{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R2G5","uniProtkbId":"A0ABY3R2G5_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenylyl-sulfate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"2.7.1.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"APS kinase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"ATP adenosine-5'-phosphosulfate 3'-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenosine-5'-phosphosulfate kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01509.1"}],"value":"cysC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01509.1"}],"value":"LQG66_19470"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002357"}],"value":"APS kinase catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024872"}],"value":"Proposed to provide activated sulfate for transfer to Nod factor. ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049370"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011760"}],"value":"Sulfate-activating enzymes, NodP and NodQ, may be physically associated"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}],"value":"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005438"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007237"}],"value":"In the N-terminal section; belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"Tr-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51722"}]},{"type":"Region","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"G1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"G2","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"G3","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"G4","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"G5","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Active site","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01509.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"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_00065"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01509.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01509.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01509.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317307.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_19470","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO: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:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04166","properties":[{"key":"EntryName","value":"CysN_ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04095","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"},{"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":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00065","properties":[{"key":"EntryName","value":"Adenylyl_sulf_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR041757","properties":[{"key":"EntryName","value":"CysN_GTP-bd"}]},{"database":"InterPro","id":"IPR044139","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"}]},{"database":"InterPro","id":"IPR031157","properties":[{"key":"EntryName","value":"G_TR_CS"}]},{"database":"InterPro","id":"IPR054696","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011779","properties":[{"key":"EntryName","value":"SO4_adenylTrfase_lsu"}]},{"database":"InterPro","id":"IPR000795","properties":[{"key":"EntryName","value":"T_Tr_GTP-bd_dom"}]},{"database":"InterPro","id":"IPR050100","properties":[{"key":"EntryName","value":"TRAFAC_GTPase_members"}]},{"database":"InterPro","id":"IPR009000","properties":[{"key":"EntryName","value":"Transl_B-barrel_sf"}]},{"database":"InterPro","id":"IPR009001","properties":[{"key":"EntryName","value":"Transl_elong_EF1A/Init_IF2_C"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02034","properties":[{"key":"EntryName","value":"CysN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003013","properties":[{"key":"EntryName","value":"PRK03846.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23115","properties":[{"key":"EntryName","value":"TRANSLATION FACTOR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22594","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00009","properties":[{"key":"EntryName","value":"GTP_EFTU"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00315","properties":[{"key":"EntryName","value":"ELONGATNFCT"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF50465","properties":[{"key":"EntryName","value":"EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF50447","properties":[{"key":"EntryName","value":"Translation proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00301","properties":[{"key":"EntryName","value":"G_TR_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51722","properties":[{"key":"EntryName","value":"G_TR_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNMRVPSAAPATPNGTTRPQVRIVIVGHVDHGKSTLVGRLLHETGSLPEGKLEMLQAVSARRGMPFEWSFLLDALQTERDQGITIDTTQIRFRTNEREVVLIDAPGHAEFLRNMITGASQADGAVLIIDALEGVRDQTRRHGYLLHLLGVKQVAVVVNKMDRVDFGQARFDEIKAEISAHLEGLGVTPVAVIPISARDGDGVAQHTSRIGWYKGPTVVEALDGLEPARPLSSLPLRLPVQAIYKFDDRRIVAGRIEAGELKTGDEIVIMPAGKIAKIKSVEGWPATPVTTPQGAGRSVGITLDRELFIERGDVIAHVGREPQASRRLHARIFWLHDQPLSKGDSIVVRLGTREARGSVVAIDKAVDPGSLSNEENAAIARNHVGEIEIALTQPVAIDPYTENARTGRLVIEVQGRIAGGGLVLTVDAGKRAQPVDIMPVESALQPQERADRYRHKGAVVWMTGLPGAGKSTLARALERRLFGRGGAPVLLDGDTVRAGLNKDLGFTPEDRAENIRRLAEVATHLARNGHIAIVAAVSPGREDRAAARRVAGDLFREIYVATAAEICESRDPKGHYAKARAGNLQNFTGIGTDYEPPLDAELVIDTATRGIADATDELEALLSRTGVLFDDIADLGANI","length":638,"molWeight":68816,"crc64":"74F25825ED256B6F","md5":"AA823B05F3B5172C69E87F572CC83270"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":4},"countByFeatureType":{"Domain":1,"Region":5,"Active site":1,"Binding site":1},"uniParcId":"UPI001E2B28BA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R2Q7","uniProtkbId":"A0ABY3R2Q7_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01399.