{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"O31246","uniProtkbId":"NERA_AGRRD","entryAudit":{"firstPublicDate":"2026-09-02","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1998-01-01","entryVersion":88,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Nitroglycerin reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}],"value":"1.7.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9401040"}],"value":"Glycerol trinitrate reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9401040"}],"value":"GTN reductase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9401040"}],"value":"Nitrate ester reductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"9401040"}],"value":"nerA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}],"value":"Nitroglycerin reductase, which enables A.radiobacter to utilize nitroglycerin (also known as glycerol trinitrate, GTN) and related explosives as sources of nitrogen for growth (PubMed:9401040). It catalyzes the NADH-dependent denitration of nitroglycerin, releasing nitrite (PubMed:14996811, PubMed:9401040). The main product is 1,3-dinitroglycerol, but it can also form small amounts of 1,2-dinitroglycerol (PubMed:9401040). It is also active on pentaerythritol tetranitrate (PETN), and, very weakly, on isosorbide dinitrate (ISDN) and ethyleneglycol dinitrate (EGDN) (PubMed:9401040). It is inactive on isopropyl nitrate (IPN), hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), 2,4,6-trinitrotoluene (TNT), ammonium ions, nitrate or nitrite (PubMed:9401040). The specific activity with NADPH is approximately 11-fold lower than with NADH (PubMed:9401040). The reduction of nitroglycerin by NADH operates via a ping-pong mechanism (PubMed:14996811)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"nitroglycerin + NADH = 1,3-dinitroglycerol + nitrite + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:80155"},{"database":"ChEBI","id":"CHEBI:16301"},{"database":"ChEBI","id":"CHEBI:18921"},{"database":"ChEBI","id":"CHEBI:28787"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:80156"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"nitroglycerin + NADH = 1,2-dinitroglycerol + nitrite + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:80159"},{"database":"ChEBI","id":"CHEBI:16301"},{"database":"ChEBI","id":"CHEBI:18898"},{"database":"ChEBI","id":"CHEBI:28787"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:80160"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}],"value":"The enzyme does not require any metal cofactors"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":22.7,"unit":"uM","substrate":"nitroglycerin","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}]},{"constant":705.0,"unit":"uM","substrate":"nitroglycerin","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"}]},{"constant":8.0,"unit":"uM","substrate":"NADH","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}],"value":"kcat is 487 min(-1) (PubMed:9401040). kcat is 8.8 sec(-1) (PubMed:14996811)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}],"value":"Optimum pH is 6.5."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}],"value":"Optimum temperature is 35 degrees Celsius."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the NADH:flavin oxidoreductase/NADH oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"9401040"}]},{"type":"Chain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"Nitroglycerin reductase","featureId":"PRO_0000464723"},{"type":"Active site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P42593"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"23606302"},{"evidenceCode":"ECO:0000269","source":"PubMed","id":"28485453"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Mutagenesis","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Binds FMN but abolishes activity toward nitroglycerin.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"Does not bind FMN. Abolishes activity toward nitroglycerin.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"}],"alternativeSequence":{"originalSequence":"N","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Active protein with the same kcat as that of wild-type enzyme but with altered KM values for nitroglycerin and NADH.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"14996811"}],"alternativeSequence":{"originalSequence":"Y","alternativeSequences":["F"]}}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"id":"KW-0288","category":"Ligand","name":"FMN"},{"id":"KW-0521","category":"Ligand","name":"NADP"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"}],"references":[{"referenceNumber":1,"citation":{"id":"9401040","citationType":"journal article","authors":["Snape J.R.","Walkley N.A.","Morby A.P.","Nicklin S.","White G.F."],"citationCrossReferences":[{"database":"PubMed","id":"9401040"},{"database":"DOI","id":"10.1128/jb.179.24.7796-7802.1997"}],"title":"Purification, properties, and sequence of glycerol trinitrate reductase from Agrobacterium radiobacter.","publicationDate":"1997","journal":"J. Bacteriol.","firstPage":"7796","lastPage":"7802","volume":"179"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 2-36","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"],"evidences":[{"evidenceCode":"ECO:0000312","source":"EMBL","id":"CAA74280.1"}]},{"referenceNumber":2,"citation":{"id":"14996811","citationType":"journal article","authors":["Marshall S.J.","Krause D.","Blencowe D.K.","White G.F."],"citationCrossReferences":[{"database":"PubMed","id":"14996811"},{"database":"DOI","id":"10.1128/jb.186.6.1802-1810.2004"}],"title":"Characterization of glycerol trinitrate reductase (NerA) and the catalytic role of active-site residues.","publicationDate":"2004","journal":"J. Bacteriol.","firstPage":"1802","lastPage":"1810","volume":"186"},"referencePositions":["FUNCTION","COFACTOR","BIOPHYSICOCHEMICAL PROPERTIES","MUTAGENESIS OF HIS-178; ASN-181 AND TYR-183"]},{"referenceNumber":3,"citation":{"id":"23606302","citationType":"journal article","authors":["Oberdorfer G.","Binter A.","Wallner S.","Durchschein K.","Hall M.","Faber K.","Macheroux P.","Gruber K."],"citationCrossReferences":[{"database":"PubMed","id":"23606302"},{"database":"DOI","id":"10.1002/cbic.201300136"}],"title":"The structure of glycerol trinitrate reductase NerA from Agrobacterium radiobacter reveals the molecular reason for nitro- and ene-reductase activity in OYE homologues.","publicationDate":"2013","journal":"ChemBioChem","firstPage":"836","lastPage":"845","volume":"14"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEXES WITH FMN; 1-NITRO-2-PHENYLPROPENE AND INHIBITOR 4-HYDROXYBENZALDEHYDE","COFACTOR","SUBUNIT"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIC"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIP"},{"evidenceCode":"ECO:0007744","source":"PDB","id":"4JIQ"}]},{"referenceNumber":4,"citation":{"id":"28485453","citationType":"journal article","authors":["Waller J.","Toogood H.S.","Karuppiah V.","Rattray N.J.W.","Mansell D.J.","Leys D.","Gardiner J.M.","Fryszkowska A.","Ahmed S.T.","Bandichhor R.","Reddy G.P.","Scrutton N.S."],"citationCrossReferences":[{"database":"PubMed","id":"28485453"},{"database":"DOI","id":"10.1039/c7ob00163k"}],"title":"Structural insights into the ene-reductase synthesis of profens.","publicationDate":"2017","journal":"Org. Biomol. Chem.","firstPage":"4440","lastPage":"4448","volume":"15"},"referencePositions":["X-RAY CRYSTALLOGRAPHY IN COMPLEX WITH FMN AND INACTIVE SUBSTRATE 2-PHENYLACRYLIC ACID","COFACTOR","SUBUNIT"],"evidences":[{"evidenceCode":"ECO:0007744","source":"PDB","id":"5N6G"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"Y13942","properties":[{"key":"ProteinId","value":"CAA74280.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"4JIC","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.60 A"},{"key":"Chains","value":"A/B/C=1-371"}]},{"database":"PDB","id":"4JIP","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.29 A"},{"key":"Chains","value":"A=1-371"}]},{"database":"PDB","id":"4JIQ","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.49 A"},{"key":"Chains","value":"A=1-371"}]},{"database":"PDB","id":"5N6G","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.58 A"},{"key":"Chains","value":"A=1-371"}]},{"database":"AlphaFoldDB","id":"O31246","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"O31246","properties":[{"key":"Description","value":"-"}]},{"database":"BioCyc","id":"MetaCyc:MONOMER-1003","properties":[{"key":"Description","value":"-"}]},{"database":"EvolutionaryTrace","id":"O31246","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016491","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02933","properties":[{"key":"EntryName","value":"OYE_like_FMN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000059","properties":[{"key":"EntryName","value":"N-ethylmaleimide reductase, FMN-linked"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR001155","properties":[{"key":"EntryName","value":"OxRdtase_FMN_N"}]},{"database":"InterPro","id":"IPR045247","properties":[{"key":"EntryName","value":"Oye-like"}]},{"database":"NCBIfam","id":"NF007899","properties":[{"key":"EntryName","value":"nemA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22893","properties":[{"key":"EntryName","value":"NADH OXIDOREDUCTASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22893:SF91","properties":[{"key":"EntryName","value":"NADPH DEHYDROGENASE 2-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00724","properties":[{"key":"EntryName","value":"Oxidored_FMN"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSLFEPAQAGDIALANRIVMAPLTRNRSPGAIPNNLNATYYEQRATAGLIVTEGTPISQQGQGYADVPGLYKREAIEGWKKITDGVHSAGGKIVAQIWHVGRISHTSLQPHGGQPVAPSAITAKSKTYIINDDGTGAFAETSEPRALTIDDIGLILEDYRSGARAALEAGFDGVEIHAANGYLIEQFLKSSTNQRTDDYGGSIENRARFLLEVVDAVAEEIGAGRTGIRLSPVTPANDIFEADPQPLYNYVVEQLGKRNLAFIHVVEGATGGPRDFKQGDKPFDYASFKAAYRNAGGKGLWIANNGYDRQSAIEAVESGKVDAVAFGKAFIANPDLVRRLKNDAPLNAPNQPTFYGGGAEGYTDYPALAQ","length":371,"molWeight":39698,"crc64":"6176F61C8D3F4AEB","md5":"7532428C9F9B011A2B584C94C7975874"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Initiator methionine":1,"Chain":1,"Active site":1,"Binding site":9,"Mutagenesis":3},"uniParcId":"UPI00000BAC05"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q60FX6","uniProtkbId":"GRDC_AGRRD","entryAudit":{"firstPublicDate":"2022-02-23","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2004-11-23","entryVersion":55,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15474471"}],"value":"Gamma-resorcylate decarboxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"value":"4.1.1.103"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15474471"}],"value":"2,6-dihydroxybenzoate decarboxylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15474471"}],"value":"Reversible gamma-RA decarboxylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"15474471"}],"value":"rdc"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"value":"Involved in the gamma-resorcylate (2,6-dihydroxybenzoate) catabolism (PubMed:15474471). Catalyzes the reversible decarboxylation of gamma-resorcylate to resorcinol (PubMed:15474471). Also catalyzes the decarboxylation of 2,3-dihydroxybenzoate to catechol, but does not act on 2-hydroxybenzoic acid 3-hydroxybenzoic acid, 4-hydroxybenzoic acid, 3,4-dihydroxybenzoic acid, 2,5-dihydroxybenzoic acid, 2,3,4-trihydroxybenzoic acid, 3,4,5-trihydroxybenzoic acid, 4-aminobenzoic acid, o-hydroxyphenylacetic acid and vanillic acid (PubMed:15474471). Resorcinol and catechol can both be carboxylated by the reverse reaction (PubMed:15474471)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2,6-dihydroxybenzoate + H(+) = resorcinol + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:49464"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:27810"},{"database":"ChEBI","id":"CHEBI:131450"}],"ecNumber":"4.1.1.103","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:49465"},"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2,3-dihydroxybenzoate + H(+) = catechol + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21492"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:18135"},{"database":"ChEBI","id":"CHEBI:36654"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60GU1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60GU1"}],"value":"Binds 1 Zn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"value":"Insensitive to oxygen. Decarboxylation and carboxylation are inhibited by AgNO(3) and by diethyl pyrocarbonate, a histidine residue-specific inhibitor. Decarboxylation is also inhibited by HgCl(2) and activated by MgCl(2)"}],"commentType":"ACTIVITY REGULATION"},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"michaelisConstants":[{"constant":7.1,"unit":"mM","substrate":"gamma-resorcylate (for decarboxylation)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}]},{"constant":0.035,"unit":"mM","substrate":"resorcinol (for carboxylation)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}]},{"constant":0.035,"unit":"mM","substrate":"catechol (for carboxylation)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}]}]},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"value":"Optimum pH is 7.0 for decarboxylation."}]},"temperatureDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"value":"Optimum temperature is 60 degrees Celsius for decarboxylation. Optimum temperature is 45 degrees Celsius for carboxylation."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Aromatic compound metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the metallo-dependent hydrolases superfamily. ACMSD family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"Gamma-resorcylate decarboxylase","featureId":"PRO_0000454503"},{"type":"Active site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60GU1"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60GU1"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60GU1"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60GU1"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q60GU1"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Mutagenesis","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"Loss of both decarboxylation and carboxylation activities.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["Q"]}},{"type":"Mutagenesis","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Loss of both decarboxylation and carboxylation activities.