{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QSA4","uniProtkbId":"A0ABW2QSA4_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418617.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"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":"MFC7418617.1"}],"value":"ACFQNF_01830"}]}],"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":"MFC7418617.1"}],"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":27,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":406,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"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":112,"modifier":"EXACT"},"end":{"value":118,"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":154,"modifier":"EXACT"},"end":{"value":155,"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":181,"modifier":"EXACT"},"end":{"value":181,"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":189,"modifier":"EXACT"},"end":{"value":189,"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":382,"modifier":"EXACT"},"end":{"value":382,"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":406,"modifier":"EXACT"},"end":{"value":409,"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":462,"modifier":"EXACT"},"end":{"value":462,"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":466,"modifier":"EXACT"},"end":{"value":466,"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":221,"modifier":"EXACT"},"end":{"value":221,"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":"MFC7418617.1"}],"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":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000004","properties":[{"key":"ProteinId","value":"MFC7418617.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185696.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000004.1"}]},{"database":"Proteomes","id":"UP001596473","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":"MKAVSWNLPTLDLPAIDAIAANARLVVDSRNIQPGDVFLAFEGEYADGRSYIADAIAAGAAAVLWEAEEFVWDPAWQTPNLAIPQLRAQAGIVAAHLLANPSRSMFVTGITGTNGKTSIANWLAQAFNLLGHKTGVLGTLGNGFIDKLESSTHTTLDPVTLQGWLSRLHGEGASHIAMEVSSHGLEQGRVHGTDFDVAVFTNLTRDHLDYHGDMASYGAAKAKLFAWEGLKVAVINTDDAFGRELASQCKAPRVLTYGLENGGIRATSVELTLSGLEMEVATPYGLCNISSPMLGRFNASNLLACLSVLLAADVPLAKAAHILGQIQPAAGRMQKLGGDERPLVVVDYAHTPDALEKALATLRESMPEKSRLYCIFGCGGDRDKGKRPLMGEIACRLADAVIITSDNPRSETPQAIIQDIVRGVSGVPGTGHANYSIDSDRASAIVDAIDVASAKDVVLIAGKGHETYQEIAGIRHPFDDVAIANRALARKKK","length":493,"molWeight":52416,"crc64":"6961C08AD8E58FC1","md5":"E0664C7AE1A0AFA516B862783EB4D97C"},"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":"UPI00360E64F9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QSV4","uniProtkbId":"A0ABW2QSV4_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418832.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418832.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418832.1"}],"value":"ACFQNF_02955"}]}],"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":"MFC7418832.1"}],"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":122,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Domain","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Mannose-1-phosphate guanyltransferase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF25087"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"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":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":104,"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":104,"modifier":"EXACT"},"end":{"value":104,"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":139,"modifier":"EXACT"},"end":{"value":139,"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":154,"modifier":"EXACT"},"end":{"value":154,"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":169,"modifier":"EXACT"},"end":{"value":169,"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":227,"modifier":"EXACT"},"end":{"value":227,"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":227,"modifier":"EXACT"},"end":{"value":227,"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":333,"modifier":"EXACT"},"end":{"value":333,"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":366,"modifier":"EXACT"},"end":{"value":366,"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":377,"modifier":"EXACT"},"end":{"value":377,"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":380,"modifier":"EXACT"},"end":{"value":380,"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":386,"modifier":"EXACT"},"end":{"value":387,"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":405,"modifier":"EXACT"},"end":{"value":405,"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":423,"modifier":"EXACT"},"end":{"value":423,"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":440,"modifier":"EXACT"},"end":{"value":440,"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":"UP001596473"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000006","properties":[{"key":"ProteinId","value":"MFC7418832.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185968.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000006.1"}]},{"database":"Proteomes","id":"UP001596473","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":"IPR056729","properties":[{"key":"EntryName","value":"GMPPB_C"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25087","properties":[{"key":"EntryName","value":"GMPPB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSALLDVVVLAAGQGKRMYSKMPKVLHRLAGKPLLGHVLDTARHLKPSKLVVVYGHGGQQVQEELLGSKDLAWAHQAEQLGTGHALAQALPHLQGETTLMLYGDVPLTRLATLQALLAASSQGKLGILTDILDDATGYGRIVRDAEGKVTCIVEQKDASPEQAAIKEMNTGILVLPTAKLAGWLSELKNDNAQGEYYATDLIALAVRDGIEIATVHPQDHWEAEGINNKVQLAQLERIHQAEIAQSLLLAGVSLIDPARIDVRGTLRHGMDVIIDVNCVFEGEVILGENVKVGANCVLKNVTINDDTIIHPFSHLENAVVGKGNLIGPFARLRPGAELADDVHIGNFVEIKKATIGKGSKVNHLSYIGDTTMGSKVNVGAGTITANYDGVNKFRTVIEDEVRIGSNNVLVAPVTIGTGATTGAGSVISKNAPAGELTVARAKQVTIYGWQRPVKK","length":455,"molWeight":48463,"crc64":"E4ECE617C3EF80BE","md5":"D98E092C25987E5FA876BBC906AECD06"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":20},"uniParcId":"UPI00360AB851"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QT85","uniProtkbId":"A0ABW2QT85_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418566.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"RecBCD enzyme subunit RecB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"3.1.11.5"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"DNA 3'-5' helicase subunit RecB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Exonuclease V subunit RecB"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"ExoV subunit RecB"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Helicase/nuclease RecBCD subunit RecB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418566.1"}],"value":"recB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418566.1"}],"value":"ACFQNF_01575"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.","ecNumber":"3.1.11.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Belongs to the helicase family. UvrD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418566.1"}],"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":1,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"UvrD-like helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51198"}]},{"type":"Domain","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":757,"modifier":"EXACT"}},"description":"UvrD-like helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51217"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":873,"modifier":"EXACT"}},"description":"DNA-binding and helicase activity, interacts with RecC","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":933,"modifier":"EXACT"},"end":{"value":1216,"modifier":"EXACT"}},"description":"Nuclease activity, interacts with RecD and RecA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":945,"modifier":"EXACT"},"end":{"value":973,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":946,"modifier":"EXACT"},"end":{"value":955,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":956,"modifier":"EXACT"},"end":{"value":969,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":1118,"modifier":"EXACT"},"end":{"value":1118,"modifier":"EXACT"}},"description":"For nuclease activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00560"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":991,"modifier":"EXACT"},"end":{"value":991,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1105,"modifier":"EXACT"},"end":{"value":1105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1118,"modifier":"EXACT"},"end":{"value":1118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000003","properties":[{"key":"ProteinId","value":"MFC7418566.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185633.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000003.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009338","properties":[{"key":"GoTerm","value":"C:exodeoxyribonuclease V complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008854","properties":[{"key":"GoTerm","value":"F:exodeoxyribonuclease V activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd22352","properties":[{"key":"EntryName","value":"RecB_C-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.320.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.486.10","properties":[{"key":"EntryName","value":"PCRA, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3170.10","properties":[{"key":"EntryName","value":"Recbcd, chain B, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01485","properties":[{"key":"EntryName","value":"RecB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011604","properties":[{"key":"EntryName","value":"PDDEXK-like_dom_sf"}]},{"database":"InterPro","id":"IPR038726","properties":[{"key":"EntryName","value":"PDDEXK_AddAB-type"}]},{"database":"InterPro","id":"IPR004586","properties":[{"key":"EntryName","value":"RecB"}]},{"database":"InterPro","id":"IPR011335","properties":[{"key":"EntryName","value":"Restrct_endonuc-II-like"}]},{"database":"InterPro","id":"IPR000212","properties":[{"key":"EntryName","value":"UvrD-like"}]},{"database":"InterPro","id":"IPR014016","properties":[{"key":"EntryName","value":"UvrD-like_ATP-bd"}]},{"database":"InterPro","id":"IPR014017","properties":[{"key":"EntryName","value":"UvrD-like_C"}]},{"database":"NCBIfam","id":"TIGR00609","properties":[{"key":"EntryName","value":"recB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070:SF23","properties":[{"key":"EntryName","value":"RECBCD ENZYME SUBUNIT RECB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070","properties":[{"key":"EntryName","value":"UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12705","properties":[{"key":"EntryName","value":"PDDEXK_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00580","properties":[{"key":"EntryName","value":"UvrD-helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13361","properties":[{"key":"EntryName","value":"UvrD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52980","properties":[{"key":"EntryName","value":"Restriction endonuclease-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51198","properties":[{"key":"EntryName","value":"UVRD_HELICASE_ATP_BIND"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51217","properties":[{"key":"EntryName","value":"UVRD_HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNLHPLNLFEMPLAGPHMIEASAGTGKTWTITGLYTRLVIEHGLKVPEILVVTFTEAATAELRDRIRGRLAEVLESFEGEEALDPFCEQLLIQHADRRQEVMRRLQRAIASLDEAAIHTIHAFCQRVLIQSAFESGADFGMEILSDTGPVLDEIAADFWREQVYPADAIYTEYLLKSKASPEEWLRVVYGHLGQPLLHTVELGMAADTAELSAALPAAFENYRQLWNEHSAVIKEMLLGQSLCKALKQTSYKPEQLEKVFLLIDDHIAGNGGWQDIDSKELIKLSSSKLISGTAKGKTPPEHAFFDAVELLASLINDLSSACQLRQKQGLAELRRRCDIELPERLARRQQLSFNDLLLRVWQGLTAEGGERLAIAMRRRYKAALIDEFQDTDGIQYDIFSRVFADGSTPLFLVGDPKQAIYSFRGADIHAYHQAEALVDAKESLDTNQRSVPALVTAVNTLFERPSEAFVDPHVSFSAVKAASKPRPELIVDGENDATDEERKSAPFRFQFLPEPEGVSDKGVQISWPKETANHLAAQITAQEIERLLRLAGEGKAKLADKPLSGGDMAVLVPDRFRAKAMQDALTQLGVPSVLRVRDSVWESQEAVELYTVLAAISEPAKQGLVRAALISTLLGNNAATLLRLEINGWDQIADAFAHWKKLWQTQGLIPMFREWLEYQGLDGRNVAQRLLSLSDGERRLTNLLQLAELLQAHKATGLEQHLAWFSRQNKNAGDEALLRLESDEDRVRIVTLHASKGLEYPIVFCPFLWDGRLLGKHTEAVRFHQDDKAWLDLGSDDFDEHKDSAKREAFEEKLRLLYVGLTRARNRCYIVWGNIGLKDGRGYAISDGLSQSAMAWLLHPLAGEHSDVLEAQKEHLKAYDHETLLGEITAMCLQQPEVFALHDAPSASGPGLKIAPSEPLVFKPYLGKKLYPTWRVASFSGMTAHNHSEGPDRDSASSAPEADSSTAPEGRSVFSFPEREAAATVAGTCLHAILEEWDWQDADTLLATTGKALEHHGIPEHWLEIVSQMVQDTVSARLDGKALTLASIPPKNRVAEMEFTYSVSHCQPERLIAALQHPSLPIEFRAAASTLDFFHINGFLRGFIDLVFEYENSYFVLDYKSNWLGNSVADYAPAKLIPAMAQHHYYLQYLIYSAAVRRFLRQRLPNFTDDQFGGVYYLFMRGLGKQDGQNGVYFSRPSMELLDDIEVALMGNAVKT","length":1216,"molWeight":135861,"crc64":"9D249AB56AD1F9A2","md5":"9A36C270C2442799B9B514E1467B677C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Compositional bias":2,"Active site":1,"Binding site":4},"uniParcId":"UPI0036191167"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QUU7","uniProtkbId":"A0ABW2QUU7_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7419507.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7419507.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7419507.1"}],"value":"ACFQNF_06405"}]}],"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":"MFC7419507.1"}],"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":2,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":388,"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":187,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"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":286,"modifier":"EXACT"},"end":{"value":286,"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":302,"modifier":"EXACT"},"end":{"value":305,"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":320,"modifier":"EXACT"},"end":{"value":320,"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":334,"modifier":"EXACT"},"end":{"value":334,"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":338,"modifier":"EXACT"},"end":{"value":338,"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":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000011","properties":[{"key":"ProteinId","value":"MFC7419507.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380187027.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000011.1"}]},{"database":"Proteomes","id":"UP001596473","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":"MSQKRIVLGVTGGVAAYKSVELVRLLTKASYEVQVVMTEAATHFVGPVTFQAVSGRPVFVDLWDGRAPNNMAHIDLTRGAHAIVVAPATADFMAKVANGFADDLLSTLVAARDCPLLLAPAMNRQMWENPPNQRNVAQLISDGVHILGPGEGEQACGEIGLGRMLEPEALLQHIDAFFQLKLLSGKRVLITAGPTFERIDAVRGITNSSSGKMGYAIARAAWESGADVVLVSGETALPTPLGCRRIDVVSAEEMLQAVNAEVEEADIFISVAAVSDYYVLNPSEQKIKKDAHILTLELGPNPDILANITARDNPPFCVGFAAESENLLEYAEAKRKRKKLPLLAANLVQNAMGSDENEIILLDDDGETRLTRAPKLDVARRLIAHIARLYQKR","length":393,"molWeight":42507,"crc64":"E24812809CCA0EDD","md5":"B87ED1D5725F7834EF2DFA8FF0419EF3"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":6},"uniParcId":"UPI00360FD839"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QWY6","uniProtkbId":"A0ABW2QWY6_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7419480.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Flavohemoprotein"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Flavohemoglobin"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Hemoglobin-like protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Nitric oxide dioxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"NO oxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"NOD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"1.14.12.17"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7419480.1"}],"value":"hmpA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"hmp"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7419480.1"}],"value":"ACFQNF_06265"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025094"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Is involved in NO detoxification in an aerobic process, termed nitric oxide dioxygenase (NOD) reaction that utilizes O(2) and NAD(P)H to convert NO to nitrate, which protects the bacterium from various noxious nitrogen compounds. Therefore, plays a central role in the inducible response to nitrosative stress"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 nitric oxide + NADH + 2 O2 = 2 nitrate + NAD(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19469"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16480"},{"database":"ChEBI","id":"CHEBI:17632"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.14.12.