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ATP-dependent zinc metalloprotease FtsH"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"3.4.24.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01399.1"}],"value":"ftsH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01399.1"}],"value":"LQG66_18880"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Multi-pass membrane protein","id":"SL-9909"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003651"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010044"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the C-terminal section; belongs to the peptidase M41 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the central section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":596,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":596,"modifier":"EXACT"},"end":{"value":607,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":631,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01399.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01399.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01399.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317197.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_18880","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004222","properties":[{"key":"GoTerm","value":"F:metalloendopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19501","properties":[{"key":"EntryName","value":"RecA-like_FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.760:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.720.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.760","properties":[{"key":"EntryName","value":"Peptidase M41"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01458","properties":[{"key":"EntryName","value":"FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR041569","properties":[{"key":"EntryName","value":"AAA_lid_3"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR003960","properties":[{"key":"EntryName","value":"ATPase_AAA_CS"}]},{"database":"InterPro","id":"IPR005936","properties":[{"key":"EntryName","value":"FtsH"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011546","properties":[{"key":"EntryName","value":"Pept_M41_FtsH_extracell"}]},{"database":"InterPro","id":"IPR000642","properties":[{"key":"EntryName","value":"Peptidase_M41"}]},{"database":"InterPro","id":"IPR037219","properties":[{"key":"EntryName","value":"Peptidase_M41-like"}]},{"database":"NCBIfam","id":"TIGR01241","properties":[{"key":"EntryName","value":"FtsH_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076:SF97","properties":[{"key":"EntryName","value":"ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076","properties":[{"key":"EntryName","value":"METALLOPROTEASE M41 FTSH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17862","properties":[{"key":"EntryName","value":"AAA_lid_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06480","properties":[{"key":"EntryName","value":"FtsH_ext"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01434","properties":[{"key":"EntryName","value":"Peptidase_M41"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140990","properties":[{"key":"EntryName","value":"FtsH protease domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00674","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNANLRNFALWVIIVLLLLALFTLFQNPGQRASSTDISFSQLLTEVDQGNVRDVVIQGPEIHGTFKNGSSFQTYAPNDPSLVTRLYNGKVSITAKPPGDNVPWFVSLLVSWLPFIALIGVWIFLSRQMQGGAGKAMGFGKSRAKMLTEAHGRVTFEDVAGVDEAKQDLQEIVEFLRDPGKFQRLGGRIPRGVLLVGPPGTGKTLIARAVAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQLLVEMDGFEANEGVILIAATNRPDVLDPALMRPGRFDRQVVVSNPDIMGREQILKVHVRKVPLAPDVNLKTIARGTPGFSGADLMNLVNEAALTAARRNKRMVTQSEFEEAKDKVLMGAERRSMVMTEEEKMLTAYHEAGHAIVGLNVPSHDPIHKATIIPRGRALGMVQSLPEADRHSHTREWCVSKLAMMFGGREAEVQKFGAEKVTNGATGDIQQATNLARAMVMEWGMSDKLGRVRYQSNEQEVFLGHSVARSTNISDDTARLIDSEIRGLIEAGELEARRIITEKREHWEAIAQALLEYETLTGEEINDLLKGKKPNRESAVEPSTPRASAVPPAGKPRPRPDPDPGLEPQPQA","length":640,"molWeight":70121,"crc64":"5BB5CB07DAB258A5","md5":"BDD6BA055A92ED971933971DB18E6961"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":2,"Active site":1,"Binding site":4},"uniParcId":"UPI001E4272D0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R594","uniProtkbId":"A0ABY3R594_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02217.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"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":"UFZ02217.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02217.1"}],"value":"LQG66_23305"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"Antitoxin FitA-like ribbon-helix-helix","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF22513"}]},{"type":"Domain","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":467,"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":257,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Compositional bias","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"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":372,"modifier":"EXACT"},"end":{"value":375,"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":392,"modifier":"EXACT"},"end":{"value":392,"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":406,"modifier":"EXACT"},"end":{"value":406,"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":410,"modifier":"EXACT"},"end":{"value":410,"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":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02217.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02217.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ02217.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231318007.