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["Q"]}}],"keywords":[{"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"15474471","citationType":"journal article","authors":["Ishii Y.","Narimatsu Y.","Iwasaki Y.","Arai N.","Kino K.","Kirimura K."],"citationCrossReferences":[{"database":"PubMed","id":"15474471"},{"database":"DOI","id":"10.1016/j.bbrc.2004.09.091"}],"title":"Reversible and nonoxidative gamma-resorcylic acid decarboxylase: characterization and gene cloning of a novel enzyme catalyzing carboxylation of resorcinol, 1,3-dihydroxybenzene, from Rhizobium radiobacter.","publicationDate":"2004","journal":"Biochem. Biophys. Res. Commun.","firstPage":"611","lastPage":"620","volume":"324"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 1-22","FUNCTION","CATALYTIC ACTIVITY","ACTIVITY REGULATION","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT","MUTAGENESIS OF HIS-164 AND HIS-218"],"referenceComments":[{"value":"WU-0108","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AB185333","properties":[{"key":"ProteinId","value":"BAD61045.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q60FX6","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q60FX6","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"4.1.1.103","properties":[{"key":"OrganismId","value":"31376"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050150","properties":[{"key":"GoTerm","value":"F:o-pyrocatechuate decarboxylase activity"},{"key":"GoEvidenceType","value":"EXP:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"15474471"}]},{"database":"GO","id":"GO:0019748","properties":[{"key":"GoTerm","value":"P:secondary metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR032465","properties":[{"key":"EntryName","value":"ACMSD"}]},{"database":"InterPro","id":"IPR006680","properties":[{"key":"EntryName","value":"Amidohydro-rel"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"PANTHER","id":"PTHR21240","properties":[{"key":"EntryName","value":"2-AMINO-3-CARBOXYLMUCONATE-6-SEMIALDEHYDE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21240:SF31","properties":[{"key":"EntryName","value":"AMIDOHYDROLASE FAMILY PROTEIN (AFU_ORTHOLOGUE AFUA_7G05840)"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04909","properties":[{"key":"EntryName","value":"Amidohydro_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQGKVALEEHFAIPETLQDSAGFVPGDYWKELQHRLLDIQDTRLKLMDAHGIETMILSLNAPAVQAIPDRKKAIEIARRANDVLAEECARRPDRFLAFAALPLQDPDAATQELQRCVNDLGFVGALVNGFSQEGDGQTPLYYDLPQYRPFWGEVEKLDVPFYLHPRNPLPQDSRIYDGHPWLLGPTWAFAQETAVHALRLMASGLFDAHPRLNIILGHMGEGLPYMMWRIDHRNAWVKLPPRYPAKRRFVDYFNENFHITTSGNFRTQTLIDAILEIGADRILFSTDWPFENIDHASDWFNATTIAEADRVKIGRTNARRLFKLDGR","length":327,"molWeight":37431,"crc64":"9F89EE385BC3EAF2","md5":"10F37737D7861A4316B12812FE0414C3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"ACTIVITY REGULATION":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":4,"Mutagenesis":2},"uniParcId":"UPI0000450395"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q44185","secondaryAccessions":["Q44203"],"uniProtkbId":"DCAS_AGRRD","entryAudit":{"firstPublicDate":"2003-09-19","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1996-11-01","entryVersion":97,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"N-carbamoyl-D-amino acid hydrolase"},"ecNumbers":[{"value":"3.5.1.77"}]},"alternativeNames":[{"fullName":{"value":"D-N-alpha-carbamilase"}}]},"comments":[{"texts":[{"value":"The enzyme catalyzes the hydrolysis of N-carbamoyl-D-amino acids to the corresponding which are useful intermediates in the preparation of beta-lactam antibiotics. Industrial production of beta-lactam antibiotics is now being developed using this enzyme"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N-carbamoyl-D-amino acid + H2O + 2 H(+) = a D-alpha-amino acid + NH4(+) + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11000"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:59871"},{"database":"ChEBI","id":"CHEBI:85602"}],"ecNumber":"3.5.1.77"}},{"texts":[{"value":"Homotetramer"}],"commentType":"SUBUNIT"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"N-carbamoyl-D-amino acid hydrolase","featureId":"PRO_0000079801"},{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"CN hydrolase","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11237598"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11237598"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"11237598"}]},{"type":"Mutagenesis","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"No activity.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11237598"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A","N","R"]}},{"type":"Mutagenesis","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"5% activity of wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11237598"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Mutagenesis","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"17% activity of wild-type.","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"11237598"}],"alternativeSequence":{"originalSequence":"H","alternativeSequences":["A"]}},{"type":"Sequence conflict","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"in Ref. 2; AAB47607","evidences":[{"evidenceCode":"ECO:0000305"}],"alternativeSequence":{"originalSequence":"V","alternativeSequences":["L"]}},{"type":"Beta strand","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Turn","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Turn","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Beta strand","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]},{"type":"Helix","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0007829","source":"PDB","id":"1FO6"}]}],"keywords":[{"id":"KW-0002","category":"Technical term","name":"3D-structure"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"8931327","citationType":"journal article","authors":["Buson A.","Negro A.","Grassato L.","Tagliaro M.","Basaglia M.","Grandi C.","Fontana A.","Nuti M.P."],"citationCrossReferences":[{"database":"PubMed","id":"8931327"},{"database":"DOI","id":"10.1111/j.1574-6968.1996.tb08556.x"}],"title":"Identification, sequencing and mutagenesis of the gene for a D-carbamoylase from Agrobacterium radiobacter.","publicationDate":"1996","journal":"FEMS Microbiol. Lett.","firstPage":"55","lastPage":"62","volume":"145"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"BCRC 13814 / CECT 4067 / NRRL B-11291","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"CI-BBU147D3B132A","citationType":"submission","authors":["Grifantini R."],"publicationDate":"AUG-1995","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"BCRC 13814 / CECT 4067 / NRRL B-11291","type":"STRAIN"}]},{"referenceNumber":3,"citation":{"id":"8621596","citationType":"journal article","authors":["Grifantini R.","Pratesi C.","Galli G.","Grandi G."],"citationCrossReferences":[{"database":"PubMed","id":"8621596"},{"database":"DOI","id":"10.1074/jbc.271.16.9326"}],"title":"Topological mapping of the cysteine residues of N-carbamyl-D-amino-acid amidohydrolase and their role in enzymatic activity.","publicationDate":"1996","journal":"J. Biol. Chem.","firstPage":"9326","lastPage":"9331","volume":"271"},"referencePositions":["CHARACTERIZATION"],"referenceComments":[{"value":"BCRC 13814 / CECT 4067 / NRRL B-11291","type":"STRAIN"}]},{"referenceNumber":4,"citation":{"id":"11237598","citationType":"journal article","authors":["Wang W.-C.","Hsu W.-H.","Chien F.-T.","Chen C.-Y."],"citationCrossReferences":[{"database":"PubMed","id":"11237598"},{"database":"DOI","id":"10.1006/jmbi.2000.4380"}],"title":"Crystal structure and site-directed mutagenesis studies of N-carbamoyl-D-amino-acid amidohydrolase from Agrobacterium radiobacter reveals a homotetramer and insight into a catalytic cleft.","publicationDate":"2001","journal":"J. Mol. Biol.","firstPage":"251","lastPage":"261","volume":"306"},"referencePositions":["X-RAY CRYSTALLOGRAPHY","MUTAGENESIS OF HIS-129; HIS-144 AND HIS-215"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"U59376","properties":[{"key":"ProteinId","value":"AAB47607.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"EMBL","id":"X91070","properties":[{"key":"ProteinId","value":"CAA62550.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PDB","id":"1FO6","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"1.95 A"},{"key":"Chains","value":"A/B/C/D=1-304"}]},{"database":"PDB","id":"2GGK","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.30 A"},{"key":"Chains","value":"A/B/C/D=1-304"}]},{"database":"PDB","id":"2GGL","properties":[{"key":"Method","value":"X-ray"},{"key":"Resolution","value":"2.40 A"},{"key":"Chains","value":"A/B/C/D=1-304"}]},{"database":"AlphaFoldDB","id":"Q44185","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q44185","properties":[{"key":"Description","value":"-"}]},{"database":"EvolutionaryTrace","id":"Q44185","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0047417","properties":[{"key":"GoTerm","value":"F:N-carbamoyl-D-amino acid hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd07569","properties":[{"key":"EntryName","value":"DCase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.110.10","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050345","properties":[{"key":"EntryName","value":"Aliph_Amidase/BUP"}]},{"database":"InterPro","id":"IPR003010","properties":[{"key":"EntryName","value":"C-N_Hydrolase"}]},{"database":"InterPro","id":"IPR036526","properties":[{"key":"EntryName","value":"C-N_Hydrolase_sf"}]},{"database":"PANTHER","id":"PTHR43674","properties":[{"key":"EntryName","value":"NITRILASE C965.09-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43674:SF12","properties":[{"key":"EntryName","value":"NITRILASE C965.09-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00795","properties":[{"key":"EntryName","value":"CN_hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56317","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50263","properties":[{"key":"EntryName","value":"CN_HYDROLASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTRQMILAVGQQGPIARAETREQVVGRLLDMLTNAASRGVNFIVFPELALTTFFPRWHFTDEAELDSFYETEMPGPVVRPLFETAAELGIGFNLGYAELVVEGGVKRRFNTSILVDKSGKIVGKYRKIHLPGHKEYEAYRPFQHLEKRYFEPGDLGFPVYDVDAAKMGMFICNDRRWPETWRVMGLKGAEIICGGYNTPTHNPPVPQHDHLTSFHHLLSMQAGSYQNGAWSAAAGKVGMEEGCMLLGHSCIVAPTGEIVALTTTLEDEVITAAVDLDRCRELREHIFNFKAHRQPQHYGLIAEF","length":304,"molWeight":34152,"crc64":"02436D8CEF925211","md5":"541ABA4424D2A46A87D1B9F3325645D9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1},"countByFeatureType":{"Chain":1,"Domain":1,"Active site":3,"Mutagenesis":3,"Sequence conflict":1,"Beta strand":16,"Helix":14,"Turn":2},"uniParcId":"UPI00000B9F30"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A6XIG7","uniProtkbId":"SLMH_AGRRD","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2007-08-21","entryVersion":41,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17660282"}],"value":"4-sulfomuconolactone hydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}],"value":"3.1.1.92"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"17660282"}],"value":"4-carboxymethylen-4-sulfo-but-2-en-olide hydrolase"}}]},"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}],"value":"Involved in the degradation of 4-sulfocatechol which is a central intermediate in the degradation of substituted sulfonated benzenes. Catalyzes the hydrolytical desulfonation of 4-sulfomuconolactone to yield maleylacetate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-sulfomuconolactone + H2O = maleylacetate + sulfite + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:33711"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16468"},{"database":"ChEBI","id":"CHEBI:17359"},{"database":"ChEBI","id":"CHEBI:20479"}],"ecNumber":"3.1.1.92","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000250"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"commentType":"BIOPHYSICOCHEMICAL PROPERTIES","kineticParameters":{"maximumVelocities":[{"velocity":12.6,"unit":"umol/min/mg","enzyme":"enzyme (at pH 8)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}]}],"michaelisConstants":[{"constant":0.34,"unit":"mM","substrate":"4-sulfomuconolactone (at pH 8)","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}]}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}],"value":"kcat is 400 min(-1) with 4-sulfomuconolactone as substrate (at pH 8)."}]}},"phDependence":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}],"value":"Optimum pH is between 7 and 7.5. Approximately 30% of the maximal activities are still detected at pH 5 and pH 9."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"17660282"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the metallo-dependent hydrolases superfamily. Sulfomuconolactone hydrolase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"4-sulfomuconolactone hydrolase","featureId":"PRO_0000422785"}],"keywords":[{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"17660282","citationType":"journal article","authors":["Halak S.","Basta T.","Burger S.","Contzen M.","Wray V.","Pieper D.H.","Stolz A."],"citationCrossReferences":[{"database":"PubMed","id":"17660282"},{"database":"DOI","id":"10.1128/jb.00611-07"}],"title":"4-sulfomuconolactone hydrolases from Hydrogenophaga intermedia S1 and Agrobacterium radiobacter S2.","publicationDate":"2007","journal":"J. Bacteriol.","firstPage":"6998","lastPage":"7006","volume":"189"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","FUNCTION","CATALYTIC ACTIVITY","BIOPHYSICOCHEMICAL PROPERTIES","SUBUNIT"],"referenceComments":[{"value":"S2","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"DQ813262","properties":[{"key":"ProteinId","value":"ABH09755.