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048649"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 nitric oxide + NADPH + 2 O2 = 2 nitrate + NADP(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19465"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16480"},{"database":"ChEBI","id":"CHEBI:17632"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.14.12.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049433"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Consists of two distinct domains; an N-terminal heme-containing oxygen-binding domain and a C-terminal reductase domain with binding sites for FAD and NAD(P)H"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008414"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Belongs to the globin family. Two-domain flavohemoproteins subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006401"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"In the C-terminal section; belongs to the flavoprotein pyridine nucleotide cytochrome reductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7419480.1"}],"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":1,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Globin","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS01033"}]},{"type":"Domain","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"FAD-binding FR-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51384"}]},{"type":"Region","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Reductase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Active site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Active site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"proximal binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Involved in heme-bound ligand stabilization and O-O bond activation","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Influences the redox potential of the prosthetic heme and FAD groups","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]},{"type":"Site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Influences the redox potential of the prosthetic heme and FAD groups","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022575"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0216","category":"Biological process","name":"Detoxification"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000356"}],"id":"KW-0561","category":"Biological process","name":"Oxygen transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01252"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000356"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000010","properties":[{"key":"ProteinId","value":"MFC7419480.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380186979.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000010.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071949","properties":[{"key":"GoTerm","value":"F:FAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008941","properties":[{"key":"GoTerm","value":"F:nitric oxide dioxygenase [NAD(P)H] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019825","properties":[{"key":"GoTerm","value":"F:oxygen binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005344","properties":[{"key":"GoTerm","value":"F:oxygen carrier activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071500","properties":[{"key":"GoTerm","value":"P:cellular response to nitrosative stress"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046210","properties":[{"key":"GoTerm","value":"P:nitric oxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd14779","properties":[{"key":"EntryName","value":"FHP_Ae-globin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd06184","properties":[{"key":"EntryName","value":"flavohem_like_fad_nad_binding"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.490.10:FF:000003","properties":[{"key":"EntryName","value":"Flavohemoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.10:FF:000034","properties":[{"key":"EntryName","value":"Flavohemoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.80:FF:000010","properties":[{"key":"EntryName","value":"Flavohemoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.490.10","properties":[{"key":"EntryName","value":"Globins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.80","properties":[{"key":"EntryName","value":"Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01252","properties":[{"key":"EntryName","value":"Hmp"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008333","properties":[{"key":"EntryName","value":"Cbr1-like_FAD-bd_dom"}]},{"database":"InterPro","id":"IPR017927","properties":[{"key":"EntryName","value":"FAD-bd_FR_type"}]},{"database":"InterPro","id":"IPR001709","properties":[{"key":"EntryName","value":"Flavoprot_Pyr_Nucl_cyt_Rdtase"}]},{"database":"InterPro","id":"IPR039261","properties":[{"key":"EntryName","value":"FNR_nucleotide-bd"}]},{"database":"InterPro","id":"IPR000971","properties":[{"key":"EntryName","value":"Globin"}]},{"database":"InterPro","id":"IPR009050","properties":[{"key":"EntryName","value":"Globin-like_sf"}]},{"database":"InterPro","id":"IPR012292","properties":[{"key":"EntryName","value":"Globin/Proto"}]},{"database":"InterPro","id":"IPR023950","properties":[{"key":"EntryName","value":"Hmp"}]},{"database":"InterPro","id":"IPR001433","properties":[{"key":"EntryName","value":"OxRdtase_FAD/NAD-bd"}]},{"database":"InterPro","id":"IPR017938","properties":[{"key":"EntryName","value":"Riboflavin_synthase-like_b-brl"}]},{"database":"NCBIfam","id":"NF009805","properties":[{"key":"EntryName","value":"hmpA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43396","properties":[{"key":"EntryName","value":"FLAVOHEMOPROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43396:SF3","properties":[{"key":"EntryName","value":"FLAVOHEMOPROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00970","properties":[{"key":"EntryName","value":"FAD_binding_6"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00042","properties":[{"key":"EntryName","value":"Globin"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00175","properties":[{"key":"EntryName","value":"NAD_binding_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00371","properties":[{"key":"EntryName","value":"FPNCR"}]},{"database":"PRINTS","id":"PR00410","properties":[{"key":"EntryName","value":"PHEHYDRXLASE"}]},{"database":"SUPFAM","id":"SSF52343","properties":[{"key":"EntryName","value":"Ferredoxin reductase-like, C-terminal NADP-linked domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46458","properties":[{"key":"EntryName","value":"Globin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63380","properties":[{"key":"EntryName","value":"Riboflavin synthase domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51384","properties":[{"key":"EntryName","value":"FAD_FR"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01033","properties":[{"key":"EntryName","value":"GLOBIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLNAAQRDLVRATAPILKQHGVALTTHFYARMFQHNPELKQIFNEGNQQSGAQQQALAMAVAAYAEHIDNPSVLAPVLTHIANKHISLGIRPEHYPIVGHHLLASIREVLGAAATDELIAAWAAAYGQLADVLIAEEAQLYAAAAFKQGGWTGWRGFVVAKKEQESSEITSFYLRPADGGSVPDYAPGQYISVRMFVPEWNLMQPRQYSLSDAPGNDYLRISVKREQAGNIIGQVSNLLHNTVNVGDVIDLAPPAGDFVLHQDRTTPVVLISGGVGITPMMAMLKHLVKTGSDRAVHFVHGCRNSEVHAFKNVVNQLATQKSSVEKTVFYGDACPDHSHDHLGYVDLAKIADSVILPDADYYLCGPLAFMQAQIKSLQTMGISAERIHAEAFGTGGVAA","length":399,"molWeight":43244,"crc64":"BAEC4F813E919997","md5":"6C0AE3DEF08B59F5B7950635A73A2E17"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"DOMAIN":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":2,"Binding site":4,"Site":3},"uniParcId":"UPI00361C7D51"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QZB4","uniProtkbId":"A0ABW2QZB4_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421023.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Pyrimidine/purine nucleoside phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"2.4.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Adenosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Cytidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Guanosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Inosine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Thymidine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Uridine phosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Xanthosine phosphorylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"ppnP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421023.1"}],"value":"ACFQNF_14245"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Catalyzes the phosphorolysis of diverse nucleosides, yielding D-ribose 1-phosphate and the respective free bases. Can use uridine, adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as substrates. Also catalyzes the reverse reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a purine D-ribonucleoside + phosphate = a purine nucleobase + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19805"},{"database":"ChEBI","id":"CHEBI:26386"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"},{"database":"ChEBI","id":"CHEBI:142355"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine + phosphate = alpha-D-ribose 1-phosphate + adenine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27642"},{"database":"ChEBI","id":"CHEBI:16335"},{"database":"ChEBI","id":"CHEBI:16708"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine + phosphate = cytosine + alpha-D-ribose 1-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:52540"},{"database":"ChEBI","id":"CHEBI:16040"},{"database":"ChEBI","id":"CHEBI:17562"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13233"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:16750"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"inosine + phosphate = alpha-D-ribose 1-phosphate + hypoxanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27646"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:17596"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"thymidine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + thymine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16037"},{"database":"ChEBI","id":"CHEBI:17748"},{"database":"ChEBI","id":"CHEBI:17821"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57259"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine + phosphate = alpha-D-ribose 1-phosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24388"},{"database":"ChEBI","id":"CHEBI:16704"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"xanthosine + phosphate = alpha-D-ribose 1-phosphate + xanthine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27638"},{"database":"ChEBI","id":"CHEBI:17712"},{"database":"ChEBI","id":"CHEBI:18107"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"value":"Belongs to the nucleoside phosphorylase PpnP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421023.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01537"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"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_01537"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000033","properties":[{"key":"ProteinId","value":"MFC7421023.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380188602.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000033.1"}]},{"database":"Proteomes","id":"UP001596473","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:0004731","properties":[{"key":"GoTerm","value":"F:purine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016154","properties":[{"key":"GoTerm","value":"F:pyrimidine-nucleoside phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd20296","properties":[{"key":"EntryName","value":"cupin_PpnP-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01537","properties":[{"key":"EntryName","value":"Nucleos_phosphorylase_PpnP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009664","properties":[{"key":"EntryName","value":"Ppnp"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"PANTHER","id":"PTHR36540","properties":[{"key":"EntryName","value":"PYRIMIDINE/PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36540:SF1","properties":[{"key":"EntryName","value":"PYRIMIDINE_PURINE NUCLEOSIDE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06865","properties":[{"key":"EntryName","value":"Ppnp"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQFDNVSVLKQGNVYFDGLCVSHTLILASGEKKTVGVILPSALTFNTGAAEIMEIVAGLCHVKLAGESEATPYTAGQSFNVPANSSFSIETLETLHYVCHFA","length":103,"molWeight":10939,"crc64":"9C61E262235F9FBB","md5":"68D0D1888CA991412D2584591DF3F5B4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"SIMILARITY":1,"CAUTION":1},"uniParcId":"UPI00361B8CF8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QZC7","uniProtkbId":"A0ABW2QZC7_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7420943.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"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":"MFC7420943.1"}],"value":"ACFQNF_13840"}]}],"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":"MFC7420943.1"}],"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":204,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":482,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":60,"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":57,"modifier":"EXACT"},"end":{"value":57,"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":115,"modifier":"EXACT"},"end":{"value":115,"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":119,"modifier":"EXACT"},"end":{"value":125,"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":148,"modifier":"EXACT"},"end":{"value":148,"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":151,"modifier":"EXACT"},"end":{"value":151,"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":247,"modifier":"EXACT"},"end":{"value":247,"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":303,"modifier":"EXACT"},"end":{"value":303,"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":356,"modifier":"EXACT"},"end":{"value":356,"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":393,"modifier":"EXACT"},"end":{"value":397,"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":421,"modifier":"EXACT"},"end":{"value":421,"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":422,"modifier":"EXACT"},"end":{"value":422,"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":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000031","properties":[{"key":"ProteinId","value":"MFC7420943.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380188530.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000031.1"}]},{"database":"Proteomes","id":"UP001596473","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":"MINPPLFLSNKLKQIEAAAARAGLPLMQRAGQCSADWIIKHHPEAQTIYVLAGPGNNGGDALVTATLLHLAGKTVLLRLSAPSGPMPAQKALAAWLAHGGQILSSTPNQADLAIDGLYGIGLNRQLGDADQQIIAELQALACPVIALDIPSGLMADSGDATATIHATHTLSFIAHKPGLFTGKGCDLAGEISLHDLQIPGDLFLAPDGHLQTQAPSSIAQLQRKPDSHKGSYGTVGVIGGATGMLGAALLAGRAALHMGTGRVVLGLLDTSLSVDSVQPELMLHSAHEALQHPALTLLAVGPGLGQSTEALELLRQSIASSLPLLLDADALNLLASSAELAAAMRQRTAASILTPHPAEAARLLHTSTQAVQANRIESAQALAQRYEATVLLKGAGSVCANEQSWSINASGNAALASAGQGDVLSGIIAALLAQGLSPLEAVQSGSWLHGRAADDWRKAHPNGIGLTASETISYARAALNQVLGKC","length":486,"molWeight":49853,"crc64":"561ABA59FF156F45","md5":"828123530A86F64B1518290779A5A6D3"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI00361F38F6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2R158","uniProtkbId":"A0ABW2R158_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421510.