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_23305","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006355","properties":[{"key":"GoTerm","value":"P:regulation of DNA-templated transcription"},{"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":"Gene3D","id":"1.10.1220.10","properties":[{"key":"EntryName","value":"Met repressor-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013321","properties":[{"key":"EntryName","value":"Arc_rbn_hlx_hlx"}]},{"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":"IPR053853","properties":[{"key":"EntryName","value":"FitA-like_RHH"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"InterPro","id":"IPR010985","properties":[{"key":"EntryName","value":"Ribbon_hlx_hlx"}]},{"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":"PF22513","properties":[{"key":"EntryName","value":"FitA-like_RHH"},{"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"}]},{"database":"SUPFAM","id":"SSF47598","properties":[{"key":"EntryName","value":"Ribbon-helix-helix"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASLTIRKLDESLKTYLRLRSAQNGRSVEEEVRVILRALIEPVDPSEPPTHPPEPTALPEVPQPGQAREARVTLIIGGGIAAYKSLDLIRRLKERHIRVRCVLTKAATQFVTELAASALAGDRVFTDLFDARSEFDVGHIRLARDCDLIVVAPATADLMAKMAHGHADDLASAVLLAASRPILLAPAMNPMMWSNPATRRNAATLQRDGIQMIGPNAGEMAEKGEAGVGRMAEPIEIAETVVRLLKPAVPQPLADKRVLITAGPTHEPIDPVRYIANRSSGKQGYAIAAAAQAAGADVRLISGPVELSDPRGVSVTHVESARQMLEAVAAELPADVAIFAAAVADWRVANEGGQKLKKTDKTIPPLQLVENPDILATISKLKEKRPGLVIGFAAETEHLIDNAKAKFARKGCDWIVANDVSPATGVMGGDRNTVHLLTRDADGVHVASWPIMTKDEVATALVAEIAKQLTKPTGPAA","length":477,"molWeight":50919,"crc64":"A8E4FC1881B184C3","md5":"FCF599B62DE6224F07DF29C223BD5256"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":3,"Compositional bias":1,"Binding site":6},"uniParcId":"UPI001E4B4EE0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R5H9","uniProtkbId":"A0ABY3R5H9_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01983.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Sulfate adenylyltransferase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"2.7.7.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"ATP-sulfurylase large subunit"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Sulfate adenylate transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"SAT"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenylyl-sulfate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"2.7.1.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"APS kinase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"ATP adenosine-5'-phosphosulfate 3'-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenosine-5'-phosphosulfate kinase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01983.1"}],"value":"cysC"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"cysN"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01983.1"}],"value":"LQG66_22020"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002357"}],"value":"APS kinase catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024872"}],"value":"Proposed to provide activated sulfate for transfer to Nod factor. ATP sulfurylase may be the GTPase, regulating ATP sulfurylase activity"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049370"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Heterodimer composed of CysD, the smaller subunit, and CysN"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011760"}],"value":"Sulfate-activating enzymes, NodP and NodQ, may be physically associated"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005438"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007237"}],"value":"In the N-terminal section; belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"Tr-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51722"}]},{"type":"Region","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"G1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"G2","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"G3","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"G4","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"G5","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Active site","location":{"start":{"value":544,"modifier":"EXACT"},"end":{"value":544,"modifier":"EXACT"}},"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01983.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"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_00062"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01983.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01983.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01983.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317776.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_22020","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO: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:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) 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:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04166","properties":[{"key":"EntryName","value":"CysN_ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03695","properties":[{"key":"EntryName","value":"CysN_NodQ_II"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04095","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000119","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase subunit 