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A6XIG7","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"A6XIG7","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ag:ABH09755","properties":[{"key":"Description","value":"-"}]},{"database":"BRENDA","id":"3.1.1.92","properties":[{"key":"OrganismId","value":"28635"}]},{"database":"GO","id":"GO:0102998","properties":[{"key":"GoTerm","value":"F:4-sulfomuconolactone hydrolase activity"},{"key":"GoEvidenceType","value":"IDA:UniProtKB"}],"evidences":[{"evidenceCode":"ECO:0000314","source":"PubMed","id":"17660282"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006680","properties":[{"key":"EntryName","value":"Amidohydro-rel"}]},{"database":"InterPro","id":"IPR052358","properties":[{"key":"EntryName","value":"Aro_Compnd_Degr_Hydrolases"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR053519","properties":[{"key":"EntryName","value":"SML-Hydrolase"}]},{"database":"NCBIfam","id":"NF042924","properties":[{"key":"EntryName","value":"SlmHylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR35563","properties":[{"key":"EntryName","value":"BARREL METAL-DEPENDENT HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G16240)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR35563:SF2","properties":[{"key":"EntryName","value":"BARREL METAL-DEPENDENT HYDROLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_1G16240)-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04909","properties":[{"key":"EntryName","value":"Amidohydro_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLPADQAGIPPCQGPRARSAPISFAIPKGAWDTHLHVFGPTAVFPYAEKRPYTPPDSPLEDYLALMERLGIERGVCVHPNVHGIDNSVTIDAVERSDRRLLGIIKPHRVMTFTELRDLKTRGVRGVRFAFNPQHGSGALDTELFERMHGWCRELDWCINMHFAPDALEGLCDLIAGAETPIIIDHFGRVETAAGVNQLPFKILRDLATLDHVWIKLTGADRISHSGVPYDDVVPFAHALSEIAPDRLLWGSDWPHSGYFDPKRMPDDGDLLNLVARFAPDVALRHKILVDNPARLFGVI","length":299,"molWeight":33289,"crc64":"A7A176833274ADE4","md5":"30C19DA09F122A5823159D5B593E8E09"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"BIOPHYSICOCHEMICAL PROPERTIES":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1},"uniParcId":"UPI00015781B3"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P26505","uniProtkbId":"HEM1_AGRRD","entryAudit":{"firstPublicDate":"1992-08-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1992-08-01","entryVersion":113,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"5-aminolevulinate synthase"},"ecNumbers":[{"value":"2.3.1.37"}]},"alternativeNames":[{"fullName":{"value":"5-aminolevulinic acid synthase"}},{"fullName":{"value":"Delta-ALA synthase"}},{"fullName":{"value":"Delta-aminolevulinate synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"2034217"}],"value":"hemA"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"succinyl-CoA + glycine + H(+) = 5-aminolevulinate + CO2 + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57292"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:356416"}],"ecNumber":"2.3.1.37"}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from glycine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the class-II pyridoxal-phosphate-dependent aminotransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"5-aminolevulinate synthase","featureId":"PRO_0000163824"},{"type":"Active site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}]},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P18079"}]}],"keywords":[{"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"id":"KW-0350","category":"Biological process","name":"Heme biosynthesis"},{"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"2034217","citationType":"journal article","authors":["Drolet M.","Sasarman A."],"citationCrossReferences":[{"database":"PubMed","id":"2034217"},{"database":"DOI","id":"10.1007/bf00273610"}],"title":"Cloning and nucleotide sequence of the hemA gene of Agrobacterium radiobacter.","publicationDate":"1991","journal":"Mol. Gen. Genet.","firstPage":"250","lastPage":"256","volume":"226"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"ATCC 4718 / JCM 20199 / IAM 1526 / LMG 139 / NBRC 12664 / CIP 104326 / R-3","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"PIR","id":"S15996","properties":[{"key":"EntryName","value":"S15996"}]},{"database":"AlphaFoldDB","id":"P26505","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P26505","properties":[{"key":"Description","value":"-"}]},{"database":"eggNOG","id":"COG0156","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OMA","id":"AAGMKCP","properties":[{"key":"Fingerprint","value":"-"}]},{"database":"UniPathway","id":"UPA00251","properties":[{"key":"RectionId","value":"UER00375"}]},{"database":"GO","id":"GO:0003870","properties":[{"key":"GoTerm","value":"F:5-aminolevulinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06454","properties":[{"key":"EntryName","value":"KBL_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000006","properties":[{"key":"EntryName","value":"5-aminolevulinate synthase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010961","properties":[{"key":"EntryName","value":"4pyrrol_synth_NH2levulA_synth"}]},{"database":"InterPro","id":"IPR001917","properties":[{"key":"EntryName","value":"Aminotrans_II_pyridoxalP_BS"}]},{"database":"InterPro","id":"IPR004839","properties":[{"key":"EntryName","value":"Aminotransferase_I/II_large"}]},{"database":"InterPro","id":"IPR050087","properties":[{"key":"EntryName","value":"AON_synthase_class-II"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR01821","properties":[{"key":"EntryName","value":"5aminolev_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13693:SF102","properties":[{"key":"EntryName","value":"2-AMINO-3-KETOBUTYRATE COENZYME A LIGASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13693","properties":[{"key":"EntryName","value":"CLASS II AMINOTRANSFERASE/8-AMINO-7-OXONONANOATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00155","properties":[{"key":"EntryName","value":"Aminotran_1_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00599","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDFEAFFTTELQSLHSEGRYRVFADIERQQGNFPRATRYNANGQRKDVTVWCSNDYLGMGQNPKVIEAMKAAIDHCGAGAGGTRNISGTNHYHVLLEQELADLHGKESALIFTSGYVSNWATLGTLGQKIPGLIIFSDALNHASMIEGIRYGRCERVIWKHNDLEDLEAKLKAADPNAPKLIAFESVYSMDGDIAPIKEICDLADRYGAMTYLDEVHAVGMYGPRGGGIAEREGLMDRLTIIEGTLGKAFGVMGGYITGSTAVCDFIRSFASGFIFTTALPPSLAAGAIASIQHLKASPFERARHQDRVRKLRGLLDARGIPHMDNPSHIVPVMVGDAAKCKWISDILLDSHGVYVQPINYPTVPRKTERLRITPTPLHSDADIEHLVGALHQLWSHCALARAVA","length":405,"molWeight":44412,"crc64":"F173AC1B13CAACDA","md5":"ADAA7933DC0E4A42DF71BBF657F6EF04"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Active site":1,"Binding site":8,"Modified residue":1},"uniParcId":"UPI000012C403"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29822","uniProtkbId":"LACE_AGRRD","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1993-04-01","entryVersion":82,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Lactose-binding protein"},"shortNames":[{"value":"LBP"}]},"flag":"Precursor"},"genes":[{"geneName":{"value":"lacE"}}],"comments":[{"texts":[{"value":"Part of the binding protein-dependent transport system for lactose"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Periplasm","id":"SL-0200"}}]},{"texts":[{"value":"By lactose and various galactosides, and subject to catabolite repression by glucose, galactose and succinate. In strain AR50 the expression of the lac operon is constitutive"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the bacterial solute-binding protein 1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"2318800"}]},{"type":"Chain","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"Lactose-binding protein","featureId":"PRO_0000031693"},{"type":"Region","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Lactose-binding","evidences":[{"evidenceCode":"ECO:0000250"}]}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-0574","category":"Cellular component","name":"Periplasm"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0762","category":"Biological process","name":"Sugar transport"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"1630315","citationType":"journal article","authors":["Williams S.G.","Greenwood J.A.","Jones C.W."],"citationCrossReferences":[{"database":"PubMed","id":"1630315"},{"database":"DOI","id":"10.1111/j.1365-2958.1992.tb01348.x"}],"title":"Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and beta-galactosidase in Agrobacterium radiobacter.","publicationDate":"1992","journal":"Mol. Microbiol.","firstPage":"1755","lastPage":"1768","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"AR50","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"2318800","citationType":"journal article","authors":["Greenwood J.A.","Cornish A.","Jones C.W."],"citationCrossReferences":[{"database":"PubMed","id":"2318800"},{"database":"DOI","id":"10.1128/jb.172.4.1703-1710.1990"}],"title":"Binding-protein-dependent lactose transport in Agrobacterium radiobacter.","publicationDate":"1990","journal":"J. Bacteriol.","firstPage":"1703","lastPage":"1710","volume":"172"},"referencePositions":["PROTEIN SEQUENCE OF 29-47","CHARACTERIZATION"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X66596","properties":[{"key":"ProteinId","value":"CAA47161.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S25247","properties":[{"key":"EntryName","value":"JGAGLR"}]},{"database":"AlphaFoldDB","id":"P29822","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P29822","properties":[{"key":"Description","value":"-"}]},{"database":"TCDB","id":"3.A.1.1.4","properties":[{"key":"FamilyName","value":"the atp-binding cassette (abc) superfamily"}]},{"database":"GO","id":"GO:0042597","properties":[{"key":"GoTerm","value":"C:periplasmic space"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050490","properties":[{"key":"EntryName","value":"Bact_solute-bd_prot1"}]},{"database":"InterPro","id":"IPR006059","properties":[{"key":"EntryName","value":"SBP"}]},{"database":"PANTHER","id":"PTHR43649","properties":[{"key":"EntryName","value":"ARABINOSE-BINDING PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43649:SF32","properties":[{"key":"EntryName","value":"SUGAR BINDING SECRETED PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13416","properties":[{"key":"EntryName","value":"SBP_bac_8"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDYSRLLKRSVSAALTAAALLCSTAAFAGEVTIWCWDPNFNVAIMKEAAERYTAKHPDTTFNIVDFAKADVEQKLQTGLASGMTDTLPDIVLIEDYGAQKYLQSFPGSFAALTDKIDFSGFAKYKVDLMTLEGQVYGVPFDSGVTGLYYRTDYLEQAGFKPEDMQNLTWDRFIEIGKEVKAKTGHEMMALDANDGGLIRIMMQSGGQWYFNEDGSLNITGNAALKAALETQARIVNERVAKPTSGSNDGIRALTSGDVASVLRGVWITGTVKSQPDQAGKWALTAIPKLNIEGATAASNLGGSSWYVLEASAEKDEAIDFLNEIYAKDLDFYQKILTERGAVGSLLAARTGEAYQKPDDFFGGQTVWQNFADWLVQVPAVNYGIFTNELDTAVTANFPALVKGTPVDEVLKAIEDQAAGQIQ","length":422,"molWeight":45904,"crc64":"23B6CBCF4BB4135A","md5":"E010F834B56B986AEF55079E14E5E295"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Region":1},"uniParcId":"UPI000012E1DA"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29824","uniProtkbId":"LACG_AGRRD","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1993-07-01","entryVersion":91,"sequenceVersion":2},"annotationScore":3.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"value":"Lactose transport system permease protein LacG"}}},"genes":[{"geneName":{"value":"lacG"}}],"comments":[{"texts":[{"value":"Part of the binding protein-dependent transport system for lactose. Probably responsible for the translocation of the substrate across the membrane"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Cell inner membrane","id":"SL-0037"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"value":"By lactose and various galactosides, and subject to catabolite repression by glucose, galactose and succinate. In strain AR50 the expression of the lac operon is constitutive"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the binding protein-dependent transport system permease family. MalFG subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"It is uncertain whether Met-1 or Met-2 is the initiator"}],"commentType":"CAUTION"},{"commentType":"SEQUENCE CAUTION","sequenceCautionType":"Erroneous initiation","sequence":"CAA47163.1","evidences":[{"evidenceCode":"ECO:0000305"}]}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Lactose transport system permease protein LacG","featureId":"PRO_0000060057"},{"type":"Transmembrane","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Domain","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"ABC transmembrane type-1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]}],"keywords":[{"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0762","category":"Biological process","name":"Sugar transport"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"1630315","citationType":"journal article","authors":["Williams S.G.","Greenwood J.A.","Jones C.W."],"citationCrossReferences":[{"database":"PubMed","id":"1630315"},{"database":"DOI","id":"10.1111/j.1365-2958.1992.tb01348.x"}],"title":"Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and beta-galactosidase in Agrobacterium radiobacter.","publicationDate":"1992","journal":"Mol. Microbiol.","firstPage":"1755","lastPage":"1768","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"AR50","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X66596","properties":[{"key":"ProteinId","value":"CAA47163.1"},{"key":"Status","value":"ALT_INIT"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S25249","properties":[{"key":"EntryName","value":"MMAGCG"}]},{"database":"AlphaFoldDB","id":"P29824","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P29824","properties":[{"key":"Description","value":"-"}]},{"database":"TCDB","id":"3.A.1.1.4","properties":[{"key":"FamilyName","value":"the atp-binding cassette (abc) superfamily"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0055085","properties":[{"key":"GoTerm","value":"P:transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06261","properties":[{"key":"EntryName","value":"TM_PBP2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3720.10","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000515","properties":[{"key":"EntryName","value":"MetI-like"}]},{"database":"InterPro","id":"IPR035906","properties":[{"key":"EntryName","value":"MetI-like_sf"}]},{"database":"PANTHER","id":"PTHR43744","properties":[{"key":"EntryName","value":"ABC TRANSPORTER PERMEASE PROTEIN MG189-RELATED-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43744:SF2","properties":[{"key":"EntryName","value":"ARABINOOLIGOSACCHARIDES TRANSPORT SYSTEM PERMEASE PROTEIN ARAQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00528","properties":[{"key":"EntryName","value":"BPD_transp_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161098","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50928","properties":[{"key":"EntryName","value":"ABC_TM1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MMTTLRRRLPDIVQYSVLSLAAFLSIFPFIWMVIGTTNTTSQIIRGKVTFGTALFDNIASFFAQVDVPLVFWNSVKIALVGTALTLLVSSLAGYGFEMFRSKLRERVYTVILLTLMVPFAALMIPLFMLMGQAGLLNTHIAIMLPMIASAFIIFYFRQASKAFPTELRDAAKVDGLKEWQIFFYIYVPVMRSTYAAAFVIVFMLNWNNYLWPLIVLQSNDTKTITLVVSSLASAYSPEYGTVMIGTILATLPTLLVFFAMQRQFVQGMLGSVK","length":273,"molWeight":30652,"crc64":"D21F8BFAF78F4BC5","md5":"489CBAE4BE06F4E3D1AF11523E992392"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"SIMILARITY":1,"CAUTION":1,"SEQUENCE CAUTION":1},"countByFeatureType":{"Chain":1,"Transmembrane":6,"Domain":1},"uniParcId":"UPI000012E1DC"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q01937","uniProtkbId":"LACK_AGRRD","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"1993-04-01","entryVersion":117,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Lactose transport ATP-binding protein LacK"}}},"genes":[{"geneName":{"value":"lacK"}}],"comments":[{"texts":[{"value":"Part of the binding protein-dependent transport system for lactose. Probably responsible for energy coupling to the transport system"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Cell inner membrane","id":"SL-0037"},"topology":{"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ABC transporter superfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Lactose transport ATP-binding protein LacK","featureId":"PRO_0000092396"},{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"ABC