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421510.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421510.1"}],"value":"ACFQNF_16730"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421510.1"}],"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":97,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000035","properties":[{"key":"ProteinId","value":"MFC7421510.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380189060.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000035.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.530:FF:000003","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000008","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSVNLLDYDAAGLAELMAQYGEKPFRAKQLMKWIHQRGEPDFDAMTDIAKSFRQKLALDAAVTPPALMAEQIAKDGTRKWLLDVGTGNGVEAVFIPEDDRGTLCVSSQVGCALDCGFCSTARQGFNRNLSTAEIIGQLWWANRRMSLDASRLGDAGLVDNRNGDTRIVSNVVMMGMGEPLANYDNVVAAMKLMLDDNAYGLSRRRVTLSTSGIVPAIDRLREDCPVALAVSLHAPNDRIRDDIVPINKKYPLHQLLAACTRYLEKAPRDFITFEYVMLDGINDSVENARELVALVRDVPCKFNLIPFNPFPNSGYKRSQRDAIMRFRDILINAGYIATVRKTRGDDIDAACGQLAGQVLDKTRRVEKRLASDAQAIIFHPQSGDTQ","length":386,"molWeight":42757,"crc64":"39FF206ACC987F98","md5":"DF515D363299DD6BC86A8118AE5A3083"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI003612AFFA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2R1H6","uniProtkbId":"A0ABW2R1H6_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421781.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"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":"MFC7421781.1"}],"value":"ACFQNF_18130"}]}],"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":"MFC7421781.1"}],"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":265,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":534,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":515,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":517,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":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":351,"modifier":"EXACT"},"end":{"value":351,"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":379,"modifier":"EXACT"},"end":{"value":382,"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":402,"modifier":"EXACT"},"end":{"value":402,"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":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000044","properties":[{"key":"ProteinId","value":"MFC7421781.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380189362.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000044.1"}]},{"database":"Proteomes","id":"UP001596473","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":"MTKFIFVTGGVVSSLGKGIAAASLAAILESRGLKVTMMKLDPYINVDPGTMSPFQHGEVFVTEDGAETDLDLGHYERFIRSKMRKSNNFTTGQIYESVITKERRGDYLGGTVQVIPHITDEIKMKVKEGAGDVDVAIVEIGGTVGDIESLPFLEAIRQMRSNLGRKNTLYVHLSYVPYLATAGEIKTKPTQHSVRELRQIGIQPDILLCRMDRELPDEERRKLALFCNVEENAVIACYDAGSIYQVPGMLHAQGIDDIACELLQIDAPKADLSAWDKIVHGLNNPTRTVNIAMVGKYVDLTESYKSLSEALIHAGVHTSSKVQIHYMDSEELEKNGTDSLKNMDAILVPGGFGKRGVEGKILAVKYARENNVPYLGICLGMQIALIEYARDVAGMKGANSTEFDLDTEFPVVALINEWVNHDGKIETRDANSNLGGTMRLGAQECRLGEDSLAARVYGASTITERHRHRYEVNNYYLPRLEAAGLTISGKSTGAEQLVETVELSGHRWFFACQFHPEFTSTPRDGHPLFTSYVEAALSYAKEQGREGLSC","length":550,"molWeight":60661,"crc64":"E18672F261BE78C4","md5":"CB5DA778F8F0F49B05531E403C48A31D"},"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":"UPI00361087E8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2R3J5","uniProtkbId":"A0ABW2R3J5_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421899.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Siroheme synthase"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Uroporphyrinogen-III C-methyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Urogen III methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"2.1.1.107"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"SUMT"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Uroporphyrinogen III methylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"UROM"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Precorrin-2 dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"1.3.1.76"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Sirohydrochlorin ferrochelatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"4.99.1.4"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421899.1"}],"value":"cysG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421899.1"}],"value":"ACFQNF_18725"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Multifunctional enzyme that catalyzes the SAM-dependent methylations of uroporphyrinogen III at position C-2 and C-7 to form precorrin-2 via precorrin-1. Then it catalyzes the NAD-dependent ring dehydrogenation of precorrin-2 to yield sirohydrochlorin. Finally, it catalyzes the ferrochelation of sirohydrochlorin to yield siroheme"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"precorrin-2 + NAD(+) = sirohydrochlorin + NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15613"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58351"},{"database":"ChEBI","id":"CHEBI:58827"}],"ecNumber":"1.3.1.76","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047561"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"siroheme + 2 H(+) = sirohydrochlorin + Fe(2+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24360"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:58351"},{"database":"ChEBI","id":"CHEBI:60052"}],"ecNumber":"4.99.1.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uroporphyrinogen III + 2 S-adenosyl-L-methionine = precorrin-2 + 2 S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32459"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57308"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:58827"},{"database":"ChEBI","id":"CHEBI:59789"}],"ecNumber":"2.1.1.107","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060548"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Cofactor biosynthesis; adenosylcobalamin biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Cofactor biosynthesis; adenosylcobalamin biosynthesis; sirohydrochlorin from precorrin-2: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025705"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; siroheme from sirohydrochlorin: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005010"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Porphyrin-containing compound metabolism; siroheme biosynthesis; sirohydrochlorin from precorrin-2: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005879"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003960"}],"value":"Belongs to the precorrin methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"In the C-terminal section; belongs to the precorrin methyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"In the N-terminal section; belongs to the precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421899.1"}],"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":150,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Sirohaem synthase dimerisation","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10414"}]},{"type":"Domain","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Tetrapyrrole methylase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00590"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"Precorrin-2 dehydrogenase / sirohydrochlorin ferrochelatase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]},{"type":"Region","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Uroporphyrinogen-III C-methyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}]},{"type":"Active site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR036426-1"}]},{"type":"Active site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR036426-1"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022573"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0169","category":"Biological process","name":"Cobalamin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"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_01646"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01646"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000044","properties":[{"key":"ProteinId","value":"MFC7421899.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380189568.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000044.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043115","properties":[{"key":"GoTerm","value":"F:precorrin-2 dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004325","properties":[{"key":"GoTerm","value":"F:protoporphyrin ferrochelatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051266","properties":[{"key":"GoTerm","value":"F:sirohydrochlorin ferrochelatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004851","properties":[{"key":"GoTerm","value":"F:uroporphyrin-III C-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009236","properties":[{"key":"GoTerm","value":"P:cobalamin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019354","properties":[{"key":"GoTerm","value":"P:siroheme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd11642","properties":[{"key":"EntryName","value":"SUMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.950.10:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1010.10:FF:000001","properties":[{"key":"EntryName","value":"Siroheme synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1010.10","properties":[{"key":"EntryName","value":"Cobalt-precorrin-4 Transmethylase, Domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.950.10","properties":[{"key":"EntryName","value":"Methyltransferase, Cobalt-precorrin-4 Transmethylase, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.210","properties":[{"key":"EntryName","value":"Sirohaem synthase, dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.160.110","properties":[{"key":"EntryName","value":"Siroheme synthase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01646","properties":[{"key":"EntryName","value":"Siroheme_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000878","properties":[{"key":"EntryName","value":"4pyrrol_Mease"}]},{"database":"InterPro","id":"IPR035996","properties":[{"key":"EntryName","value":"4pyrrol_Methylase_sf"}]},{"database":"InterPro","id":"IPR014777","properties":[{"key":"EntryName","value":"4pyrrole_Mease_sub1"}]},{"database":"InterPro","id":"IPR014776","properties":[{"key":"EntryName","value":"4pyrrole_Mease_sub2"}]},{"database":"InterPro","id":"IPR006366","properties":[{"key":"EntryName","value":"CobA/CysG_C"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR050161","properties":[{"key":"EntryName","value":"Siro_Cobalamin_biosynth"}]},{"database":"InterPro","id":"IPR037115","properties":[{"key":"EntryName","value":"Sirohaem_synt_dimer_dom_sf"}]},{"database":"InterPro","id":"IPR012409","properties":[{"key":"EntryName","value":"Sirohaem_synth"}]},{"database":"InterPro","id":"IPR019478","properties":[{"key":"EntryName","value":"Sirohaem_synthase_dimer_dom"}]},{"database":"InterPro","id":"IPR006367","properties":[{"key":"EntryName","value":"Sirohaem_synthase_N"}]},{"database":"InterPro","id":"IPR003043","properties":[{"key":"EntryName","value":"Uropor_MeTrfase_CS"}]},{"database":"NCBIfam","id":"TIGR01469","properties":[{"key":"EntryName","value":"cobA_cysG_Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF007922","properties":[{"key":"EntryName","value":"cysG"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01470","properties":[{"key":"EntryName","value":"cysG_Nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004790","properties":[{"key":"EntryName","value":"PRK06136.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45790:SF1","properties":[{"key":"EntryName","value":"SIROHEME SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45790","properties":[{"key":"EntryName","value":"SIROHEME SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10414","properties":[{"key":"EntryName","value":"CysG_dimeriser"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13241","properties":[{"key":"EntryName","value":"NAD_binding_7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00590","properties":[{"key":"EntryName","value":"TP_methylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF036426","properties":[{"key":"EntryName","value":"Sirohaem_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75615","properties":[{"key":"EntryName","value":"Siroheme synthase middle domains-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53790","properties":[{"key":"EntryName","value":"Tetrapyrrole methylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00840","properties":[{"key":"EntryName","value":"SUMT_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNYFPLFLNLRDQHCLVIGGGDVAARKIRLLTAAGGRITVVAPALCEELAQAVAAGALIYLAASFNELQLQNMRLVIAATDSEEINRQVFEACEARGILVNAVDDPASCRFITPAIVDRSPLMIAISTSGGVPVLARQLRSQLEALIPHGYGDLAQMASDFREEVKQTLTSVDARKQFWEKTLAGPIPDMVFAGQHDAARRALSAAIKADADAPLQGAVYLVGCGPGNPDLLTFRALRLMQQADVVLYDNLVSAPILDMVRRDAERVYVGKKSNNHAVPQEEINQLLVRYARQGKKVLRLKGGDPFIFGRGGEEIEELADAGIAFEVVPGITSAAGASCYAGIPLTHRDYAQSVTFVTGHRRDGEVELDWPRLVSPTETVVVYMGVAQVDKICVQLIKHGRNPATPAAMVEKATLSKQRVVVGTLSDLAQKVADLGIKPPALIIIGEVVSLHDKLKWLAD","length":460,"molWeight":49654,"crc64":"816EF1F4C6806621","md5":"3AA334EDD78D586B6369925B8FC865F9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"PATHWAY":5,"SIMILARITY":3,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":2,"Binding site":7},"uniParcId":"UPI0036234D56"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2R3S5","uniProtkbId":"A0ABW2R3S5_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421974.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421974.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7421974.1"}],"value":"ACFQNF_19105"}]}],"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":"MFC7421974.1"}],"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":1073,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5049655961"},{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":673,"modifier":"EXACT"},"end":{"value":868,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":935,"modifier":"EXACT"},"end":{"value":1073,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":935,"modifier":"EXACT"},"end":{"value":1073,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":709,"modifier":"EXACT"},"end":{"value":709,"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":748,"modifier":"EXACT"},"end":{"value":748,"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":750,"modifier":"EXACT"},"end":{"value":750,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":755,"modifier":"EXACT"},"end":{"value":755,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":780,"modifier":"EXACT"},"end":{"value":780,"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":781,"modifier":"EXACT"},"end":{"value":781,"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":782,"modifier":"EXACT"},"end":{"value":782,"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":783,"modifier":"EXACT"},"end":{"value":783,"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":823,"modifier":"EXACT"},"end":{"value":823,"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":823,"modifier":"EXACT"},"end":{"value":823,"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":823,"modifier":"EXACT"},"end":{"value":823,"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":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":839,"modifier":"EXACT"},"end":{"value":839,"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":839,"modifier":"EXACT"},"end":{"value":839,"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":839,"modifier":"EXACT"},"end":{"value":839,"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":839,"modifier":"EXACT"},"end":{"value":839,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":"UP001596473"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000044","properties":[{"key":"ProteinId","value":"MFC7421974.