1"},{"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":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00065","properties":[{"key":"EntryName","value":"Adenylyl_sulf_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00062","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_sub1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR041757","properties":[{"key":"EntryName","value":"CysN_GTP-bd"}]},{"database":"InterPro","id":"IPR044138","properties":[{"key":"EntryName","value":"CysN_II"}]},{"database":"InterPro","id":"IPR044139","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"}]},{"database":"InterPro","id":"IPR004161","properties":[{"key":"EntryName","value":"EFTu-like_2"}]},{"database":"InterPro","id":"IPR031157","properties":[{"key":"EntryName","value":"G_TR_CS"}]},{"database":"InterPro","id":"IPR054696","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011779","properties":[{"key":"EntryName","value":"SO4_adenylTrfase_lsu"}]},{"database":"InterPro","id":"IPR000795","properties":[{"key":"EntryName","value":"T_Tr_GTP-bd_dom"}]},{"database":"InterPro","id":"IPR050100","properties":[{"key":"EntryName","value":"TRAFAC_GTPase_members"}]},{"database":"InterPro","id":"IPR009000","properties":[{"key":"EntryName","value":"Transl_B-barrel_sf"}]},{"database":"InterPro","id":"IPR009001","properties":[{"key":"EntryName","value":"Transl_elong_EF1A/Init_IF2_C"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02034","properties":[{"key":"EntryName","value":"CysN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003013","properties":[{"key":"EntryName","value":"PRK03846.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004035","properties":[{"key":"EntryName","value":"PRK05506.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23115","properties":[{"key":"EntryName","value":"TRANSLATION FACTOR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22594","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00009","properties":[{"key":"EntryName","value":"GTP_EFTU"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03144","properties":[{"key":"EntryName","value":"GTP_EFTU_D2"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00315","properties":[{"key":"EntryName","value":"ELONGATNFCT"}]},{"database":"SUPFAM","id":"SSF50465","properties":[{"key":"EntryName","value":"EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF50447","properties":[{"key":"EntryName","value":"Translation proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00301","properties":[{"key":"EntryName","value":"G_TR_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51722","properties":[{"key":"EntryName","value":"G_TR_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVHHAIIGRTPEAAWTYAEDNAHDKPTLRLVTCGSVDDGKSTLVGRLLYDSKMLLDDQLDALASDSKVAGTAGPALDFALLVDGLQAEREQGITIDVAYRFFATRRRRFVVADTPGHVQYTRNMATGASHADLAVVLIDARKGVVSQTRRHSHILALLGVRHVLVAVNKMDLVGFDADRFTTISVAFRTMAEQLGIADVQCVPVAARDGDNVFRTSGRMPWYSGPSVMEHLESVDVADGIEGRPFRFPVQWVNRPNAEFRGFSGRVASGTLRCGDPVVVHPSGRRSRVSGIVTADGRLQQAISGQSVTLLLADEVDASRGDVLTSGTPPMVADHIAAHLIWFDDEAMRPGRRYLLKSGTSSIGAVVSAMKHRVCIDTMAQETALTLEANEIGCVDLVLDRPLVCDAYRDNRDLGSFILIDPFNRRTVAAGLIDAPLRRPANISWQTIDIDKSVRARLKQQKPCVLWLTGLSGAGKSTIANLVDRRLCELGRHTALLDGDNLRHGINRDLGFSPEARVENIRRVTEIAALFVDAGLITLVSLISPFRAERETARRRFATGEFIEVHVATPLAACEARDPKGLYKRARAGELSNFTGIDQPYEAPETPDITIDGAALSADEAAELIVRHLREHHYF","length":635,"molWeight":69424,"crc64":"DEF0C4638527CF1E","md5":"D11C7CEDAD6485F5B8D71AEE8FF6F0CA"},"extraAttributes":{"countByCommentType":{"FUNCTION":4,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":2,"SIMILARITY":4},"countByFeatureType":{"Domain":1,"Region":5,"Active site":1,"Binding site":4},"uniParcId":"UPI001E49A4D2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R5M4","uniProtkbId":"A0ABY3R5M4_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02062.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"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":"UFZ02062.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02062.1"}],"value":"LQG66_22470"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"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":150,"modifier":"EXACT"},"end":{"value":150,"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":153,"modifier":"EXACT"},"end":{"value":153,"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":204,"modifier":"EXACT"},"end":{"value":205,"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":236,"modifier":"EXACT"},"end":{"value":236,"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":258,"modifier":"EXACT"},"end":{"value":260,"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":335,"modifier":"EXACT"},"end":{"value":335,"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":"UP001431010"}],"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":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02062.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ02062.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ02062.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317855.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_22470","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO: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":"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":"MPPTAGLREPSAPLEKIPLETYVPPAKPSLIGLSRAELAAKLGEIGVPAHQQKMRVQQLWHWIYFRGARTFDEMTSVSKDTRTALAEHVTVDRPEVVAEQISNDGTRKWLLRLPSGDDLQKAHEVECVYIPETDRGTLCVSSQVGCTLNCSFCHTGTQRLVRNLTAGEIAGQVMVARDRLNDWADRETPLGNRLITNVVMMGMGEPLYNFDAVRDALLVVSDNEGIGISRRRITLSTSGVVPNIKRAGEEIGVMLAISLHAVRDELRNELVPLNRKYPIAELLQACRDYPGASNARRITFEYVMLKGVNDSLDDARLLVKLLKGIPAKINLIPFNPWPGSAYECSDWEQIEKFSEYVFNAGYSSPVRTPRGRDILAACGQLKSETEKLSARERQALRAMAMTD","length":403,"molWeight":44825,"crc64":"417852CAA3B745F5","md5":"39C8148139961907D3C175F85CFB8D7E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI001E420D76"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R7W8","uniProtkbId":"A0ABY3R7W8_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate dehydrogenase [ubiquinone]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"1.2.5.