transporter","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00434"}]},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00434"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"id":"KW-0762","category":"Biological process","name":"Sugar transport"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"1630315","citationType":"journal article","authors":["Williams S.G.","Greenwood J.A.","Jones C.W."],"citationCrossReferences":[{"database":"PubMed","id":"1630315"},{"database":"DOI","id":"10.1111/j.1365-2958.1992.tb01348.x"}],"title":"Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and beta-galactosidase in Agrobacterium radiobacter.","publicationDate":"1992","journal":"Mol. Microbiol.","firstPage":"1755","lastPage":"1768","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"AR50","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X66596","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S34734","properties":[{"key":"EntryName","value":"S34734"}]},{"database":"AlphaFoldDB","id":"Q01937","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q01937","properties":[{"key":"Description","value":"-"}]},{"database":"TCDB","id":"3.A.1.1.4","properties":[{"key":"FamilyName","value":"the atp-binding cassette (abc) superfamily"}]},{"database":"GO","id":"GO:0055052","properties":[{"key":"GoTerm","value":"C:ATP-binding cassette (ABC) transporter complex, substrate-binding subunit-containing"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1990060","properties":[{"key":"GoTerm","value":"C:maltose transport complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0015423","properties":[{"key":"GoTerm","value":"F:ABC-type maltose transporter activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03301","properties":[{"key":"EntryName","value":"ABC_MalK_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000042","properties":[{"key":"EntryName","value":"Maltose/maltodextrin ABC transporter, ATP-binding protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR003439","properties":[{"key":"EntryName","value":"ABC_transporter-like_ATP-bd"}]},{"database":"InterPro","id":"IPR017871","properties":[{"key":"EntryName","value":"ABC_transporter-like_CS"}]},{"database":"InterPro","id":"IPR015855","properties":[{"key":"EntryName","value":"ABC_transpr_MalK-like"}]},{"database":"InterPro","id":"IPR047641","properties":[{"key":"EntryName","value":"ABC_transpr_MalK/UgpC-like"}]},{"database":"InterPro","id":"IPR008995","properties":[{"key":"EntryName","value":"Mo/tungstate-bd_C_term_dom"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR040582","properties":[{"key":"EntryName","value":"OB_MalK-like"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF008653","properties":[{"key":"EntryName","value":"ugpC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43875","properties":[{"key":"EntryName","value":"MALTODEXTRIN IMPORT ATP-BINDING PROTEIN MSMX"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43875:SF3","properties":[{"key":"EntryName","value":"MALTOSE_MALTODEXTRIN IMPORT ATP-BINDING PROTEIN MALK"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00005","properties":[{"key":"EntryName","value":"ABC_tran"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17912","properties":[{"key":"EntryName","value":"OB_MalK"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50331","properties":[{"key":"EntryName","value":"MOP-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":"PS00211","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50893","properties":[{"key":"EntryName","value":"ABC_TRANSPORTER_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAEVRLTDIRKSYGSLEVIKGVNLEVSSGEFVVFVGPSGCGKSTLLRMIAGLEDISSGELTIGGTVMNDVDPSKRGIAMVFQTYALYPHMTVRENMGFALRFAGMAKDEIERRVNAAAKILELDALMDRKPKALSGGQRQRVAIGRAIVRQPDVFLFDEPLSNLDAELRVHMRVEIARLHKELNATIVYVTHDQVEAMTLADKIVVMRGGIVEQVGAPLALYDDPDNMFVAGFIGSPRMNFLPAVVIGQAEGGQVTVALKARPDTQLTVACATPPQGGDAVTVGVRPEHFLPAGSGDTQLTAHVDVVEHLGNTSYVYAHTVPGEQIIIEQEERRHGGRYGDEIAVGISAKTSFLFDASGRRIR","length":363,"molWeight":39324,"crc64":"1B1F8CC29453B8B2","md5":"DC71F14A46A0D274AC9555C1573C3150"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Domain":1,"Binding site":1},"uniParcId":"UPI000012E1E4"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q44184","uniProtkbId":"HYDA_AGRRD","entryAudit":{"firstPublicDate":"1998-07-15","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-11-01","entryVersion":103,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"D-hydantoinase"},"ecNumbers":[{"value":"3.5.2.-"}]}},"genes":[{"geneName":{"value":"hyuA"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Catalyzes the stereospecific hydrolysis of the cyclic amide bond of D-hydantoin derivatives"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q55DL0"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q55DL0"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Carboxylation allows a single lysine to coordinate two zinc ions"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the metallo-dependent hydrolases superfamily. Hydantoinase/dihydropyrimidinase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"D-hydantoinase","featureId":"PRO_0000165932"},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Phosphoserine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q14117"}]},{"type":"Modified residue","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"Q9P903"}]}],"keywords":[{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BBU147D3B132A","citationType":"submission","authors":["Grifantini R."],"publicationDate":"AUG-1995","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"BCRC 13814 / CECT 4067 / NRRL B-11291","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X91070","properties":[{"key":"ProteinId","value":"CAA62549.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"Q44184","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q44184","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016812","properties":[{"key":"GoTerm","value":"F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in cyclic amides"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01314","properties":[{"key":"EntryName","value":"D-HYD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.140:FF:000217","properties":[{"key":"EntryName","value":"Dihydropyrimidinase-related protein 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.40.10","properties":[{"key":"EntryName","value":"Urease, subunit C, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006680","properties":[{"key":"EntryName","value":"Amidohydro-rel"}]},{"database":"InterPro","id":"IPR011778","properties":[{"key":"EntryName","value":"Hydantoinase/dihydroPyrase"}]},{"database":"InterPro","id":"IPR011059","properties":[{"key":"EntryName","value":"Metal-dep_hydrolase_composite"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR050378","properties":[{"key":"EntryName","value":"Metallo-dep_Hydrolases_sf"}]},{"database":"InterPro","id":"IPR011612","properties":[{"key":"EntryName","value":"Urease_alpha_N_dom"}]},{"database":"NCBIfam","id":"TIGR02033","properties":[{"key":"EntryName","value":"D-hydantoinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11647:SF1","properties":[{"key":"EntryName","value":"COLLAPSIN RESPONSE MEDIATOR PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11647","properties":[{"key":"EntryName","value":"HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01979","properties":[{"key":"EntryName","value":"Amidohydro_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00449","properties":[{"key":"EntryName","value":"Urease_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51338","properties":[{"key":"EntryName","value":"Composite domain of metallo-dependent hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDIIIKNGTIVTADGISPADLGIKDGKIAQIGGTFGPAGRTIDASGRYVFPGGIDVHTHVETVSFNTQSADTFATATVAAACGGTTTIVDFCQQDRGHSLREAVAKWDGMAGGKSAIDYGYHIIVLDPTDSVIEELEVLPDLGITSFKVFMAYRGMNMIDDVTLLRTLDKAAKTGSLVMVHAENGDAADYLRDKFVADGKTAPIYHALSRPPRVEAEATARALALAEIVNAPIYIVHLTCEESFDELMRAKARGVHALAETCTQYLYLTKDDLERPDFEGAKYVFTPPPRTKKDQEILWNALRNGVLETVSSDHCSWLFEGHKDRGRNDFRAIPNGAPGVEERLMMVYQGVNEGRISLTQFVELVATRPAKVFGMFPEKGTVAVGSDADIVLWDPEAEMVIEQSAMHNAMDYSSYEGHKIKGVPKTVLLRGKVIVDEGTYVGAPTDGQFRKRRKYKQ","length":457,"molWeight":49940,"crc64":"9BC8EE0A86914A5B","md5":"524344458D23694C6F6DF0CFDC1766F7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Binding site":10,"Modified residue":2},"uniParcId":"UPI000012CFE8"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P55324","uniProtkbId":"ROSA_AGRRD","entryAudit":{"firstPublicDate":"1996-10-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1996-10-01","entryVersion":89,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Transcriptional regulatory protein rosAr"}}},"genes":[{"geneName":{"value":"rosAR"}}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the ros/MucR family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"Transcriptional regulatory protein rosAr","featureId":"PRO_0000168173"},{"type":"Zinc finger","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"C2H3-type"}],"keywords":[{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"id":"KW-0862","category":"Ligand","name":"Zinc"},{"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"7579618","citationType":"journal article","authors":["Brightwell G.","Hussain H.A.","Tiburtius A.","Yeoman K.H.","Johnston A.W.B."],"citationCrossReferences":[{"database":"PubMed","id":"7579618"},{"database":"DOI","id":"10.1094/mpmi-8-0747"}],"title":"Pleiotropic effects of regulatory ros mutants of Agrobacterium radiobacter and their interaction with Fe and glucose.","publicationDate":"1995","journal":"Mol. Plant Microbe Interact.","firstPage":"747","lastPage":"754","volume":"8"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"T1305","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X82941","properties":[{"key":"ProteinId","value":"CAA58116.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S49916","properties":[{"key":"EntryName","value":"S49916"}]},{"database":"AlphaFoldDB","id":"P55324","properties":[{"key":"Description","value":"-"}]},{"database":"BMRB","id":"P55324","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P55324","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9809693at2","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006355","properties":[{"key":"GoTerm","value":"P:regulation of DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"1.10.10.1550","properties":[{"key":"EntryName","value":"ROS/MUCR transcriptional regulator protein"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR041920","properties":[{"key":"EntryName","value":"ROS/MUCR_sf"}]},{"database":"InterPro","id":"IPR008807","properties":[{"key":"EntryName","value":"ROS_MUCR"}]},{"database":"Pfam","id":"PF05443","properties":[{"key":"EntryName","value":"ROS_MUCR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTETAYGNAQDLLVELTADIVAAYVSNHVVPVTELPGLISDVHTALSGTSAPASVAVNVEKQKPAVSVRKSVQDDHIVCLECGGSFKSLKRHLTTHHSMTPEEYREKWDLQVDYPMVAPAYAEARSRLAKEMGLGQRRKANR","length":142,"molWeight":15558,"crc64":"FA63A0A52047F260","md5":"D063DBA37C315DCFA9E89E718D83714C"},"extraAttributes":{"countByCommentType":{"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Zinc finger":1},"uniParcId":"UPI000013454D"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q01936","uniProtkbId":"LACI_AGRRD","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1993-04-01","entryVersion":77,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"value":"Lactose operon repressor"}},"flag":"Fragment"},"genes":[{"geneName":{"value":"lacI"}}],"comments":[{"texts":[{"value":"Repressor of the lactose operon. Binds lactose as an inducer"}],"commentType":"FUNCTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"OUTSIDE"},"end":{"value":113,"modifier":"EXACT"}},"description":"Lactose operon repressor","featureId":"PRO_0000107962"},{"type":"Non-terminal residue","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":""}],"keywords":[{"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"id":"KW-0678","category":"Molecular function","name":"Repressor"},{"id":"KW-0804","category":"Biological process","name":"Transcription"},{"id":"KW-0805","category":"Biological process","name":"Transcription regulation"}],"references":[{"referenceNumber":1,"citation":{"id":"1630315","citationType":"journal article","authors":["Williams S.G.","Greenwood J.A.","Jones C.W."],"citationCrossReferences":[{"database":"PubMed","id":"1630315"},{"database":"DOI","id":"10.1111/j.1365-2958.1992.tb01348.x"}],"title":"Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and beta-galactosidase in Agrobacterium radiobacter.","publicationDate":"1992","journal":"Mol. Microbiol.","firstPage":"1755","lastPage":"1768","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"AR50","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X66596","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S34733","properties":[{"key":"EntryName","value":"S34733"}]},{"database":"AlphaFoldDB","id":"Q01936","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q01936","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0003700","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000976","properties":[{"key":"GoTerm","value":"F:transcription cis-regulatory region binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.40.50.2300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR046335","properties":[{"key":"EntryName","value":"LacI/GalR-like_sensor"}]},{"database":"InterPro","id":"IPR028082","properties":[{"key":"EntryName","value":"Peripla_BP_I"}]},{"database":"PANTHER","id":"PTHR30146:SF109","properties":[{"key":"EntryName","value":"HTH-TYPE TRANSCRIPTIONAL REGULATOR GALS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30146","properties":[{"key":"EntryName","value":"LACI-RELATED TRANSCRIPTIONAL REPRESSOR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13377","properties":[{"key":"EntryName","value":"Peripla_BP_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53822","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like I"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"ETGYQQAKSLLALEVRPDAIVAANDNMAIGTYRAIQEAGLSIPGDIAVVAFNDIPVAQFLTPPLSTMRIPGELIGEVAVDLLVERLNGRDYSKHVTLPTEMIWRASAKKPSAS","length":113,"molWeight":12146,"crc64":"14565A160E3A7919","md5":"82224443020840DB7F5E2D11F662174B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1},"countByFeatureType":{"Chain":1,"Non-terminal residue":1},"uniParcId":"UPI000012E1E2"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P29823","uniProtkbId":"LACF_AGRRD","entryAudit":{"firstPublicDate":"1993-04-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1993-04-01","entryVersion":97,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"value":"Lactose transport system permease protein LacF"}}},"genes":[{"geneName":{"value":"lacF"}}],"comments":[{"texts":[{"value":"Part of the binding protein-dependent transport system for lactose. Probably responsible for the translocation of the substrate across the membrane"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Cell inner membrane","id":"SL-0037"},"topology":{"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"value":"By lactose and various galactosides, and subject to catabolite repression by glucose, galactose and succinate. In strain AR50 the expression of the lac operon is constitutive"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the binding protein-dependent transport system permease family. MalFG subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"Lactose transport system permease protein LacF","featureId":"PRO_0000060056"},{"type":"Transmembrane","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Transmembrane","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]},{"type":"Domain","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"ABC transmembrane type-1","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00441"}]}],"keywords":[{"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0762","category":"Biological process","name":"Sugar transport"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"1630315","citationType":"journal article","authors":["Williams S.G.","Greenwood J.A.","Jones C.W."],"citationCrossReferences":[{"database":"PubMed","id":"1630315"},{"database":"DOI","id":"10.1111/j.1365-2958.1992.tb01348.x"}],"title":"Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and beta-galactosidase in Agrobacterium radiobacter.","publicationDate":"1992","journal":"Mol. Microbiol.","firstPage":"1755","lastPage":"1768","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"AR50","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X66596","properties":[{"key":"ProteinId","value":"CAA47162.