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380189695.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000044.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"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":"MPKRTDLKSILIIGAGPIVIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPNMADVTYIEPITWQMVEKIIEKERPCALLPTMGGQTALNCALDLWRHGVLEKYNVEMIGAKPDAIDKAEDRGKFKDAMTKIGLSTPKSGIAHNMEQALAVQATVGYPTLIRPSFTMGGSGGGIAYNREEFVEICDRGFEASPTNELLIEQSVLGWKEYEMEVVRDRADNCIIICSIENFDPMGVHTGDSITVAPAQTLTDKEYQIMRNASLAVLREIGVDTGGSNVQFATNPENGEMIVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGFTLDELQNEITGGKTPASFEPSIDYVVTKIPRFAFEKFPQANNKLTTQMKSVGEVMAIGRTVQESMQKALRGLETGMSGFDEMTTDRSLIEAEIANPGPERIWYVADAFRVGMSMDEVFNLTKIDPWFLRQIEDLVIEENAIRGTAVESIDYATMRRLKRKGFSDRRLASLLDTDQAAVRKARHALKIRPVYKRVDTCAAEFSTDTAYMYSTYEEECEAQPTNNRKIMILGGGPNRIGQGIEFDYCCVHAALALREDGFETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVNIEKPEGVIVQYGGQTPLKLARALEANGVPIIGTTPDMIDAAEDRERFQKLLHELGLRQPPNRTARNERDALILAAEIGYPLVVRPSYVLGGRAMEIVHQQSDLERYMREAVKVSNDSPVLLDRFLNDAIEVDVDAICDGTDVLIGGIMEHIEQAGVHSGDSACSLPPFSLSKEIQDELRRQTVLMAKGLNVVGLMNVQFAIQGKGSDAVVFVLEVNPRASRTVPYVSKATSLPIAKIAARCMAGQSLVSQGMTKEVIPPFFSVKEAVFPFIKFPGVDSILGPEMKSTGEVMGVGDTFAEAFVKSQLAAGVALPTQGNVFISVRDGDKTGAVECAKVLTGLGFKVFATKGTAAEISGAGVVVQSVNKVTEGRPHIVDMIKNGEIGMIVNTVDERRQAIQDSYSIRHEAMKARLPVFTTIAGAKAACIGMRDLGEMRVYDLQGLHRTIKH","length":1073,"molWeight":117415,"crc64":"A2C7465F5D3583A3","md5":"773BEBFFF0DD5DDCDD3825CA3525711F"},"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":"UPI00362030D8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRB3","uniProtkbId":"A0ABW2QRB3_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418291.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"Glutamine-dependent NAD(+) synthetase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"6.3.5.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"NAD(+) synthase [glutamine-hydrolyzing]"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"value":"nadE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418291.1"}],"value":"ACFQNF_00145"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"value":"Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"deamido-NAD(+) + L-glutamine + ATP + H2O = L-glutamate + AMP + diphosphate + NAD(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24384"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:58437"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005188"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003811"}],"value":"Belongs to the NAD synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"In the C-terminal section; belongs to the NAD synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418291.1"}],"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":251,"modifier":"EXACT"}},"description":"CN hydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50263"}]},{"type":"Active site","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Proton acceptor; for glutaminase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}]},{"type":"Active site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"For glutaminase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}]},{"type":"Active site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"Nucleophile; for glutaminase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}]},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":514,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418291.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185192.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003952","properties":[{"key":"GoTerm","value":"F:NAD+ synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008795","properties":[{"key":"GoTerm","value":"F:NAD+ synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009435","properties":[{"key":"GoTerm","value":"P:NAD+ biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07570","properties":[{"key":"EntryName","value":"GAT_Gln-NAD-synth"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00553","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000106","properties":[{"key":"EntryName","value":"Glutamine-dependent NAD(+) synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.110.10","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02090","properties":[{"key":"EntryName","value":"NadE_glutamine_dep"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003010","properties":[{"key":"EntryName","value":"C-N_Hydrolase"}]},{"database":"InterPro","id":"IPR036526","properties":[{"key":"EntryName","value":"C-N_Hydrolase_sf"}]},{"database":"InterPro","id":"IPR014445","properties":[{"key":"EntryName","value":"Gln-dep_NAD_synthase"}]},{"database":"InterPro","id":"IPR022310","properties":[{"key":"EntryName","value":"NAD/GMP_synthase"}]},{"database":"InterPro","id":"IPR003694","properties":[{"key":"EntryName","value":"NAD_synthase"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR00552","properties":[{"key":"EntryName","value":"nadE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010588","properties":[{"key":"EntryName","value":"PRK13981.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23090:SF9","properties":[{"key":"EntryName","value":"GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23090","properties":[{"key":"EntryName","value":"NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00795","properties":[{"key":"EntryName","value":"CN_hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02540","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006630","properties":[{"key":"EntryName","value":"NADS_GAT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"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":"MAFLLLAETNPMKIAIAQLNSLVGDLAGNTDKIFAAALQAKADGADILLTPELALSGYPPEDLLLRPAFLAECAQCVGRFIDELDGITLVLGYPRASSDERFNSAIVIRDGNVLGRYDKLLLPNDQVFDEVRYFSPGYSPFVFEQDGVQIGLAICEDIWDIEPASAADDEGAELLLILNASPYNQAKQSTRREVVGQRVEETGMAMVYCNMIGGQDELIFDGQSFALNKSGELVAQLPAFSEQVAIVEYQKGDLQAATITPDLSDEASAYQALVLGVQDYIGKNRFSGVLLGLSGGIDSALTLAIAVDALGADKVHAVMMPSRYTADISVDDSREMIKILGCKYSEIEIWPIYEAFMNGLAGEFEGTAADTTEENLQARARGTLLMALSNKSGKLVLTTGNKSEMTTGYATLYGDMAGGFAVLKDVAKTLVYRLSSWRNTQGVVIPERIITRPPSAELRPDQTDQDSLPAYEILDVILQAYVEENLSRAEIIAKGFAKADVDRVVHLLTINEYKRRQAPVGPRITPRAFGKDWRMPITNRFSM","length":543,"molWeight":59198,"crc64":"4CEAE0ECFDA72A89","md5":"0DECB494FE1E3ACC1C5FE25663682497"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":6,"Binding site":7},"uniParcId":"UPI00361D5DF8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRC4","uniProtkbId":"A0ABW2QRC4_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418322.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"Beta-ketoacyl-[acyl-carrier-protein] synthase III"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"Beta-ketoacyl-ACP synthase III"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"KAS III"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"2.3.1.180"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"3-oxoacyl-[acyl-carrier-protein] synthase 3"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"3-oxoacyl-[acyl-carrier-protein] synthase III"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"fabH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418322.1"}],"value":"ACFQNF_00315"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"Catalyzes the condensation reaction of fatty acid synthesis by the addition to an acyl acceptor of two carbons from malonyl-ACP. Catalyzes the first condensation reaction which initiates fatty acid synthesis and may therefore play a role in governing the total rate of fatty acid production. Possesses both acetoacetyl-ACP synthase and acetyl transacylase activities. Its substrate specificity determines the biosynthesis of branched-chain and/or straight-chain of fatty acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"malonyl-[ACP] + acetyl-CoA + H(+) = 3-oxobutanoyl-[ACP] + CO2 + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12080"},{"database":"Rhea","id":"RHEA-COMP:9623"},{"database":"Rhea","id":"RHEA-COMP:9625"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:78449"},{"database":"ChEBI","id":"CHEBI:78450"}],"ecNumber":"2.3.1.180","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"Lipid metabolism; fatty acid biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"The last Arg residue of the ACP-binding site is essential for the weak association between ACP/AcpP and FabH"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008642"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"value":"Belongs to the thiolase-like superfamily. FabH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418322.1"}],"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":106,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Beta-ketoacyl-[acyl-carrier-protein] synthase III N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08545"}]},{"type":"Domain","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Beta-ketoacyl-[acyl-carrier-protein] synthase III C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08541"}]},{"type":"Region","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"ACP-binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}]},{"type":"Active site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}]},{"type":"Active site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}]},{"type":"Active site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01815"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"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_01815"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418322.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185236.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","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:0004315","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033818","properties":[{"key":"GoTerm","value":"F:beta-ketoacyl-acyl-carrier-protein synthase III activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044550","properties":[{"key":"GoTerm","value":"P:secondary metabolite biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00830","properties":[{"key":"EntryName","value":"KAS_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.47.10:FF:000004","properties":[{"key":"EntryName","value":"3-oxoacyl-[acyl-carrier-protein] synthase 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.47.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01815","properties":[{"key":"EntryName","value":"FabH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013747","properties":[{"key":"EntryName","value":"ACP_syn_III_C"}]},{"database":"InterPro","id":"IPR013751","properties":[{"key":"EntryName","value":"ACP_syn_III_N"}]},{"database":"InterPro","id":"IPR004655","properties":[{"key":"EntryName","value":"FabH"}]},{"database":"InterPro","id":"IPR016039","properties":[{"key":"EntryName","value":"Thiolase-like"}]},{"database":"NCBIfam","id":"TIGR00747","properties":[{"key":"EntryName","value":"fabH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006829","properties":[{"key":"EntryName","value":"PRK09352.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34069","properties":[{"key":"EntryName","value":"3-OXOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR34069:SF2","properties":[{"key":"EntryName","value":"BETA-KETOACYL-[ACYL-CARRIER-PROTEIN] SYNTHASE III"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08545","properties":[{"key":"EntryName","value":"ACP_syn_III"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08541","properties":[{"key":"EntryName","value":"ACP_syn_III_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53901","properties":[{"key":"EntryName","value":"Thiolase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYARIVGTGSYLPSRVVSNQEIAERVETSDEWIFSRTGIRERHIAAEGEMTSDMALKAIEAAIAAAGVSKEEIDLLIVATTTGDQIFPSTACILQDKLGVHGFPAFDVQAVCAGFIYALSTAEKFVKTGAAQCAVVVGAETLSHIVNWDDRGTCILFGDGAGAVVLKPSTETGILATHLRADGRYRHILKADAKVKYGALTGSPWLYMEGNAVFKFAVRALADIAVETLEAAGIEQAEIDWLVPHQANIRIIESTAKHLGLSMDKVVVTVAEHGNTSAASIPLALDTAVRDGRIKAGHKVLMEGIGGGFAWGSVLVQF","length":318,"molWeight":33795,"crc64":"23FBCD8BB1D25D61","md5":"6B4AB9EEBCC74C15E95F7E405FF8BD7B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":3},"uniParcId":"UPI00361C673E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRD8","uniProtkbId":"A0ABW2QRD8_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418331.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"Glutamate--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"6.1.1.17"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"Glutamyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"GluRS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418331.1"}],"value":"gltX"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418331.1"}],"value":"ACFQNF_00365"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Glu) + L-glutamate + ATP = L-glutamyl-tRNA(Glu) + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23540"},{"database":"Rhea","id":"RHEA-COMP:9663"},{"database":"Rhea","id":"RHEA-COMP:9680"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78520"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007894"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"Belongs to the class-I aminoacyl-tRNA synthetase family. Glutamate--tRNA ligase type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418331.1"}],"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":309,"modifier":"EXACT"}},"description":"Glutamyl/glutaminyl-tRNA synthetase class Ib catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00749"}]},{"type":"Domain","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"Aminoacyl-tRNA synthetase class I anticodon-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF19269"}]},{"type":"Motif","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"'HIGH' region","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}]},{"type":"Motif","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"'KMSKS' region","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}]},{"type":"Binding site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00022"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418331.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185252.