOS010000036","properties":[{"key":"ProteinId","value":"MBJ7267544.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_054490495.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CAXBHZ010000006.1"}]},{"database":"AlphaFoldDB","id":"A0A8I1G2T1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9810298at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000655994","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004418","properties":[{"key":"GoTerm","value":"F:hydroxymethylbilane synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd13646","properties":[{"key":"EntryName","value":"PBP2_EcHMBS_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.160.40:FF:000002","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.190.10:FF:000004","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.190.10:FF:000005","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.160.40","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00260","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000860","properties":[{"key":"EntryName","value":"HemC"}]},{"database":"InterPro","id":"IPR022419","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_cofac_BS"}]},{"database":"InterPro","id":"IPR022417","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_N"}]},{"database":"InterPro","id":"IPR022418","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C"}]},{"database":"InterPro","id":"IPR036803","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C_sf"}]},{"database":"NCBIfam","id":"TIGR00212","properties":[{"key":"EntryName","value":"hemC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557:SF0","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01379","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03900","properties":[{"key":"EntryName","value":"Porphobil_deamC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001438","properties":[{"key":"EntryName","value":"4pyrrol_synth_OHMeBilane_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00151","properties":[{"key":"EntryName","value":"PORPHBDMNASE"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54782","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00533","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN_DEAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQRVRIATRKSKLALWQAEHIQQRLEELHPGLSVELVPMSTKGDVILDTPLAKIGGKGLFVKELEVAMLEGRADIAVHSMKDLPVEFPPGLELHTICEREDPRDAFVSNNYKNLNELPEGAVVGTCSLRRRCQVKEQFPHLVIKDLRGNVQTRLRKLDDSEFDAIILAASGLIRLELGDRITSFIPVEQSLPANGQGALGIECRSDDDEMKALLAPLQCQETRTRVLAERAMNRGLDGGCQVPIGAYAELEGDNVYLRGLVGEPDGGKVLRDEVRGPASKAEELGSELAERLLKQGAAEILSAVYDSESSQS","length":313,"molWeight":34340,"crc64":"D99D433098951141","md5":"7DBADAFC4AC68DC10EF18F159BE135C4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Modified residue":1},"uniParcId":"UPI0006C8779E"}}]}