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S25248","properties":[{"key":"EntryName","value":"MMAGCF"}]},{"database":"AlphaFoldDB","id":"P29823","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P29823","properties":[{"key":"Description","value":"-"}]},{"database":"TCDB","id":"3.A.1.1.4","properties":[{"key":"FamilyName","value":"the atp-binding cassette (abc) superfamily"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0055085","properties":[{"key":"GoTerm","value":"P:transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06261","properties":[{"key":"EntryName","value":"TM_PBP2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3720.10","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051393","properties":[{"key":"EntryName","value":"ABC_transporter_permease"}]},{"database":"InterPro","id":"IPR000515","properties":[{"key":"EntryName","value":"MetI-like"}]},{"database":"InterPro","id":"IPR035906","properties":[{"key":"EntryName","value":"MetI-like_sf"}]},{"database":"PANTHER","id":"PTHR30193","properties":[{"key":"EntryName","value":"ABC TRANSPORTER PERMEASE PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30193:SF37","properties":[{"key":"EntryName","value":"INNER MEMBRANE ABC TRANSPORTER PERMEASE PROTEIN YCJO"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00528","properties":[{"key":"EntryName","value":"BPD_transp_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF161098","properties":[{"key":"EntryName","value":"MetI-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50928","properties":[{"key":"EntryName","value":"ABC_TM1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATTSRSSLKRYYDVNGWLFVAPAIALISVFMLYPILRSLVLSLYTGRGMMLKFSGTGNLVRLWNDPVFWQALQNTVIFFVVQVPIMITMALILAAMLNNPKLRYSGLFRTMIFLPCVSSLVAYSILFKSMFSLDGVVNNTLLAIGIIGEPIGWLTDPFWAKVLIIIAITWRWTGYNMIFYLAALQNIDRSIYEAAKIDGVPSWGRFAFLTIPMLKPVILFTTITSTIGTLQLFDEVYNFTEGTGGPANSTLTLSLYIYNLTFRFMPSFSYAATVSYVIVLMVAVLSFLQFYAARERK","length":298,"molWeight":33618,"crc64":"DFC82440F126DAD0","md5":"81CA2A3F4D4A92F96F3E7EEC7E3EB00F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":6,"Domain":1},"uniParcId":"UPI000012E1DB"}},{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"P30812","uniProtkbId":"BGAL_AGRRD","entryAudit":{"firstPublicDate":"1993-07-01","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"1993-07-01","entryVersion":64,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Beta-galactosidase"},"shortNames":[{"value":"Beta-gal"}],"ecNumbers":[{"value":"3.2.1.23"}]},"alternativeNames":[{"fullName":{"value":"Lactase"}}],"flag":"Fragment"},"genes":[{"geneName":{"value":"lacZ"}}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of terminal non-reducing beta-D-galactose residues in beta-D-galactosides.","ecNumber":"3.2.1.23"}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the glycosyl hydrolase 2 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":138,"modifier":"OUTSIDE"}},"description":"Beta-galactosidase","featureId":"PRO_0000057655"},{"type":"Non-terminal residue","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":""}],"keywords":[{"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"}],"references":[{"referenceNumber":1,"citation":{"id":"1630315","citationType":"journal article","authors":["Williams S.G.","Greenwood J.A.","Jones C.W."],"citationCrossReferences":[{"database":"PubMed","id":"1630315"},{"database":"DOI","id":"10.1111/j.1365-2958.1992.tb01348.x"}],"title":"Molecular analysis of the lac operon encoding the binding-protein-dependent lactose transport system and beta-galactosidase in Agrobacterium radiobacter.","publicationDate":"1992","journal":"Mol. Microbiol.","firstPage":"1755","lastPage":"1768","volume":"6"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]"],"referenceComments":[{"value":"AR50","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"X66596","properties":[{"key":"ProteinId","value":"-"},{"key":"Status","value":"NOT_ANNOTATED_CDS"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"S34735","properties":[{"key":"EntryName","value":"S34735"}]},{"database":"AlphaFoldDB","id":"P30812","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"P30812","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0004565","properties":[{"key":"GoTerm","value":"F:beta-galactosidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR040605","properties":[{"key":"EntryName","value":"Glyco_hydro2_dom5"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"Pfam","id":"PF18565","properties":[{"key":"EntryName","value":"Glyco_hydro2_C5"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRIIENFNEFGEWGMTWRDGELVGFINGEEVVRRHLPADPLPTTLEIAADDTELRAGEKDTVRVILRALDQGGNVLSFFDDPVEVSLQGPGRIVGPSLLSFKGGAVGVYVEAGNEAGHLTLSATCRPFGTQRITFNVT","length":138,"molWeight":15016,"crc64":"2C6A3DFBE22D5EF5","md5":"6C788C49B6CC687A0FC625D908EC24A1"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Non-terminal residue":1},"uniParcId":"UPI00001268D1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LA80","uniProtkbId":"A0ABD5LA80_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489511.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine hydroxymethyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"SHMT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"2.1.2.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"glyA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489511.1"}],"value":"GGE40_001291"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057572"}],"value":"Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = 2-methylserine + (6S)-5,6,7,8-tetrahydrofolate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:58275"}],"ecNumber":"2.1.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051216"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15481"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57453"}],"ecNumber":"2.1.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"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_00051"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006376"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Belongs to the SHMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489511.1"}],"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":12,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Site","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Plays an important role in substrate specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]},{"type":"Modified residue","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"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_00051"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489511.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489511.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4489511.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003512506.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CBCSCS010000001.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LA80","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92923251","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"97363911","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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:0050413","properties":[{"key":"GoTerm","value":"F:D-alanine 2-hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00378","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000001","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000003","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00051","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"InterPro","id":"IPR001085","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase"}]},{"database":"InterPro","id":"IPR049943","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase-like"}]},{"database":"InterPro","id":"IPR019798","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase_PLP_BS"}]},{"database":"InterPro","id":"IPR039429","properties":[{"key":"EntryName","value":"SHMT-like_dom"}]},{"database":"NCBIfam","id":"NF000586","properties":[{"key":"EntryName","value":"PRK00011.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680:SF35","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00464","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000412","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00096","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNTDAFFSRPLAEVDPDIFGAIEKELGRQRHEIELIASENIVSRAVLEAQGSIMTNKYAEGYPGKRYYGGCQFVDIAEELAIERAKKLFGVNFANVQPNSGSQMNQAVFLALLQPGDTFMGLDLNSGGHLTHGSPVNMSGKWFNVVSYGVREGDNLLDMDEVERKAKETRPKLILAGGTAYSRIWDWKRFREIADEVGAYLMVDMAHIAGLVAGGQHPSPFPHCHVATTTTHKSLRGPRGGMILTNDEDLAKKFNSAVFPGLQGGPLMHVIAAKAVAFGEALQPEFKDYAAQVVKNAKALAETLIEGGLDVVSGGTDNHLMLVDLRKKNATGKRAEAALGRAYVTCNKNGIPFDPEKPFVTSGVRLGTPAGTTRGFKEAEFREIGKLIVEVLDGLKVANSDEGNAAVEAAVREKVVGLTDRFPMYPYM","length":429,"molWeight":46546,"crc64":"54EF8F6186CE2986","md5":"76C5DE7F8AA74EC51DDA912D1D44ADB7"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":1,"Modified residue":1},"uniParcId":"UPI00023A51DD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LG16","uniProtkbId":"A0ABD5LG16_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-06-18","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488664.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-tripeptide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramyl-tripeptide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488664.1"}],"value":"GGE40_000444"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488664.1"}],"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":26,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":116,"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":152,"modifier":"EXACT"},"end":{"value":153,"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":179,"modifier":"EXACT"},"end":{"value":179,"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":185,"modifier":"EXACT"},"end":{"value":185,"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":187,"modifier":"EXACT"},"end":{"value":187,"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":383,"modifier":"EXACT"},"end":{"value":383,"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":407,"modifier":"EXACT"},"end":{"value":410,"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":455,"modifier":"EXACT"},"end":{"value":455,"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":459,"modifier":"EXACT"},"end":{"value":459,"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":219,"modifier":"EXACT"},"end":{"value":219,"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":"MBB4488664.1"}],"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":"UP000534590"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488664.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488664.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4488664.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_060727410.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP184251.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LG16","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92922341","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNLRDISGNAFPELKELLLSEIGAIEIGGITADSRKAAPGSLFVAVAGTRADGAAYVKDAVAKGAVAVVSGHALEADVPVLSVTDPRLYLSLAASRFYGKQPETMVAVTGTAGKTSVASFVRQIWAFAGHAAAQIGTTGVIAPGREDYGALTTPDPVTLHALLAELAAEGVTHAAMEASSHGLDQRRLDGVKLAAAGFTNLGRDHMDYHPTVEDYMAAKMRLFDTLMEKGSPAVIFADDPWSDQAIRAAREAGLDVRTVGRKGDYLTLKRVEHFRHKQMIEVHHDGVIHEVDIPLAGDFQVANALVAAGLAMSTGVAATTALKALEKLIGAAGRLELVGQTGNGALAYVDYAHKPDALENVLTSVRPFTSGRIVTVFGCGGDRDKGKRPIMGEVATRLSDIVIVTDDNPRSEDAATIRSEVMAAAPGALEIGDRAEAIRHAVSMLSHGDTLIVAGKGHEEGQIVGSVTLPFSDHEQVRAALAGLEGSKI","length":489,"molWeight":51239,"crc64":"4E8A6DDE00612BD4","md5":"7C9205C38B45BC54A43E23F19F4B31B8"},"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":10,"Modified residue":1},"uniParcId":"UPI0007618D96"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LGZ0","uniProtkbId":"A0ABD5LGZ0_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489117.