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004818","properties":[{"key":"GoTerm","value":"F:glutamate-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA 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:0006424","properties":[{"key":"GoTerm","value":"P:glutamyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00808","properties":[{"key":"EntryName","value":"GluRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000007","properties":[{"key":"EntryName","value":"Glutamate--tRNA ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.350","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00022","properties":[{"key":"EntryName","value":"Glu_tRNA_synth_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045462","properties":[{"key":"EntryName","value":"aa-tRNA-synth_I_cd-bd"}]},{"database":"InterPro","id":"IPR020751","properties":[{"key":"EntryName","value":"aa-tRNA-synth_I_codon-bd_sub2"}]},{"database":"InterPro","id":"IPR001412","properties":[{"key":"EntryName","value":"aa-tRNA-synth_I_CS"}]},{"database":"InterPro","id":"IPR008925","properties":[{"key":"EntryName","value":"aa_tRNA-synth_I_cd-bd_sf"}]},{"database":"InterPro","id":"IPR004527","properties":[{"key":"EntryName","value":"Glu-tRNA-ligase_bac/mito"}]},{"database":"InterPro","id":"IPR000924","properties":[{"key":"EntryName","value":"Glu/Gln-tRNA-synth"}]},{"database":"InterPro","id":"IPR020058","properties":[{"key":"EntryName","value":"Glu/Gln-tRNA-synth_Ib_cat-dom"}]},{"database":"InterPro","id":"IPR049940","properties":[{"key":"EntryName","value":"GluQ/Sye"}]},{"database":"InterPro","id":"IPR033910","properties":[{"key":"EntryName","value":"GluRS_core"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR00464","properties":[{"key":"EntryName","value":"gltX_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43311","properties":[{"key":"EntryName","value":"GLUTAMATE--TRNA LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43311:SF2","properties":[{"key":"EntryName","value":"GLUTAMATE--TRNA LIGASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF19269","properties":[{"key":"EntryName","value":"Anticodon_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00749","properties":[{"key":"EntryName","value":"tRNA-synt_1c"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00987","properties":[{"key":"EntryName","value":"TRNASYNTHGLU"}]},{"database":"SUPFAM","id":"SSF48163","properties":[{"key":"EntryName","value":"An anticodon-binding domain of class I aminoacyl-tRNA synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00178","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_I"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVRTRFAPSPTGLLHIGGVRTALFSWAHARKNGGAFVLRIEDTDLERSTPESVKAIMDGMHWVGIDYDEGPFYQMQRMDRYREVVKQLLASGHAYPCYMSKEELDVMRATQEALGLKAKYDRRWRPEEGKVLPEPPLGVQPVLRFRTPLDGVVAWDDLVKGRIEIGNVELDDLIIARPDGTPTYNFCVVVDDWDMGITQVIRGDDHVNNTPRQIHIFNALGAAVPQFAHLPMIHNDQGQKLSKRRDAVSVVDYDSAGYLPEALLNYLARLGWGHGDDECFSMAQFVEWFDLKDVSASPSRFDKEKLLWLNAQHIKTADAARLADLAKRFLDEKGVDLSQGPALVDVVTLLKDRVQTIVELATEATYFYQPLTPSDEVVAKHLTSDDLARLTVFASEAAALEVWDTTSIAAFIKEFCKSQGVKMGQVGMPLRAKVCGTTHTPSVDAVLALLGKAEVLKRLA","length":461,"molWeight":51406,"crc64":"31C05A32B1B9F90A","md5":"36F4A4F697B62C3943674ECCCF327E8A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Motif":2,"Binding site":1},"uniParcId":"UPI0036245697"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRE1","uniProtkbId":"A0ABW2QRE1_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418321.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Phosphate acyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"2.3.1.274"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Acyl-ACP phosphotransacylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Acyl-[acyl-carrier-protein]--phosphate acyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Phosphate-acyl-ACP acyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418321.1"}],"value":"plsX"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418321.1"}],"value":"ACFQNF_00310"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Catalyzes the reversible formation of acyl-phosphate (acyl-PO(4)) from acyl-[acyl-carrier-protein] (acyl-ACP). This enzyme utilizes acyl-ACP as fatty acyl donor, but not acyl-CoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a fatty acyl-[ACP] + phosphate = an acyl phosphate + holo-[ACP]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42292"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:14125"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:59918"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:138651"}],"ecNumber":"2.3.1.274","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Lipid metabolism; phospholipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Homodimer. Probably interacts with PlsY"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Associated with the membrane possibly through PlsY"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"value":"Belongs to the PlsX family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418321.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418321.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00019"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418321.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418321.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185234.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","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:0043811","properties":[{"key":"GoTerm","value":"F:phosphate:acyl-[acyl carrier protein] acyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006644","properties":[{"key":"GoTerm","value":"P:phospholipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.718.10","properties":[{"key":"EntryName","value":"Isopropylmalate Dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00019","properties":[{"key":"EntryName","value":"PlsX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003664","properties":[{"key":"EntryName","value":"FA_synthesis"}]},{"database":"InterPro","id":"IPR012281","properties":[{"key":"EntryName","value":"Phospholipid_synth_PlsX-like"}]},{"database":"NCBIfam","id":"TIGR00182","properties":[{"key":"EntryName","value":"plsX"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30100","properties":[{"key":"EntryName","value":"FATTY ACID/PHOSPHOLIPID SYNTHESIS PROTEIN PLSX"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30100:SF1","properties":[{"key":"EntryName","value":"PHOSPHATE ACYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02504","properties":[{"key":"EntryName","value":"FA_synthesis"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002465","properties":[{"key":"EntryName","value":"Phsphlp_syn_PlsX"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53659","properties":[{"key":"EntryName","value":"Isocitrate/Isopropylmalate dehydrogenase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDITVAVDAMGGDHGTHVTVPAVLRFLKEFPNVNVVLVGLPDVLEVELKACHATVGPRLRVHAASEVVTMDESPQSAMKNKKDSSMRVAINLVKSGEANACVSAGNTGALMATARFVLKTIPGIDRPAIAKMMPSSRNETCVLDLGANAVCTPHNLLQFAIMGSSLVAATRHIENPTVGLLNIGSEDQKGNEVVKEASELLKASRLNFYGNVEGNDIYRGSVDVVTCDGFTGNVALKASEGLAKMLAEFLKQEFTRSWWTRIIALLAWPVLARFKARVDPRRYNGASLLGLKGIVVKSHGGADKVAFYWALRQAMDEARSGVIQRITEQVQDQLAELAAQEE","length":342,"molWeight":36864,"crc64":"232D415F0C414E93","md5":"E16F970572F56B3C6D186A101DBAA892"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"uniParcId":"UPI003612F1E9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRF4","uniProtkbId":"A0ABW2QRF4_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418352.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"Thiol:disulfide interchange protein DsbD"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"1.8.1.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"Protein-disulfide reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"Disulfide reductase"}]}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418352.1"}],"value":"dsbD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418352.1"}],"value":"ACFQNF_00470"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"Required to facilitate the formation of correct disulfide bonds in some periplasmic proteins and for the assembly of the periplasmic c-type cytochromes. Acts by transferring electrons from cytoplasmic thioredoxin to the periplasm. This transfer involves a cascade of disulfide bond formation and reduction steps"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[protein]-dithiol + NAD(+) = [protein]-disulfide + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18749"},{"database":"Rhea","id":"RHEA-COMP:10593"},{"database":"Rhea","id":"RHEA-COMP:10594"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.8.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047388"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[protein]-dithiol + NADP(+) = [protein]-disulfide + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18753"},{"database":"Rhea","id":"RHEA-COMP:10593"},{"database":"Rhea","id":"RHEA-COMP:10594"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.8.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047804"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004429"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004429"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007241"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"value":"Belongs to the thioredoxin family. DsbD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418352.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Chain","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":653,"modifier":"EXACT"}},"description":"Thiol:disulfide interchange protein DsbD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"featureId":"PRO_5051567285"},{"type":"Transmembrane","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Transmembrane","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Transmembrane","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Transmembrane","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Transmembrane","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Transmembrane","location":{"start":{"value":441,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Transmembrane","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":482,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Transmembrane","location":{"start":{"value":494,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Domain","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":653,"modifier":"EXACT"}},"description":"Thioredoxin","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51352"}]},{"type":"Disulfide bond","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Disulfide bond","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}]},{"type":"Disulfide bond","location":{"start":{"value":570,"modifier":"EXACT"},"end":{"value":573,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00691"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022519"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022748"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0201","category":"Biological process","name":"Cytochrome c-type biogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0676","category":"Domain","name":"Redox-active center"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00399"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418352.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185292.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","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:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0047134","properties":[{"key":"GoTerm","value":"F:protein-disulfide reductase [NAD(P)H] activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0045454","properties":[{"key":"GoTerm","value":"P:cell redox homeostasis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0017004","properties":[{"key":"GoTerm","value":"P:cytochrome complex assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02953","properties":[{"key":"EntryName","value":"DsbDgamma"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.30.10","properties":[{"key":"EntryName","value":"Glutaredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1250","properties":[{"key":"EntryName","value":"Thiol:disulfide interchange protein DsbD, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00399","properties":[{"key":"EntryName","value":"DbsD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003834","properties":[{"key":"EntryName","value":"Cyt_c_assmbl_TM_dom"}]},{"database":"InterPro","id":"IPR035671","properties":[{"key":"EntryName","value":"DsbD_gamma"}]},{"database":"InterPro","id":"IPR028250","properties":[{"key":"EntryName","value":"DsbDN"}]},{"database":"InterPro","id":"IPR036929","properties":[{"key":"EntryName","value":"DsbDN_sf"}]},{"database":"InterPro","id":"IPR022910","properties":[{"key":"EntryName","value":"Thiol_diS_interchange_DbsD"}]},{"database":"InterPro","id":"IPR012336","properties":[{"key":"EntryName","value":"Thioredoxin-like_fold"}]},{"database":"InterPro","id":"IPR036249","properties":[{"key":"EntryName","value":"Thioredoxin-like_sf"}]},{"database":"InterPro","id":"IPR017937","properties":[{"key":"EntryName","value":"Thioredoxin_CS"}]},{"database":"InterPro","id":"IPR013766","properties":[{"key":"EntryName","value":"Thioredoxin_domain"}]},{"database":"NCBIfam","id":"NF001419","properties":[{"key":"EntryName","value":"dsbD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32234","properties":[{"key":"EntryName","value":"THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32234:SF0","properties":[{"key":"EntryName","value":"THIOL:DISULFIDE INTERCHANGE PROTEIN DSBD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11412","properties":[{"key":"EntryName","value":"DsbD_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02683","properties":[{"key":"EntryName","value":"DsbD_TM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13098","properties":[{"key":"EntryName","value":"Thioredoxin_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF74863","properties":[{"key":"EntryName","value":"Thiol:disulfide interchange protein DsbD, N-terminal domain (DsbD-alpha)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52833","properties":[{"key":"EntryName","value":"Thioredoxin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00194","properties":[{"key":"EntryName","value":"THIOREDOXIN_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51352","properties":[{"key":"EntryName","value":"THIOREDOXIN_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKTYLDLIRVAACPHPTRFTREIMFKTIKNTLCAALLALSFSQGWAEDPVFLEPEQALKMSAKAKDHQTVEVRFAIAEGYYLYKNKLKFSADSGVELAAPKFPPSLSHDDPNFGKVETYRQQVLLPIQVKNAAATSFKLTVISQGCADAGLCYPPITQVADIKLPAATTKLVTEIKLPAAPAQLVEATPAPVHAITPDTVAVAETNIQAPLVQAAATTAPLEEAPQGDTGSVTSLLGSGNLPLILLSFFGFGLLLALTPCVFPMMPILSGIIVGSGNNISKKRALVLSLAYVLGMAISYALAGVAAGLSGSLLSAALQNVWVLGSFAMVFVLLSLSMFGFYELQLPASLQSKLSNSANQQKGGSLLGVLIMGALSALIVGPCVAAPLAGALLYIAQTHNALLGGVALFVMALGMGVPLIIVGCAASALPRAGGWMENIKKVFGVLLLGVAIWLVSPVLPALFSMLAWGTLLIISAVFLHALDPLPPQTAGCPRFCKGLGVIALLAGSAMLIGALSGNRDPLQPLQGFQGMAAQTAAPHSQFERVTSVADLESKLANSKQPVMLDFYADWCVSCKEMEKFTFSDPEVAARMGQMRLLQADVTANTDADKALLKRFKLFGPPGIIFFDPQGKEQFSTVGFQDAVAFKATLDKALK","length":653,"molWeight":68905,"crc64":"6EB9E3F1C22FFFFF","md5":"E7CE95D27EBC2128EE5944CC1DF29D2C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":8,"Domain":1,"Disulfide bond":3},"uniParcId":"UPI0036164B17"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRK1","uniProtkbId":"A0ABW2QRK1_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418391.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"GTPase Obg"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"3.6.5.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"GTP-binding protein Obg"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418391.1"}],"value":"obgE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"obg"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418391.1"}],"value":"ACFQNF_00670"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"An essential GTPase which binds GTP, GDP and possibly (p)ppGpp with moderate affinity, with high nucleotide exchange rates and a fairly low GTP hydrolysis rate. Plays a role in control of the cell cycle, stress response, ribosome biogenesis and in those bacteria that undergo differentiation, in morphogenesis control"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007699"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"value":"Belongs to the TRAFAC class OBG-HflX-like GTPase superfamily. OBG GTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418391.1"}],"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":1,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Obg","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51883"}]},{"type":"Domain","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"OBG-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51710"}]},{"type":"Region","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01047"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01454"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418391.