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate oxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"POX"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate:ubiquinone-8 oxidoreductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"}],"value":"poxB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"}],"value":"LQG66_27900"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ubiquinone + pyruvate + H2O = a ubiquinol + acetate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27405"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:30089"}],"ecNumber":"1.2.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 thiamine pyrophosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362132"}],"value":"Belongs to the TPP enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme N-terminal TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02776"}]},{"type":"Domain","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00205"}]},{"type":"Domain","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":528,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02775"}]},{"type":"Region","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"FAD-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Region","location":{"start":{"value":534,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"Membrane-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"Moves into active site upon enzyme activation, plays a role in electron transfer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03044.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ03044.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231318926.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_27900","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008289","properties":[{"key":"GoTerm","value":"F:lipid 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:0052737","properties":[{"key":"GoTerm","value":"F:pyruvate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048039","properties":[{"key":"GoTerm","value":"F:ubiquinone binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042867","properties":[{"key":"GoTerm","value":"P:pyruvate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02014","properties":[{"key":"EntryName","value":"TPP_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07039","properties":[{"key":"EntryName","value":"TPP_PYR_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1220:FF:000013","properties":[{"key":"EntryName","value":"Pyruvate dehydrogenase [ubiquinone]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1220","properties":[{"key":"EntryName","value":"TPP-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00850","properties":[{"key":"EntryName","value":"POX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR047211","properties":[{"key":"EntryName","value":"POXB-like"}]},{"database":"InterPro","id":"IPR044261","properties":[{"key":"EntryName","value":"Pyruvate_dehydrogenase"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR012000","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_cen_dom"}]},{"database":"InterPro","id":"IPR012001","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_TPP-bd_dom"}]},{"database":"InterPro","id":"IPR011766","properties":[{"key":"EntryName","value":"TPP_enzyme_TPP-bd"}]},{"database":"InterPro","id":"IPR047212","properties":[{"key":"EntryName","value":"TPP_POXB-like"}]},{"database":"InterPro","id":"IPR047210","properties":[{"key":"EntryName","value":"TPP_PYR_POXB-like"}]},{"database":"NCBIfam","id":"NF006591","properties":[{"key":"EntryName","value":"poxB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981:SF2","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02775","properties":[{"key":"EntryName","value":"TPP_enzyme_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00205","properties":[{"key":"EntryName","value":"TPP_enzyme_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02776","properties":[{"key":"EntryName","value":"TPP_enzyme_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTTIADQIVETLEIAGVKRIYGVVGDSLNGLTESLCVRKTIDWVHVRHEEVAAFAASGESQITGALAVCAGSCGPGNLHLINGLYDAQRSRTPVVAIAAQIPSAEIGGGYFQETHPQNLFRECSVYCELVSDPAQMPFVLENAIRAATGERGVAVIVIPGDVALKPAPKRAPSPGLGLMPPKPVVRPAEPELDALAEFLNKASRVTLFCGRGCAGSHAELMRLAEILHSPIVHALGGKEHVEYDNPYDVGLTGFIGFSSGYAAMHSCDALVMLGTDFPYKQFIPSDVGIAQVDIRPSQLGRRARLDVGVVGDVGETLRALLPKLTAKTDRRHLDDNLARYAAARKGLDDLAVGTPGRRPIHPQYLTRLVSERAADDAVFTFDVGTPTIWAARYIAMNGRRRLIGSLVHGSMANAMAQAIGIQAAQVGRQVISLSGDGGFAMLMGDLITLKQEKLPVKVVIYNNGTLGFVALEMKASGFVEYGTDLENPDFAAMARAMGIHARRVEDPGELPGAVADWLAHDGPAVLDVITAKQELSMPPTIGLEQVKGFSVWLIRAVMSGRGDEVIDLAKENLLPR","length":576,"molWeight":61542,"crc64":"D69EB6143FC99692","md5":"00358D1921EEAB55EBE8AEF1056AD937"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":8,"Site":1},"uniParcId":"UPI001E39782D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R8V2","uniProtkbId":"A0ABY3R8V2_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03681.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"Periplasmic nitrate reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"1.9.6.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03681.1"}],"value":"napA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03681.1"}],"value":"LQG66_31455"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055000"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"Catalytic subunit of the periplasmic nitrate reductase complex NapAB. Receives electrons from NapB and catalyzes the reduction of nitrate to nitrite"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 Fe(II)-[cytochrome] + nitrate + 2 H(+) = 2 Fe(III)-[cytochrome] + nitrite + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12909"},{"database":"Rhea","id":"RHEA-COMP:11777"},{"database":"Rhea","id":"RHEA-COMP:11778"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16301"},{"database":"ChEBI","id":"CHEBI:17632"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:29034"}],"ecNumber":"1.9.6.