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"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":"MBB4489117.1"}],"value":"GGE40_000897"}]}],"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":"MBB4489117.1"}],"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":264,"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":533,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":514,"modifier":"EXACT"},"end":{"value":514,"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":516,"modifier":"EXACT"},"end":{"value":516,"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":13,"modifier":"EXACT"},"end":{"value":13,"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":13,"modifier":"EXACT"},"end":{"value":13,"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":14,"modifier":"EXACT"},"end":{"value":19,"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":71,"modifier":"EXACT"},"end":{"value":71,"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":71,"modifier":"EXACT"},"end":{"value":71,"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":139,"modifier":"EXACT"},"end":{"value":139,"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":146,"modifier":"EXACT"},"end":{"value":148,"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":186,"modifier":"EXACT"},"end":{"value":191,"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":186,"modifier":"EXACT"},"end":{"value":191,"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":222,"modifier":"EXACT"},"end":{"value":222,"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":222,"modifier":"EXACT"},"end":{"value":222,"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":240,"modifier":"EXACT"},"end":{"value":240,"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":353,"modifier":"EXACT"},"end":{"value":353,"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":381,"modifier":"EXACT"},"end":{"value":384,"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":404,"modifier":"EXACT"},"end":{"value":404,"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":469,"modifier":"EXACT"},"end":{"value":469,"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":"UP000534590"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489117.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489117.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4489117.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003502929.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CBCSCS010000009.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LGZ0","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92922795","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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":"MARYVFITGGVVSSLGKGIAAAALGALLQSRGYRVRLRKLDPYLNVDPGTMSPTQHGEVFVTDDGAETDLDLGHYERFTGRSATKTDNITTGRIYKNIIDKERRGDYLGATVQVIPHVTNEIKDFVIEGNDDYDFVICEIGGTVGDIEAMPFMEAIRQLGNDLPRGTAIYLHLTLMPYIPAAGELKTKPTQHSVKELQALGIHPDILLVRADREIPEAERRKLSLFCNVRPSAVIQALDVANIYDVPIAYHKEGLDSEVLAAFGIEPAPKPRLEPWEEVCNRIRTPEGEVTIAIVGKYTGLKDAYKSLIEALHHGGFANRVKVKLEWIESEVFEKEDPTPYLEKVNGILVPGGFGERGSEGKIMAAQFARERNVPYFGICFGMQMAVVEAARHLAGIENASSTEFGPTSEPVVGLMTEWVKGNELEKRSSKGDLGGTMRLGAYKAALKKDTKIAEIYGTTDISERHRHRYEVNVDYKDRLENCGLVFSGMSPDGVLPETVEYPDHPWFIGVQYHPELKSRPLDPHPLFASFVEAAVEQSRLV","length":542,"molWeight":60025,"crc64":"2DF80A92148EC338","md5":"196B75B95BDAC91F831A59AD1FB28848"},"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":"UPI0002331720"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LHD4","uniProtkbId":"A0ABD5LHD4_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-06-18","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488969.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"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":"MBB4488969.1"}],"value":"GGE40_000749"}]}],"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":"MBB4488969.1"}],"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":15,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":66,"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":63,"modifier":"EXACT"},"end":{"value":63,"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":123,"modifier":"EXACT"},"end":{"value":123,"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":127,"modifier":"EXACT"},"end":{"value":133,"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":156,"modifier":"EXACT"},"end":{"value":156,"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":159,"modifier":"EXACT"},"end":{"value":159,"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":258,"modifier":"EXACT"},"end":{"value":258,"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":321,"modifier":"EXACT"},"end":{"value":321,"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":373,"modifier":"EXACT"},"end":{"value":373,"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":410,"modifier":"EXACT"},"end":{"value":414,"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":439,"modifier":"EXACT"},"end":{"value":439,"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":440,"modifier":"EXACT"},"end":{"value":440,"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":"UP000534590"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488969.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488969.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4488969.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_060726323.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAAQPQ010000001.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LHD4","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92922648","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"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":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"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":"MTSLSQLSLFDPAVMASIDAAAGQSGIPLYDLMERAGQAVAASALRHYPQAQRFVVLCGGGNNGGDGYVAARALVESGAVVVVHHLGDAGTLRGDARMAFERSGMAPLPLGDYAPLAGDVVIDAVFGAGLSRDIPRELARIIEAVTNAKASVLAVDLPSGLCGRRGVPLGASFRAERTVTFMARKPGHLLMPGRELCGALEVFDIGIPSRILTDHAGSVAENHPLVWRDALPASDIETHKFRRGHLTVFSGPAHATGASRMTALAALKAGAGIVAVAAPRQALDVLSVTLTAVMNAPMDDADDLRLWLDDRRHGAFVLGPGFGDLEKARQFVSLLGDKAVVLDADAITAFKDHTETLFERITSGAGKFILTPHEGEFARLFPDLAADRVLSKIEKVQVASARSGAVLVYKGADTVIAAPDGRALVNTNAPASLATAGSGDVLAGIIGALLAQGAPAFEAAAAGVWLHGQAGHRAGDGMTAEDLAHAVRPFG","length":491,"molWeight":50803,"crc64":"2FC0C8C2187C5CB0","md5":"A2EB61462525C93E90805C5B429B797C"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI000762116C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LHQ6","uniProtkbId":"A0ABD5LHQ6_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4490320.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4490320.1"}],"value":"GGE40_002100"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4490320.1"}],"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":180,"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":401,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":311,"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":"UP000534590"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4490320.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4490320.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4490320.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_020811189.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP197629.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LHQ6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92924858","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"97365880","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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":"MTLSGKHILLIISGGIAAYKSLDLIRRLKERGAKVTPVMTKGAQEFVTPLAVGALSATHVFTELFSRQDEQDVGHIRLARDCDLVLVAPATADLMAKMAHGLADDLASTILLATDRKVLVAPAMNPKMWSAKPMVRNVETLKKDGVFFIGPMVGEMAEKGEAGFGRMAEPLQIVEAVAALLDEGPKPLNGKTAIVTSGPTHEPIDPVRYIANRSSGKQGHAIAAALAELGAKVTLVSGPVTIADPAGVETVHVERAEEMRDAVISRLPADIAVMVAAVADWRVTGSSEQKIKKQPGDAPLALQLTENPDILKTVGHHEKRPTLVVGFAAETQDIEKNGRAKLERKGADYIVANDVSAQTGIMGGDRNSVKIISADGVEAWPDLDKTEVAKRLAALIAEKLA","length":401,"molWeight":42573,"crc64":"9941BB0CDA08C7F5","md5":"B189C341525F9125AB2A456BDCB8AD3A"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI000370C93D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LI58","uniProtkbId":"A0ABD5LI58_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-06-18","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491300.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"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"}],"value":"ftsH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491300.1"}],"value":"GGE40_003131"}]}],"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":"MBB4491300.1"}],"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":"Transmembrane","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":126,"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":601,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":625,"modifier":"EXACT"},"end":{"value":637,"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:0000313","source":"EMBL","id":"MBB4491300.1"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491300.1"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"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":"UP000534590"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"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-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491300.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491300.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000002","properties":[{"key":"ProteinId","value":"MBB4491300.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003506249.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CBCSCS010000011.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LI58","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92924354","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"97366626","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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":"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":"MNPNFRNFALWAVIALLLIALFSMFQTSPTQTGSREIPYSQFLRDVDSGRVRDVTVTGNRVLGTYTENGTAFQTYSPVIDDSLMERLQSKNVTIVARPESDGSSGFLSYLGTLLPMFLILGVWLFFMRQMQGGSRGAMGFGKSKAKLLTEAHGRVTFDDVAGVDEAKQDLEEIVEFLRDPQKFQRLGGKIPRGVLLVGPPGTGKTLLARSVAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGIILIAATNRPDVLDPALLRPGRFDRQVVVPNPDIVGRERILKVHIRNVPLAPNVDLKILARGTPGFSGADLMNLVNEAALMAARRNKRVVTMQEFEDAKDKIMMGAERRSSAMTEAEKKLTAYHEAGHAITALKVAVADPLHKATIIPRGRALGMVMQLPEGDRYSMSYKWMVSRLVIMMGGRVAEELTFGKENITSGASSDIEQATKLARAMVTQWGFSDALGQVAYGENQQEVFLGHSVSQSKNVSEATAQTIDTEVRRLIDEAYTEARRILTDNHDGFVAIAEGLLEYETLTGDEIKALLRGEKPARDLGDDSPGSRGSAVPKAGAKKDGPSEAKGDGEAEGGMEPQPH","length":648,"molWeight":70563,"crc64":"BAE070FBCAF025E5","md5":"858A9F0758FFF47AA73F6C9C0A2107B1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":2},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":4},"uniParcId":"UPI00023332E6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LLK1","uniProtkbId":"A0ABD5LLK1_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488950.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00016090"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012916"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"2.6.1.16"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"D-fructose-6-phosphate amidotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"GFAT"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Glucosamine-6-phosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Hexosephosphate aminotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"L-glutamine--D-fructose-6-phosphate amidotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"glmS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488950.1"}],"value":"GGE40_000730"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"value":"Catalyzes the first step in hexosamine metabolism, converting fructose-6P into glucosamine-6P using glutamine as a nitrogen source"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054671"}],"value":"Involved in the production of the root hair deformation (HAD) factor specifically on medicago"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-fructose 6-phosphate + L-glutamine = D-glucosamine 6-phosphate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13237"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:58725"},{"database":"ChEBI","id":"CHEBI:61527"}],"ecNumber":"2.6.1.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001031"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"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_00164"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488950.1"}],"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":"Initiator methionine","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":1,"modifier":"EXACT"}},"description":"Removed","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]},{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"Glutamine amidotransferase type-2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51278"}]},{"type":"Domain","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"SIS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51464"}]},{"type":"Domain","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":598,"modifier":"EXACT"}},"description":"SIS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51464"}]},{"type":"Active site","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}]},{"type":"Active site","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Nucleophile; for GATase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]},{"type":"Active site","location":{"start":{"value":603,"modifier":"EXACT"},"end":{"value":603,"modifier":"EXACT"}},"description":"For Fru-6P isomerization activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022576"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00797"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00609"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00164"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488950.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488950.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4488950.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_020809235.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CBCSCS010000021.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LLK1","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92922629","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004360","properties":[{"key":"GoTerm","value":"F:L-glutamine:D-fructose-6-phosphate transaminase (isomerizing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046349","properties":[{"key":"GoTerm","value":"P:amino sugar biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006487","properties":[{"key":"GoTerm","value":"P:protein N-linked glycosylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006047","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00714","properties":[{"key":"EntryName","value":"GFAT"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05008","properties":[{"key":"EntryName","value":"SIS_GlmS_GlmD_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05009","properties":[{"key":"EntryName","value":"SIS_GlmS_GlmD_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000001","properties":[{"key":"EntryName","value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000002","properties":[{"key":"EntryName","value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.20.10:FF:000006","properties":[{"key":"EntryName","value":"Glutamine--fructose-6-phosphate aminotransferase [isomerizing]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10490","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase like protein, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.60.20.10","properties":[{"key":"EntryName","value":"Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00164","properties":[{"key":"EntryName","value":"GlmS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017932","properties":[{"key":"EntryName","value":"GATase_2_dom"}]},{"database":"InterPro","id":"IPR005855","properties":[{"key":"EntryName","value":"GFAT"}]},{"database":"InterPro","id":"IPR047084","properties":[{"key":"EntryName","value":"GFAT_N"}]},{"database":"InterPro","id":"IPR035466","properties":[{"key":"EntryName","value":"GlmS/AgaS_SIS"}]},{"database":"InterPro","id":"IPR035490","properties":[{"key":"EntryName","value":"GlmS/FrlB_SIS"}]},{"database":"InterPro","id":"IPR029055","properties":[{"key":"EntryName","value":"Ntn_hydrolases_N"}]},{"database":"InterPro","id":"IPR001347","properties":[{"key":"EntryName","value":"SIS_dom"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01135","properties":[{"key":"EntryName","value":"glmS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001484","properties":[{"key":"EntryName","value":"PRK00331.