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185350.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","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:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase 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:0043022","properties":[{"key":"GoTerm","value":"F:ribosome binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0042254","properties":[{"key":"GoTerm","value":"P:ribosome biogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01898","properties":[{"key":"EntryName","value":"Obg"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.70.210.12:FF:000001","properties":[{"key":"EntryName","value":"GTPase Obg"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.70.210.12","properties":[{"key":"EntryName","value":"GTP1/OBG domain"},{"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_01454","properties":[{"key":"EntryName","value":"GTPase_Obg"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR031167","properties":[{"key":"EntryName","value":"G_OBG"}]},{"database":"InterPro","id":"IPR006073","properties":[{"key":"EntryName","value":"GTP-bd"}]},{"database":"InterPro","id":"IPR014100","properties":[{"key":"EntryName","value":"GTP-bd_Obg/CgtA"}]},{"database":"InterPro","id":"IPR006074","properties":[{"key":"EntryName","value":"GTP1-OBG_CS"}]},{"database":"InterPro","id":"IPR006169","properties":[{"key":"EntryName","value":"GTP1_OBG_dom"}]},{"database":"InterPro","id":"IPR036726","properties":[{"key":"EntryName","value":"GTP1_OBG_dom_sf"}]},{"database":"InterPro","id":"IPR045086","properties":[{"key":"EntryName","value":"OBG_GTPase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR02729","properties":[{"key":"EntryName","value":"Obg_CgtA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008955","properties":[{"key":"EntryName","value":"obgE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008956","properties":[{"key":"EntryName","value":"obgE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11702","properties":[{"key":"EntryName","value":"DEVELOPMENTALLY REGULATED GTP-BINDING PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11702:SF31","properties":[{"key":"EntryName","value":"MITOCHONDRIAL RIBOSOME-ASSOCIATED GTPASE 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01018","properties":[{"key":"EntryName","value":"GTP1_OBG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01926","properties":[{"key":"EntryName","value":"MMR_HSR1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00326","properties":[{"key":"EntryName","value":"GTP1OBG"}]},{"database":"SUPFAM","id":"SSF82051","properties":[{"key":"EntryName","value":"Obg GTP-binding protein N-terminal domain"},{"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":"PS51710","properties":[{"key":"EntryName","value":"G_OBG"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00905","properties":[{"key":"EntryName","value":"GTP1_OBG"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51883","properties":[{"key":"EntryName","value":"OBG"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKFIDEAKIEAIAGKGGSGSASMRREKFIPRGGPDGGDGGRGGSVWAVADEDINTLVDYRFVKKYKARDGENGRGADCYGKGGDDVELRMPVGTSIVDAESGELIADLTESGQRVVIAKGGKGGLGNLHFKSSVNRAPRQTAPSEEGERRELRLELKVLADIGLLGMPNAGKSTFIRAVSAAKPKVADYPFTTLFPNLGVVRIDDNRSFVVADIPGLIEGAAEGAGLGHRFLKHLQRTGILLHIVDLAPFDESTDPVAEACAIVEELRKYDEELHKKPRWLVLNKLDMIPEEERSERVANFLKAYGWEAGSHDAYEAFDPMQPRLFTISGLTGEGCRDLTYAIMDYLEAARIYTRNQDKIRAEQLEIAREAAAVAKAAADAVKEAAKEAAKVAATQEDLLASDDSASA","length":408,"molWeight":44049,"crc64":"210DBC8A430C76DF","md5":"F5B1566964FD1B1C6716F2A1846C30C7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Binding site":7},"uniParcId":"UPI003618031D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRQ7","uniProtkbId":"A0ABW2QRQ7_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418426.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00070675"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"value":"Chaperone protein HtpG"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"value":"Heat shock protein HtpG"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"value":"High temperature protein G"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418426.1"}],"value":"htpG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418426.1"}],"value":"ACFQNF_00850"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058590"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"value":"Molecular chaperone. Has ATPase activity"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"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_00505"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"value":"Belongs to the heat shock protein 90 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418426.1"}],"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":181,"modifier":"EXACT"}},"description":"Histidine kinase/HSP90-like ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00387"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"A; substrate-binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}]},{"type":"Region","location":{"start":{"value":559,"modifier":"EXACT"},"end":{"value":633,"modifier":"EXACT"}},"description":"C","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}]},{"type":"Coiled coil","location":{"start":{"value":495,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR002583-1"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023016"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00505"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000002","properties":[{"key":"ProteinId","value":"MFC7418426.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185407.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000002.1"}]},{"database":"Proteomes","id":"UP001596473","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:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0140662","properties":[{"key":"GoTerm","value":"F:ATP-dependent protein folding chaperone"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16927","properties":[{"key":"EntryName","value":"HATPase_Hsp90-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.80:FF:000002","properties":[{"key":"EntryName","value":"Molecular chaperone HtpG"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.565.10:FF:000009","properties":[{"key":"EntryName","value":"Molecular chaperone HtpG"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.80","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.11260","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.790","properties":[{"key":"EntryName","value":"Heat shock protein 90, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.565.10","properties":[{"key":"EntryName","value":"Histidine kinase-like ATPase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00505","properties":[{"key":"EntryName","value":"HSP90"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036890","properties":[{"key":"EntryName","value":"HATPase_C_sf"}]},{"database":"InterPro","id":"IPR003594","properties":[{"key":"EntryName","value":"HATPase_dom"}]},{"database":"InterPro","id":"IPR019805","properties":[{"key":"EntryName","value":"Heat_shock_protein_90_CS"}]},{"database":"InterPro","id":"IPR037196","properties":[{"key":"EntryName","value":"HSP90_C"}]},{"database":"InterPro","id":"IPR001404","properties":[{"key":"EntryName","value":"Hsp90_fam"}]},{"database":"InterPro","id":"IPR020575","properties":[{"key":"EntryName","value":"Hsp90_N"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"NCBIfam","id":"NF003555","properties":[{"key":"EntryName","value":"htpG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11528","properties":[{"key":"EntryName","value":"HEAT SHOCK PROTEIN 90 FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13589","properties":[{"key":"EntryName","value":"HATPase_c_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00183","properties":[{"key":"EntryName","value":"HSP90"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF002583","properties":[{"key":"EntryName","value":"Hsp90"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00775","properties":[{"key":"EntryName","value":"HEATSHOCK90"}]},{"database":"SMART","id":"SM00387","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55874","properties":[{"key":"EntryName","value":"ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF110942","properties":[{"key":"EntryName","value":"HSP90 C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00298","properties":[{"key":"EntryName","value":"HSP90"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKETLGFQTEVKQLLQLMIHSLYSNKEIFLRELISNASDACDKLRFEALNDASLYGDDSELKISLSFDKEARTLTLNDNGIGMSRDEVVKNIGTIARSGTKEFFGKLSGDAQKDANLIGQFGVGFYSAFIVADKVTLTSRRAGEATATQWESLGDGEFTLEEVAKEGRGTEIVLHLKEGEDEYLSDWSLRSIIRKYSDHITLPIFMPKTAGYDDEGNVTPAEGVEAVNQASALWARAKSEISDEQYTEFYKHVSHDFEAPLAWSHARVEGKQEYTELLYIPQRAPFDMHDRERRHGIKLYVRRVFIMEDAEKLLPQYLRFVRGLIDSSNLPLNVSREILQHSKDIEQIKQGCVKKVLGLLESMANSDDAAEQAKYVTFWEQFGRVMKEGVAEDFANKDRIAALLRFSSSHSDSTEQNVSLAAYVGRMKEGQDKIYFITADSFAAAKNSPHLEVFRKKGIEVLLMSERVDEWMISGLTEFDGKKLQSVTKGELDLSQFENEEEKQQQEAAASELKDVLDKVKAVLGDKVKDVRVTNRLTDSPACIVVENQDMSANLERLLKSAGQDVKGSKPILEINPEHMLVKKLKAELEGERFSDWTELLFDQAQLAEGAQLDDPATFVKRLNSLMMSVAA","length":633,"molWeight":71195,"crc64":"C12F897D3FB99244","md5":"2B8095BABB8F3D491489C35C2FEEE379"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Coiled coil":1,"Binding site":9},"uniParcId":"UPI0036179E7D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRX1","uniProtkbId":"A0ABW2QRX1_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418502.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029514"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Adenosine 5'-phosphosulfate reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"APS reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024386"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"1.8.4.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032041"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"5'-adenylylsulfate reductase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030894"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Thioredoxin-dependent 5'-adenylylsulfate reductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"cysH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418502.1"}],"value":"ACFQNF_01235"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024298"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Catalyzes the formation of sulfite from adenosine 5'-phosphosulfate (APS) using thioredoxin as an electron donor"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[thioredoxin]-disulfide + sulfite + AMP + 2 H(+) = adenosine 5'-phosphosulfate + [thioredoxin]-dithiol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21976"},{"database":"Rhea","id":"RHEA-COMP:10698"},{"database":"Rhea","id":"RHEA-COMP:10700"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17359"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:50058"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"1.8.4.10","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048441"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Binds 1 [4Fe-4S] cluster per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024327"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009732"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"value":"Belongs to the PAPS reductase family. CysH subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418502.1"}],"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":25,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Phosphoadenosine phosphosulphate reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01507"}]},{"type":"Active site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"Nucleophile; cysteine thiosulfonate intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}]},{"type":"Binding site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00063"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000002","properties":[{"key":"ProteinId","value":"MFC7418502.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185538.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000002.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043866","properties":[{"key":"GoTerm","value":"F:adenylyl-sulfate reductase (thioredoxin) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004604","properties":[{"key":"GoTerm","value":"F:phosphoadenylyl-sulfate reductase (thioredoxin) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019344","properties":[{"key":"GoTerm","value":"P:L-cysteine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd23945","properties":[{"key":"EntryName","value":"PAPS_reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00063","properties":[{"key":"EntryName","value":"CysH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011798","properties":[{"key":"EntryName","value":"APS_reductase"}]},{"database":"InterPro","id":"IPR004511","properties":[{"key":"EntryName","value":"PAPS/APS_Rdtase"}]},{"database":"InterPro","id":"IPR002500","properties":[{"key":"EntryName","value":"PAPS_reduct_dom"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR02055","properties":[{"key":"EntryName","value":"APS_reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00434","properties":[{"key":"EntryName","value":"cysH"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002537","properties":[{"key":"EntryName","value":"PRK02090.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46482:SF9","properties":[{"key":"EntryName","value":"5'-ADENYLYLSULFATE REDUCTASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46482","properties":[{"key":"EntryName","value":"5'-ADENYLYLSULFATE REDUCTASE 3, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01507","properties":[{"key":"EntryName","value":"PAPS_reduct"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000857","properties":[{"key":"EntryName","value":"PAPS_reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSFEEKLTETIALLHKIADEYSPAVFANSLGAEDMVITDLIAKHQVGVQIFSLDTGRLPTQTYALMQKSAEQYPSHPIQVFFPQTSATESFVNQHGINAFYESIELRKACCQIRKMEPLKRALAGKKAWVTGLRREQSPTRTDLGNQEFDSGNGLEKFNPLIEWTEKEVWAYLRDNNVPYNALHDQHYPSIGCEPCTRAISMGEDVRAGRWWWEDPENKECGLHVKK","length":227,"molWeight":25905,"crc64":"2821107956870054","md5":"A69631F322FF514533A13C1CFA2853F8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":4},"uniParcId":"UPI00360BECB2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRZ0","uniProtkbId":"A0ABW2QRZ0_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418296.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Bifunctional protein FolD"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Methylenetetrahydrofolate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"1.5.1.5"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Methenyltetrahydrofolate cyclohydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"3.5.4.9"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418296.1"}],"value":"folD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418296.1"}],"value":"ACFQNF_00185"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57455"},{"database":"ChEBI","id":"CHEBI:195366"}],"ecNumber":"3.5.4.9","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22812"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57455"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.5.