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10937","properties":[{"key":"EntryName","value":"GLUCOSAMINE--FRUCTOSE-6-PHOSPHATE AMINOTRANSFERASE, ISOMERIZING"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10937:SF0","properties":[{"key":"EntryName","value":"GLUTAMINE--FRUCTOSE-6-PHOSPHATE TRANSAMINASE (ISOMERIZING)"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13537","properties":[{"key":"EntryName","value":"GATase_7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01380","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF56235","properties":[{"key":"EntryName","value":"N-terminal nucleophile aminohydrolases (Ntn hydrolases)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51278","properties":[{"key":"EntryName","value":"GATASE_TYPE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51464","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MCGIVGIVGTQPVAERLVDALKRLEYRGYDSAGVATIDNGAMDRRRAEGKLFNLEKRLSEEPLPGVVGIAHTRWATHGVPNETNAHPHFVDGVAVVHNGIIENFSELRDELSAEGATFTTQTDTEVVAQLLAKYTREGLGHREAMLKMLNRVTGAYALVVMFKDDPGTLLSARSGPPLAVGYGRGEMFLGSDAIALSPFTNEITYLVDGDCAILTRQGAEIIDFSGKPVKRERQISQATAFVVDKGNHRHFMEKEIYEQPEVISHALSHYVDFASKTVKQADTAIDFAKLSGLAISACGTAYLSGLIGKYWFERYARLPVEIDVASEFRYREIPLVPTQAALFISQSGETADTLAALRYCQQEGLKIGAVVNTRESTMARESDAIFPILAGPEIGVASTKAFTCQLAVLASLAVAAGKARGTITPQQETELVRHLTEMPRIMSKVLNSIQPQIEALSRDLSRFKDVLYLGRGTSFPLALEGALKLKEISYIHAEGYAAGELKHGPIALIDENMPVIVIAPHDRFFEKTVSNMQEVAARGGRIIFITDEKGAAASKLDTMATITLPNVDELIAPMVFSLPIQLLAYHTAVFMGTDVDQPRNLAKSVTVE","length":608,"molWeight":66192,"crc64":"5701DCAF8F6B2AF5","md5":"1DCD238BCBF4EAB5791DC2D0CAB82380"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Initiator methionine":1,"Domain":3,"Active site":3},"uniParcId":"UPI00036C688F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LM37","uniProtkbId":"A0ABD5LM37_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488949.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488949.1"}],"value":"GGE40_000729"}]}],"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":"MBB4488949.1"}],"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":7,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"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":82,"modifier":"EXACT"},"end":{"value":83,"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":105,"modifier":"EXACT"},"end":{"value":107,"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":107,"modifier":"EXACT"},"end":{"value":107,"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":143,"modifier":"EXACT"},"end":{"value":143,"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":157,"modifier":"EXACT"},"end":{"value":157,"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":172,"modifier":"EXACT"},"end":{"value":172,"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":229,"modifier":"EXACT"},"end":{"value":229,"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":229,"modifier":"EXACT"},"end":{"value":229,"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":318,"modifier":"EXACT"},"end":{"value":318,"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":336,"modifier":"EXACT"},"end":{"value":336,"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":351,"modifier":"EXACT"},"end":{"value":351,"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":362,"modifier":"EXACT"},"end":{"value":362,"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":365,"modifier":"EXACT"},"end":{"value":365,"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":371,"modifier":"EXACT"},"end":{"value":372,"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":390,"modifier":"EXACT"},"end":{"value":390,"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":408,"modifier":"EXACT"},"end":{"value":408,"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":425,"modifier":"EXACT"},"end":{"value":425,"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":"UP000534590"}],"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-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488949.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488949.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4488949.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_020809234.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAAQPQ010000001.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LM37","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92922628","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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:InterPro"}]},{"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":"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":"NF010933","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"2"}]},{"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":"MERSSLAIILAAGDSTRMKSSKSKVLHPVAGRPMIAHVVEAVAGSGVGTVALVVGRDADNVTAAASMKGIQVEAFLQTERKGTGHAVLAARAALERGFDDLIIAYGDVPLITSATLDRAREAIAAGADVAVIGFHTDRPTGYGRLLVENGELVAIREEKDATDAERKVTWCNSGLMAINGRNALDLLDRIGNSNVKGEYYLTDVVEIARSLGRRAVAIDAPEAELVGCNNRAELAFIEKLWQERRRHELMVDGVSMIAPETVFLSFDTKIGQDVLIEPNVVIGPGVTIEPGAVIHAFSHLEGAHVAEGAAVGPYARLRPGANLHANAKVGNFCEVKKAEIGEGAKVNHLTYIGDAFIGAGSNIGAGTITCNYDGYNKAETRIGANSFIGSNSSLVAPVTIGEGAYIASGSVITDDVPDDALAFGRARQEVKPGRATVVRERAKALKEAKKKSS","length":453,"molWeight":47698,"crc64":"AD8AAF678E8B2FC4","md5":"2E474B002AE9F2C5CA0886C32C729676"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":20},"uniParcId":"UPI00037A3B2C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LN05","uniProtkbId":"A0ABD5LN05_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488589.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488589.1"}],"value":"GGE40_000369"}]}],"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":"MBB4488589.1"}],"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":1162,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5048530928"},{"type":"Domain","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":743,"modifier":"EXACT"},"end":{"value":955,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1027,"modifier":"EXACT"},"end":{"value":1162,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":1027,"modifier":"EXACT"},"end":{"value":1162,"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":222,"modifier":"EXACT"},"end":{"value":222,"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":228,"modifier":"EXACT"},"end":{"value":228,"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":229,"modifier":"EXACT"},"end":{"value":229,"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":261,"modifier":"EXACT"},"end":{"value":261,"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":263,"modifier":"EXACT"},"end":{"value":263,"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":268,"modifier":"EXACT"},"end":{"value":268,"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":294,"modifier":"EXACT"},"end":{"value":294,"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":295,"modifier":"EXACT"},"end":{"value":295,"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":296,"modifier":"EXACT"},"end":{"value":296,"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":338,"modifier":"EXACT"},"end":{"value":338,"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":338,"modifier":"EXACT"},"end":{"value":338,"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":338,"modifier":"EXACT"},"end":{"value":338,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":354,"modifier":"EXACT"},"end":{"value":354,"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":354,"modifier":"EXACT"},"end":{"value":354,"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":779,"modifier":"EXACT"},"end":{"value":779,"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":839,"modifier":"EXACT"},"end":{"value":839,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":846,"modifier":"EXACT"},"end":{"value":846,"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":871,"modifier":"EXACT"},"end":{"value":871,"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":872,"modifier":"EXACT"},"end":{"value":872,"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":873,"modifier":"EXACT"},"end":{"value":873,"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":874,"modifier":"EXACT"},"end":{"value":874,"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":914,"modifier":"EXACT"},"end":{"value":914,"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":914,"modifier":"EXACT"},"end":{"value":914,"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":914,"modifier":"EXACT"},"end":{"value":914,"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":926,"modifier":"EXACT"},"end":{"value":926,"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":926,"modifier":"EXACT"},"end":{"value":926,"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":926,"modifier":"EXACT"},"end":{"value":926,"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":926,"modifier":"EXACT"},"end":{"value":926,"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":926,"modifier":"EXACT"},"end":{"value":926,"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":928,"modifier":"EXACT"},"end":{"value":928,"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":928,"modifier":"EXACT"},"end":{"value":928,"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":"UP000534590"}],"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-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488589.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4488589.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4488589.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_020808737.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM139109.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LN05","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92922265","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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_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":"3"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRQDIKSILIIGAGPIVIGQACEFDYSGTQACKALKEEGYRVILVNSNPATIMTDPGLADATYVEPITPEVVAKIIAKERPDALLPTMGGQTALNTALSLKRMGVLDRYNVEMIGAKPEAIDMAEDRALFREAMARIGLETPKSMLANATEIKDADRKKHEAARTELKGKLSGPDLDKALDDLENQWNLGETDRKQRYMAHAMAIAAQAIDHVGLPAIIRPSFTLGGTGGGIAYNRSEFFDIVSGGLDASPTTEVLVEESVLGWKEYEMEVVRDTADNCIIICSIENIDPMGVHTGDSITVAPALTLTDKEYQIMRNASIAVLREIGVETGGSNVQFAVNPKDGRLVVIEMNPRVSRSSALASKATGFPIAKIAAKLAIGYTLDELENDITGGATPASFEPSIDYVVTKIPRFAFEKFPGASPILTTAMKSVGEVMAIGRTFAESLQKALRGMETGLTGLDEIEIPGFEEGEGSKNAIRAAIGTPTPDRLRMVAQALRMGMTAEEVHENSKIDPWFIAQFKAIVDMEARIREQGLPQDAENLRMLKAMGFSDARLAILTGKRPKEVAELRNSLNVRPVFKRIDTCAAEFASPTAYMYSTYEIPFVGAARSEAQVSDRKKVVILGGGPNRIGQGIEFDYCCCHAAFALKDAGFEAIMINCNPETVSTDYDTSDRLYFEPLTAEDVIEIMRAEQERGELVGVIVQFGGQTPLKLAEALEKNGIPILGTAPDMIDLAEDRDRFQKLLMKLDLAQPNNGIAYSVEQARLVASEIGFPLVVRPSYVLGGRAMQIIHSEGQLQTYLLDTVPGLVPEDIKQRYPNDKTGQINTLLGKNPLLFDSYLTNAVEVDVDALCDGENVFVSGIMEHIEEAGIHSGDSACSLPSRSLSKETLDELERQTTALAKALNVGGLMNVQYAIKDGTIYVLEVNPRASRTVPFVAKTIGAPIAKIAARVMAGEKLDAAIAAYGQKPDPRNLKHIAVKEAVFPFARFPGVDILLGPEMRSTGEVIGLDTDFALAFAKSQLGAGVDLPRSGTVFVSVRDDDKEGVLPAIRILVESGFKVLATGGTQRFLAEQGINAEKINKVQEGRPHIEDAIRNRQVQLVINTTDSNKAISDSKSLRRATLMQKVPYYTTMAGAEAAALAIKALKAGNLEVKPLQSYFN","length":1162,"molWeight":125888,"crc64":"802123D1A1A20D02","md5":"764EADC7B0CE32AD19747BC80036B16D"},"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":2,"Binding site":38,"Lipidation":2},"uniParcId":"UPI0003790316"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LPE9","uniProtkbId":"A0ABD5LPE9_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489276.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme IspD/IspF"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2.7.7.60"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4-diphosphocytidyl-2C-methyl-D-erythritol synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MEP cytidylyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MCT"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECDP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4.6.1.12"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"ispDF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489276.1"}],"value":"GGE40_001056"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13429"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:57823"},{"database":"ChEBI","id":"CHEBI:58262"}],"ecNumber":"2.7.7.60","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001282"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23864"},{"database":"ChEBI","id":"CHEBI:57919"},{"database":"ChEBI","id":"CHEBI:58483"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"4.6.1.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000200"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001968"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004787"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004709"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009789"}],"value":"Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008480"}],"value":"Belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the C-terminal section; belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489276.1"}],"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":236,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02542"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Region","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0414","category":"Biological process","name":"Isoprene biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"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_01520"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"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_01520"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489276.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4489276.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000001","properties":[{"key":"ProteinId","value":"MBB4489276.