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"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_01576"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418296.1"}],"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":6,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Tetrahydrofolate dehydrogenase/cyclohydrolase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00763"}]},{"type":"Domain","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"Tetrahydrofolate dehydrogenase/cyclohydrolase NAD(P)-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02882"}]},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023102"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0368","category":"Biological process","name":"Histidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418296.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_046351386.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","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:0004477","properties":[{"key":"GoTerm","value":"F:methenyltetrahydrofolate cyclohydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004488","properties":[{"key":"GoTerm","value":"F:methylenetetrahydrofolate dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01080","properties":[{"key":"EntryName","value":"NAD_bind_m-THF_DH_Cyclohyd"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000006","properties":[{"key":"EntryName","value":"Bifunctional protein FolD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01576","properties":[{"key":"EntryName","value":"THF_DHG_CYH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR000672","properties":[{"key":"EntryName","value":"THF_DH/CycHdrlase"}]},{"database":"InterPro","id":"IPR020630","properties":[{"key":"EntryName","value":"THF_DH/CycHdrlase_cat_dom"}]},{"database":"InterPro","id":"IPR020631","properties":[{"key":"EntryName","value":"THF_DH/CycHdrlase_NAD-bd_dom"}]},{"database":"NCBIfam","id":"NF008058","properties":[{"key":"EntryName","value":"folD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010783","properties":[{"key":"EntryName","value":"folD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48099:SF5","properties":[{"key":"EntryName","value":"C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48099","properties":[{"key":"EntryName","value":"C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00763","properties":[{"key":"EntryName","value":"THF_DHG_CYH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02882","properties":[{"key":"EntryName","value":"THF_DHG_CYH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00085","properties":[{"key":"EntryName","value":"THFDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAQILDGKIISAEIVSDVRAKVDARVASGLRAPALAVILVGADPASQVYVGNKKRQCANAGIRSIDIDLPADTSEADLLALVAKFNQDDEIDGILVQLPLPKHINAEKVIELIDPVKDVDGFHPYNIGRLALKMPLLRPCTPRGVMTLLERTGIDIVGKDAVIVGASNIVGRPQALELLLARATVTICHSKTQDLESKVRGADIVVAGVGIPNFVKGDWIKAGAIVIDVGINRLENGKLCGDVEFDVAKEKAAWITPVPGGVGLMTVATLMQNTFDACVNRKG","length":284,"molWeight":30104,"crc64":"33ED7C30A864ED18","md5":"B9FA8D22C4BAB757A499FEC43CF94707"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":2},"uniParcId":"UPI00061D3B06"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QRZ9","uniProtkbId":"A0ABW2QRZ9_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418300.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"Ion-translocating oxidoreductase complex subunit C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"7.-.-.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"Rnf electron transport complex subunit C"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418300.1"}],"value":"rsxC"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"rnfC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418300.1"}],"value":"ACFQNF_00205"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"Part of a membrane-bound complex that couples electron transfer with translocation of ions across the membrane"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"Binds 2 [4Fe-4S] clusters per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"The complex is composed of six subunits: RnfA, RnfB, RnfC, RnfD, RnfE and RnfG"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"value":"Belongs to the 4Fe4S bacterial-type ferredoxin family. RnfC subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418300.1"}],"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":360,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"4Fe-4S ferredoxin-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51379"}]},{"type":"Domain","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"4Fe-4S ferredoxin-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51379"}]},{"type":"Region","location":{"start":{"value":551,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":589,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}},{"type":"Binding site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"2"}},{"type":"Binding site","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0997","category":"Cellular component","name":"Cell inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"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_00461"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00461"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000001","properties":[{"key":"ProteinId","value":"MFC7418300.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185205.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000001.1"}]},{"database":"Proteomes","id":"UP001596473","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:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0022900","properties":[{"key":"GoTerm","value":"P:electron transport chain"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.10.20.600","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.11540","properties":[{"key":"EntryName","value":"NADH-ubiquinone oxidoreductase 51kDa subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00461","properties":[{"key":"EntryName","value":"RsxC_RnfC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017896","properties":[{"key":"EntryName","value":"4Fe4S_Fe-S-bd"}]},{"database":"InterPro","id":"IPR017900","properties":[{"key":"EntryName","value":"4Fe4S_Fe_S_CS"}]},{"database":"InterPro","id":"IPR010208","properties":[{"key":"EntryName","value":"Ion_transpt_RnfC/RsxC"}]},{"database":"InterPro","id":"IPR011538","properties":[{"key":"EntryName","value":"Nuo51_FMN-bd"}]},{"database":"InterPro","id":"IPR037225","properties":[{"key":"EntryName","value":"Nuo51_FMN-bd_sf"}]},{"database":"InterPro","id":"IPR026902","properties":[{"key":"EntryName","value":"RnfC_N"}]},{"database":"InterPro","id":"IPR019554","properties":[{"key":"EntryName","value":"Soluble_ligand-bd"}]},{"database":"NCBIfam","id":"TIGR01945","properties":[{"key":"EntryName","value":"rnfC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003454","properties":[{"key":"EntryName","value":"rsxC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43034","properties":[{"key":"EntryName","value":"ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43034:SF2","properties":[{"key":"EntryName","value":"ION-TRANSLOCATING OXIDOREDUCTASE COMPLEX SUBUNIT C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01512","properties":[{"key":"EntryName","value":"Complex1_51K"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12838","properties":[{"key":"EntryName","value":"Fer4_7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13375","properties":[{"key":"EntryName","value":"RnfC_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10531","properties":[{"key":"EntryName","value":"SLBB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46548","properties":[{"key":"EntryName","value":"alpha-helical ferredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142019","properties":[{"key":"EntryName","value":"Nqo1 FMN-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00198","properties":[{"key":"EntryName","value":"4FE4S_FER_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51379","properties":[{"key":"EntryName","value":"4FE4S_FER_2"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MNRQIITFHGGVHPPEHKAESSHYPIRTAALPARLILSLQQSIGSAAKPLVKVGDEVAKGQLIAAADGMISAALHAPTSGRIEAIDLYSIAHPSGLSDNCIVLIPDGKDQWLERPLFDWRNAEPNAVRTYLRDMGVVGLGGAVFPSHLKLSSKTQLDTLIINGAECEPYITCDDRLMRERATEIIAGILMVQSLLNAKQVLIGIEDNKPEAAAALRDAIKASRSQAVAAIEVVQVSTLYPSGGAKQLIKLLCNIEVPSGVRSTDLGVQCFNVATIHSIYCALAHAEPVIRRVVTITGNVARPGNYEALIGTPLAALLKEAGGKGSSGYIYGGPMMGFELPSLEVGLSKAGNCVIAKTPADFPEQPREMPCIRCSKCAEACPAELQPMDLFWFAKSKNFGKAQERNLFDCIECGACAYVCPSNIRLVDYYRFAKSEIWAAEKTKHAADLARERFEFREFRAEREKQEKAERLAAKASQKLAQAVASDDPEDAIRAAKIKAAIAKSAVANESPVSDAGVAVTDADQAAQLAAEKKAKIAAAMARAAAKKAEAEAAVPVARPEPPMAPSQTLPASSMDKTDRTKEILDKRREERARIAAMSPEERSEWEAAKKIEIEAAKAAAALRKGSGEPGAVS","length":633,"molWeight":67831,"crc64":"3FE2C00634E82939","md5":"45CD8F31CB83E788E2794436453CEBBE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Binding site":8},"uniParcId":"UPI00362362B2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QS60","uniProtkbId":"A0ABW2QS60_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418468.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"Cysteine desulfurase IscS"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"2.8.1.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"iscS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418468.1"}],"value":"ACFQNF_01065"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"Master enzyme that delivers sulfur to a number of partners involved in Fe-S cluster assembly, tRNA modification or cofactor biosynthesis. Catalyzes the removal of elemental sulfur atoms from cysteine to produce alanine. Functions as a sulfur delivery protein for Fe-S cluster synthesis onto IscU, an Fe-S scaffold assembly protein, as well as other S acceptor proteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(sulfur carrier)-H + L-cysteine = (sulfur carrier)-SH + L-alanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43892"},{"database":"Rhea","id":"RHEA-COMP:14737"},{"database":"Rhea","id":"RHEA-COMP:14739"},{"database":"ChEBI","id":"CHEBI:29917"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:57972"},{"database":"ChEBI","id":"CHEBI:64428"}],"ecNumber":"2.8.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050776"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004504"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005151"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"Cofactor biosynthesis; iron-sulfur cluster biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"Homodimer. Forms a heterotetramer with IscU, interacts with other sulfur acceptors"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"value":"Belongs to the class-V pyridoxal-phosphate-dependent aminotransferase family. NifS/IscS subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418468.1"}],"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":367,"modifier":"EXACT"}},"description":"Aminotransferase class V","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00266"}]},{"type":"Active site","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}]},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"via persulfide group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:190135"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"ligand":{"name":"[2Fe-2S] cluster","id":"ChEBI:CHEBI:190135","note":"ligand shared with IscU"}},{"type":"Modified residue","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022714"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00331"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"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_00331"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000002","properties":[{"key":"ProteinId","value":"MFC7418468.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185478.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000002.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0051537","properties":[{"key":"GoTerm","value":"F:2 iron, 2 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031071","properties":[{"key":"GoTerm","value":"F:cysteine desulfurase 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:0044571","properties":[{"key":"GoTerm","value":"P:[2Fe-2S] cluster assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.640.10:FF:000003","properties":[{"key":"EntryName","value":"Cysteine desulfurase IscS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000002","properties":[{"key":"EntryName","value":"Cysteine desulfurase IscS"},{"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_00331","properties":[{"key":"EntryName","value":"Cys_desulf_IscS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000192","properties":[{"key":"EntryName","value":"Aminotrans_V_dom"}]},{"database":"InterPro","id":"IPR020578","properties":[{"key":"EntryName","value":"Aminotrans_V_PyrdxlP_BS"}]},{"database":"InterPro","id":"IPR010240","properties":[{"key":"EntryName","value":"Cys_deSase_IscS"}]},{"database":"InterPro","id":"IPR016454","properties":[{"key":"EntryName","value":"Cysteine_dSase"}]},{"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":"TIGR02006","properties":[{"key":"EntryName","value":"IscS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010611","properties":[{"key":"EntryName","value":"PRK14012.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11601:SF34","properties":[{"key":"EntryName","value":"CYSTEINE DESULFURASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11601","properties":[{"key":"EntryName","value":"CYSTEINE DESULFURYLASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00266","properties":[{"key":"EntryName","value":"Aminotran_5"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005572","properties":[{"key":"EntryName","value":"NifS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00595","properties":[{"key":"EntryName","value":"AA_TRANSFER_CLASS_5"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSATKPIYLDYSATTPVDPRVAAKMIPCLTEHFGNPASRSHAFGWEAEAAVEEAREQVAALVNCDPKEIVWTSGATESNNLALKGAAHFYQAKGKHLITVKTEHKAILDTMRELEREGFEVTYLDVKDNGLLDLDVLKAAIRPDTIVISVMSVNNEIGVIQDIATIGEICREKGIIFHVDSAQATGKIAIDLSVLKVDLMSFSAHKTYGPKGIGALYIRRKPRIRLEAQMHGGGHERGFRSGTLATHQIVGMGEAFRIAKEDMGTELERMRMLRDRLWAGLSDIEEVHLNGDMEQRVPHNLNVSFNYVEGESLVMALKELAVSSGSACTSASLEPSYVLRALGRSDELAHSSIRFTIGRFNTVEEIDFAITLIRSKIGKLRELSPLWDMYKEGIDISTIEWAAH","length":404,"molWeight":44675,"crc64":"E9477815CFD96026","md5":"68E2D7E0D9C61CB47383674875F53744"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":6,"Modified residue":1},"uniParcId":"UPI00361D5FA6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QSB4","uniProtkbId":"A0ABW2QSB4_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418623.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"value":"Protein-methionine-sulfoxide reductase catalytic subunit MsrP"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"value":"1.8.5.