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_003502618.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CM139109.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LPE9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"92923013","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008685","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050518","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019288","properties":[{"key":"GoTerm","value":"P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016114","properties":[{"key":"GoTerm","value":"P:terpenoid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02516","properties":[{"key":"EntryName","value":"CDP-ME_synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00554","properties":[{"key":"EntryName","value":"MECDP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.550.10:FF:000003","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1330.50","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},{"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_00108","properties":[{"key":"EntryName","value":"IspD"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01520","properties":[{"key":"EntryName","value":"IspDF"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00107","properties":[{"key":"EntryName","value":"IspF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001228","properties":[{"key":"EntryName","value":"IspD"}]},{"database":"InterPro","id":"IPR026596","properties":[{"key":"EntryName","value":"IspD/F"}]},{"database":"InterPro","id":"IPR034683","properties":[{"key":"EntryName","value":"IspD/TarI"}]},{"database":"InterPro","id":"IPR018294","properties":[{"key":"EntryName","value":"ISPD_synthase_CS"}]},{"database":"InterPro","id":"IPR003526","properties":[{"key":"EntryName","value":"MECDP_synthase"}]},{"database":"InterPro","id":"IPR020555","properties":[{"key":"EntryName","value":"MECDP_synthase_CS"}]},{"database":"InterPro","id":"IPR036571","properties":[{"key":"EntryName","value":"MECDP_synthase_sf"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"NCBIfam","id":"TIGR00453","properties":[{"key":"EntryName","value":"ispD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00151","properties":[{"key":"EntryName","value":"ispF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006899","properties":[{"key":"EntryName","value":"PRK09382.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181:SF1","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01128","properties":[{"key":"EntryName","value":"IspD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02542","properties":[{"key":"EntryName","value":"YgbB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69765","properties":[{"key":"EntryName","value":"IpsF-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01295","properties":[{"key":"EntryName","value":"ISPD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01350","properties":[{"key":"EntryName","value":"ISPF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLGIVIVAAGRGERAGSPQEGPKQYRPIGGRAVIEHTLATFLGWNGASPIVVVSHADDKALLSPVLQRLDAGERIVTVTGGATRQQSVLAGLEALASEELTHVMIHDAVRPFVAVDMLERIIALHQAGATGVLPALPVTDTLKRGSDDLVVQTVSRQGLYAAQTPQSFNYGDILRAHRAAAASGKTDFTDDASIAEWAGLTVTLTEGSVDNVKLTLKRDIAMADEKLSHGLPDVRTGNGYDVHQLEAGDGVTLCGIFIEHDQRLKGHSDADVALHALTDALLATCGAGDIGDHFPPSDPQWKGAASRIFLEHAAKVVRDNGGTIMNADVSLIAEAPRIGPHRQAMREALSDMLGIALERCSVKATTNETIGFVGRREGIAAIATATVVYRGRPL","length":395,"molWeight":41746,"crc64":"F7D2E1B3C6969F76","md5":"346DD6639BD1020AEE08EA853830DB7D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":9,"Site":6},"uniParcId":"UPI000233100A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABD5LQF5","uniProtkbId":"A0ABD5LQF5_AGRRD","entryAudit":{"firstPublicDate":"2025-06-18","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-06-18","entryVersion":6,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491898.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine hydroxymethyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"SHMT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"2.1.2.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"glyA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491898.1"}],"value":"GGE40_003740"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057572"}],"value":"Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = 2-methylserine + (6S)-5,6,7,8-tetrahydrofolate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:58275"}],"ecNumber":"2.1.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051216"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15481"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57453"}],"ecNumber":"2.1.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"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_00051"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006376"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Belongs to the SHMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491898.1"}],"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":11,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Plays an important role in substrate specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]},{"type":"Modified residue","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"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_00051"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491898.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491898.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000003","properties":[{"key":"ProteinId","value":"MBB4491898.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_080864576.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JACIGN010000004.1"}]},{"database":"AlphaFoldDB","id":"A0ABD5LQF5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"97367186","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000534590","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:0050413","properties":[{"key":"GoTerm","value":"F:D-alanine 2-hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00378","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000001","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00051","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"InterPro","id":"IPR001085","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase"}]},{"database":"InterPro","id":"IPR049943","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase-like"}]},{"database":"InterPro","id":"IPR019798","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase_PLP_BS"}]},{"database":"InterPro","id":"IPR039429","properties":[{"key":"EntryName","value":"SHMT-like_dom"}]},{"database":"NCBIfam","id":"NF000586","properties":[{"key":"EntryName","value":"PRK00011.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680:SF35","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00464","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000412","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00096","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLNRLSHNTVSDTVIADAIAEELDRQKTQIELIASENIVSADVLAAQGSVLTNKYAEGYPGKRYYGGCEFVDKVEQVAIDRLKQLFGAEFANVQPHSGAQANQAVFLALLQPGDRIMGMSLAHGGHLTHGSPVTMSGKWFDVVSYEVDADTHLIDMEKVRARALETKPKLIVAGASAYPRQIDFAGFRRIADEVGAYLMVDMAHYAGLIAGGKYPNPVPHAHVVTSTTHKTLRGPRGGVILTNDADLAKKLNSAVFPGNQGGPLMHVIAAKAVAFGEALRPEFSDYAGQVIANAQALAKVLTKGGLGIVSGGTDSHMVLVDLRPKGVTGKVAEIALERAGLTCNKNAIPNDPEKPFVTSGVRLGSSAGTTRGFGVAEFEQIGALILRVIDALAANAEGDAAVEAEVRGEVAALCEAFPIYGS","length":422,"molWeight":44508,"crc64":"F8E118656A5C15E3","md5":"BD8C0E4C07F92C8D91D526DC2AF95CD9"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":2,"Site":1,"Modified residue":1},"uniParcId":"UPI0009BC688D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6J7Y4","uniProtkbId":"A0ABR6J7Y4_AGRRD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Agrobacterium radiobacter","taxonId":362,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Rhizobiaceae","Rhizobium/Agrobacterium group","Agrobacterium","Agrobacterium tumefaciens complex"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030902"}],"value":"D-malate dehydrogenase [decarboxylating]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013126"}],"value":"1.1.1.83"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013144"}],"value":"1.1.1.93"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012223"}],"value":"4.1.1.73"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491053.1"}],"value":"GGE40_002884"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004033"}],"value":"Has multiple catalytic activities. Apart from catalyzing the oxidation of (+)-tartrate to oxaloglycolate, also converts meso-tartrate to D-glycerate and catalyzes the oxidative decarboxylation of D-malate to pyruvate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R,3R)-tartrate + H(+) = (R)-glycerate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13317"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:16659"},{"database":"ChEBI","id":"CHEBI:30924"}],"ecNumber":"4.1.1.73","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001421"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R,3R)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15209"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30924"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58265"}],"ecNumber":"1.1.1.93","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048069"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R,3S)-tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30928"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58265"}],"ecNumber":"1.1.1.93","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048855"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-malate + NAD(+) = pyruvate + CO2 + NADH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18365"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15588"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.83","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049301"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tartrate + NAD(+) = 2-hydroxy-3-oxosuccinate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18853"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30929"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58265"}],"ecNumber":"1.1.1.93","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049377"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001958"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}]},{"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":"ARBA00004981"}],"value":"Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy-3-oxosuccinate from L-tartrate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005110"}],"value":"Carbohydrate acid metabolism; tartrate degradation; 2-hydroxy-3-oxosuccinate from meso-tartrate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004803"}],"value":"Carbohydrate acid metabolism; tartrate degradation; D-glycerate from L-tartrate: step 1/1"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007769"}],"value":"Belongs to the isocitrate and isopropylmalate dehydrogenases family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491053.1"}],"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":342,"modifier":"EXACT"}},"description":"Isopropylmalate dehydrogenase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01329"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491053.1"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"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":"ARBA00023027"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491053.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-SFHRA5RFMADG","citationType":"submission","authors":["Whitman W."],"title":"Genomic Encyclopedia of Type Strains, Phase IV (KMG-V): Genome sequencing to study the core and pangenomes of soil and plant-associated prokaryotes.","publicationDate":"AUG-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}],"value":"SEMIA 461","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB4491053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000534590"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JACIHP010000002","properties":[{"key":"ProteinId","value":"MBB4491053.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_135521599.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JACIGN010000002.1"}]},{"database":"Proteomes","id":"UP000534590","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:0046553","properties":[{"key":"GoTerm","value":"F:D-malate dehydrogenase (decarboxylating) (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050319","properties":[{"key":"GoTerm","value":"F:tartrate decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009027","properties":[{"key":"GoTerm","value":"F:tartrate dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"Gene3D","id":"3.40.718.10","properties":[{"key":"EntryName","value":"Isopropylmalate Dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050501","properties":[{"key":"EntryName","value":"ICDH/IPMDH"}]},{"database":"InterPro","id":"IPR019818","properties":[{"key":"EntryName","value":"IsoCit/isopropylmalate_DH_CS"}]},{"database":"InterPro","id":"IPR024084","properties":[{"key":"EntryName","value":"IsoPropMal-DH-like_dom"}]},{"database":"InterPro","id":"IPR011829","properties":[{"key":"EntryName","value":"TTC_DH"}]},{"database":"NCBIfam","id":"TIGR02089","properties":[{"key":"EntryName","value":"TTC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43275","properties":[{"key":"EntryName","value":"D-MALATE DEHYDROGENASE [DECARBOXYLATING]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43275:SF1","properties":[{"key":"EntryName","value":"D-MALATE DEHYDROGENASE [DECARBOXYLATING]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00180","properties":[{"key":"EntryName","value":"Iso_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01329","properties":[{"key":"EntryName","value":"Iso_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53659","properties":[{"key":"EntryName","value":"Isocitrate/Isopropylmalate dehydrogenase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00470","properties":[{"key":"EntryName","value":"IDH_IMDH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKTHRIALIPGDGVGKSVTDAAWQVLNAAAQTSGFALEGTEFPWSCAFYKETGAMMPKDGIETLRGFDAILLGAVGWPAEVPDSVSLHGLLLPIRKAFVQYANIRPHRLLPGVQGPLKADGFDILCIRENTEGEYSGAGGRVHQGTDDEVAVETSIFTRKGVERILRFGFEQAQKRRGKLASITKSNAQKYSMVFWDEVTHKLAAEYPDVEVSSYHIDAMAARMVMAPESLDVVVASNLFGDILTDLGAAIQGGLGFAASANINPDRSAPSMFEPVHGSAPDIAHLGIANPIAAIWSGAMMLEHLGEKDAAVRIMTALETATGRGIGTVPGKDKTDAITAAILAALD","length":347,"molWeight":36898,"crc64":"451137DAD2C7325A","md5":"D7DB974B50179EF4C6A199DFEC69AAF4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":3,"PATHWAY":3,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI001080A613"}}]}