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418623.1"}],"value":"msrP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418623.1"}],"value":"ACFQNF_01860"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"value":"Part of the MsrPQ system that repairs oxidized periplasmic proteins containing methionine sulfoxide residues (Met-O), using respiratory chain electrons. Thus protects these proteins from oxidative-stress damage caused by reactive species of oxygen and chlorine generated by the host defense mechanisms. MsrPQ is essential for the maintenance of envelope integrity under bleach stress, rescuing a wide series of structurally unrelated periplasmic proteins from methionine oxidation. The catalytic subunit MsrP is non-stereospecific, being able to reduce both (R-) and (S-) diastereoisomers of methionine sulfoxide"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-methionyl-[protein] + a quinone + H2O = L-methionyl-(R)-S-oxide-[protein] + a quinol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51296"},{"database":"Rhea","id":"RHEA-COMP:12313"},{"database":"Rhea","id":"RHEA-COMP:12314"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16044"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:45764"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-methionyl-[protein] + a quinone + H2O = L-methionyl-(S)-S-oxide-[protein] + a quinol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:51292"},{"database":"Rhea","id":"RHEA-COMP:12313"},{"database":"Rhea","id":"RHEA-COMP:12315"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16044"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:44120"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mo-molybdopterin","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:71302"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"value":"Binds 1 Mo-molybdopterin (Mo-MPT) cofactor per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"value":"Heterodimer of a catalytic subunit (MsrP) and a heme-binding subunit (MsrQ)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00648"}],"value":"Predicted to be exported by the Tat system. The position of the signal peptide cleavage has not been experimentally proven"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"value":"Belongs to the MsrP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418623.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"Protein-methionine-sulfoxide reductase catalytic subunit MsrP","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00648"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5050148080"},{"type":"Domain","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Oxidoreductase molybdopterin-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00174"}]},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:71302"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"ligand":{"name":"Mo-molybdopterin","id":"ChEBI:CHEBI:71302"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:71302"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"ligand":{"name":"Mo-molybdopterin","id":"ChEBI:CHEBI:71302"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:71302"},{"database":"ChEBI","id":"CHEBI:28685"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"ligand":{"name":"Mo-molybdopterin","id":"ChEBI:CHEBI:71302"},"ligandPart":{"name":"Mo","id":"ChEBI:CHEBI:28685"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:71302"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"ligand":{"name":"Mo-molybdopterin","id":"ChEBI:CHEBI:71302"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:71302"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"ligand":{"name":"Mo-molybdopterin","id":"ChEBI:CHEBI:71302"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:71302"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"ligand":{"name":"Mo-molybdopterin","id":"ChEBI:CHEBI:71302"}},{"type":"Binding site","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:71302"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"ligand":{"name":"Mo-molybdopterin","id":"ChEBI:CHEBI:71302"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022505"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"id":"KW-0500","category":"Ligand","name":"Molybdenum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01206"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000004","properties":[{"key":"ProteinId","value":"MFC7418623.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185700.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000004.1"}]},{"database":"Proteomes","id":"UP001596473","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0043546","properties":[{"key":"GoTerm","value":"F:molybdopterin cofactor binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016672","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on a sulfur group of donors, quinone or similar compound as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030091","properties":[{"key":"GoTerm","value":"P:protein repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.90.420.10","properties":[{"key":"EntryName","value":"Oxidoreductase, molybdopterin-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01206","properties":[{"key":"EntryName","value":"MsrP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022867","properties":[{"key":"EntryName","value":"MsrP"}]},{"database":"InterPro","id":"IPR000572","properties":[{"key":"EntryName","value":"OxRdtase_Mopterin-bd_dom"}]},{"database":"InterPro","id":"IPR036374","properties":[{"key":"EntryName","value":"OxRdtase_Mopterin-bd_sf"}]},{"database":"InterPro","id":"IPR006311","properties":[{"key":"EntryName","value":"TAT_signal"}]},{"database":"NCBIfam","id":"NF003767","properties":[{"key":"EntryName","value":"msrP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43032","properties":[{"key":"EntryName","value":"PROTEIN-METHIONINE-SULFOXIDE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43032:SF3","properties":[{"key":"EntryName","value":"PROTEIN-METHIONINE-SULFOXIDE REDUCTASE CATALYTIC SUBUNIT MSRP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00174","properties":[{"key":"EntryName","value":"Oxidored_molyb"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56524","properties":[{"key":"EntryName","value":"Oxidoreductase molybdopterin-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51318","properties":[{"key":"EntryName","value":"TAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLIRSSTEILPSEITPESIWLNRRQIMTGAAALGLAAALPAQAAGELVYRSSPLSAKDDKNTFEQITQYNNYYEFGTGKDDPAKAAHTLKTRPWNIVIEGECEKPRTFSIEELLKIAPLEERIYRLRCVEGWSMVIPWVGFPLSELIKRVNPTSKAKYVEFISLADKAQMPGVGRSVLDWPYTEGLRMDEAMHPLAIMVVGLYGKVLPNQNGAPIRLVVPWKYGFKSAKSIVKIRLTEKQPQTSWNKAGPNEYGFYSNVNPEVDHPRWSQVTERRIGEFFKRKTLMFNGYGDQVAGMYKGMDLKKLF","length":307,"molWeight":34811,"crc64":"99DA5B4784017F75","md5":"184F2E33153537146971C00CBFDE757D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Binding site":7},"uniParcId":"UPI0036194715"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QSF7","uniProtkbId":"A0ABW2QSF7_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418682.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012081"}],"value":"lactoylglutathione lyase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012081"}],"value":"4.4.1.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030892"}],"value":"Aldoketomutase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030537"}],"value":"Glyoxalase I"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030291"}],"value":"Ketone-aldehyde mutase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032460"}],"value":"Methylglyoxalase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033298"}],"value":"S-D-lactoylglutathione methylglyoxal lyase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418682.1"}],"value":"gloA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418682.1"}],"value":"ACFQNF_02160"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-S-lactoylglutathione = methylglyoxal + glutathione","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19069"},{"database":"ChEBI","id":"CHEBI:17158"},{"database":"ChEBI","id":"CHEBI:57474"},{"database":"ChEBI","id":"CHEBI:57925"}],"ecNumber":"4.4.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048273"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001967"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-3"}],"value":"Binds 1 zinc ion per subunit. In the homodimer, two zinc ions are bound between subunits."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005008"}],"value":"Secondary metabolite metabolism; methylglyoxal degradation; (R)-lactate from methylglyoxal: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010363"}],"value":"Belongs to the glyoxalase I family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418682.1"}],"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":2,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"VOC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51819"}]},{"type":"Active site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-1"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}]},{"type":"Binding site","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01163"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418682.1"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR604361-3"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000004","properties":[{"key":"ProteinId","value":"MFC7418682.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185911.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000004.1"}]},{"database":"Proteomes","id":"UP001596473","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:0004462","properties":[{"key":"GoTerm","value":"F:lactoylglutathione lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.10.180.10","properties":[{"key":"EntryName","value":"2,3-Dihydroxybiphenyl 1,2-Dioxygenase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029068","properties":[{"key":"EntryName","value":"Glyas_Bleomycin-R_OHBP_Dase"}]},{"database":"InterPro","id":"IPR004360","properties":[{"key":"EntryName","value":"Glyas_Fos-R_dOase_dom"}]},{"database":"InterPro","id":"IPR004361","properties":[{"key":"EntryName","value":"Glyoxalase_1"}]},{"database":"InterPro","id":"IPR018146","properties":[{"key":"EntryName","value":"Glyoxalase_1_CS"}]},{"database":"InterPro","id":"IPR037523","properties":[{"key":"EntryName","value":"VOC_core"}]},{"database":"NCBIfam","id":"TIGR00068","properties":[{"key":"EntryName","value":"glyox_I"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46036","properties":[{"key":"EntryName","value":"LACTOYLGLUTATHIONE LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46036:SF5","properties":[{"key":"EntryName","value":"LACTOYLGLUTATHIONE LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00903","properties":[{"key":"EntryName","value":"Glyoxalase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54593","properties":[{"key":"EntryName","value":"Glyoxalase/Bleomycin resistance protein/Dihydroxybiphenyl dioxygenase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00934","properties":[{"key":"EntryName","value":"GLYOXALASE_I_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51819","properties":[{"key":"EntryName","value":"VOC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRLMHTMLRVADLDASIRFYQAVLGMQVLRRIDFSEGRFSLVYLGYGPESEQAAIELTWNWDKQDYTHGNYYGHIAIESDDIKGLCKQASELAYRVSRKPGPMKQSSAIIAFIEDPDGHQIELIQQGSL","length":129,"molWeight":14712,"crc64":"6B1B10E298B8228D","md5":"672D3239CDF1C458D47759B38378F05F"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":7},"uniParcId":"UPI00362159AE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW2QSG0","uniProtkbId":"A0ABW2QSG0_9NEIS","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Iodobacter arcticus","taxonId":590593,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418573.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Betaproteobacteria","Neisseriales","Chitinibacteraceae","Iodobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"Acetate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"2.7.2.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"Acetokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"ackA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418573.1"}],"value":"ACFQNF_01610"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"Catalyzes the formation of acetyl phosphate from acetate and ATP. Can also catalyze the reverse reaction"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetate + ATP = acetyl phosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11352"},{"database":"ChEBI","id":"CHEBI:22191"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"Mg(2+). Can also accept Mn(2+)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"Metabolic intermediate biosynthesis; acetyl-CoA biosynthesis; acetyl-CoA from acetate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008748"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003835"}],"value":"Belongs to the acetokinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC7418573.1"}],"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":"Active site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":9,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":328,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}]},{"type":"Site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00020"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"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_00020"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}],"value":"CCUG 62945","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001596473"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTBQ010000004","properties":[{"key":"ProteinId","value":"MFC7418573.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_380185643.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTBQ010000004.1"}]},{"database":"Proteomes","id":"UP001596473","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:0008776","properties":[{"key":"GoTerm","value":"F:acetate kinase 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:0006083","properties":[{"key":"GoTerm","value":"P:acetate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006085","properties":[{"key":"GoTerm","value":"P:acetyl-CoA biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00020","properties":[{"key":"EntryName","value":"Acetate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004372","properties":[{"key":"EntryName","value":"Ac/propionate_kinase"}]},{"database":"InterPro","id":"IPR000890","properties":[{"key":"EntryName","value":"Aliphatic_acid_kin_short-chain"}]},{"database":"InterPro","id":"IPR023865","properties":[{"key":"EntryName","value":"Aliphatic_acid_kinase_CS"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"NCBIfam","id":"TIGR00016","properties":[{"key":"EntryName","value":"ackA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21060","properties":[{"key":"EntryName","value":"ACETATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21060:SF21","properties":[{"key":"EntryName","value":"ACETATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00871","properties":[{"key":"EntryName","value":"Acetate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000722","properties":[{"key":"EntryName","value":"Acetate_prop_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00471","properties":[{"key":"EntryName","value":"ACETATEKNASE"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS01075","properties":[{"key":"EntryName","value":"ACETATE_KINASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01076","properties":[{"key":"EntryName","value":"ACETATE_KINASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKAILVLNAGSSSLKFSLFEYEAASDLHLMAKGQVEGIGNAPHFVAKDHHEQILADEHWQGEDKDHDHCLRAIATLLNQHYQGLKLLGVGHRVVHGGAHYAAPVRLTPGIINALDALTPLAPLHQSHNLAAIRAVASALPGLPQIACFDTAFHRSQNQINQLFGLPYSCYERGIRRYGFHGLSYEYVSSTLKQREPEIAAGKVVIAHLGNGASMCAVQNGKSVASSMGFTALDGLMMGTRTGNLDAGVVLYLLQQEQLSVQQVEELLYKRSGLLGLSGISSDMRVLLDSHEPQAALAVDYFVHRISRELGSLAASMNGLDALVFTAGIGENSAIIRQRVCEQAQWLGIDIDPHANAANEFCISAIDSPTTVWLIPSNEELMIARHTRTQLGL","length":393,"molWeight":42578,"crc64":"D11E9361885ED925","md5":"47A26BE6A9CF1F726A99EFF5708768AA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":1,"Binding site":7,"Site":2},"uniParcId":"UPI0036239CA6"}}]}