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052176"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mo-bis(molybdopterin guanine dinucleotide)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60539"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) (Mo-bis-MGD) cofactor per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"Binds 1 [4Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"Component of the periplasmic nitrate reductase NapAB complex composed of NapA and NapB"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"Periplasm","id":"SL-0200"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"},{"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":"ARBA","id":"ARBA00008747"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"value":"Belongs to the prokaryotic molybdopterin-containing oxidoreductase family. NasA/NapA/NarB subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":834,"modifier":"EXACT"}},"description":"Periplasmic nitrate reductase","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5046328711"},{"type":"Chain","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":834,"modifier":"EXACT"}},"description":"Periplasmic nitrate reductase","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00648"}],"featureId":"PRO_5048683244"},{"type":"Domain","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"4Fe-4S Mo/W bis-MGD-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51669"}]},{"type":"Binding site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01004"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01004"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01004"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01004"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":514,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":537,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":564,"modifier":"EXACT"},"end":{"value":564,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":724,"modifier":"EXACT"},"end":{"value":733,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":800,"modifier":"EXACT"},"end":{"value":800,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":808,"modifier":"EXACT"},"end":{"value":808,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}},{"type":"Binding site","location":{"start":{"value":825,"modifier":"EXACT"},"end":{"value":825,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60539"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"ligand":{"name":"Mo-bis(molybdopterin guanine dinucleotide)","id":"ChEBI:CHEBI:60539"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"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_01630"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022505"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0500","category":"Ligand","name":"Molybdenum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023063"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0534","category":"Biological process","name":"Nitrate assimilation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022764"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0574","category":"Cellular component","name":"Periplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"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_01630"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01630"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03681.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03681.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ03681.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231319698.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_31455","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009325","properties":[{"key":"GoTerm","value":"C:nitrate reductase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042597","properties":[{"key":"GoTerm","value":"C:periplasmic space"},{"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:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030151","properties":[{"key":"GoTerm","value":"F:molybdenum ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043546","properties":[{"key":"GoTerm","value":"F:molybdopterin cofactor binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050140","properties":[{"key":"GoTerm","value":"F:nitrate reductase (cytochrome) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0045333","properties":[{"key":"GoTerm","value":"P:cellular respiration"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006777","properties":[{"key":"GoTerm","value":"P:Mo-molybdopterin cofactor biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042128","properties":[{"key":"GoTerm","value":"P:nitrate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02791","properties":[{"key":"EntryName","value":"MopB_CT_Nitrate-R-NapA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02754","properties":[{"key":"EntryName","value":"MopB_Nitrate-R-NapA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.40.20:FF:000005","properties":[{"key":"EntryName","value":"Periplasmic nitrate reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.40.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.200.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.740","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.228.10","properties":[{"key":"EntryName","value":"Dimethylsulfoxide Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01630","properties":[{"key":"EntryName","value":"Nitrate_reduct_NapA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009010","properties":[{"key":"EntryName","value":"Asp_de-COase-like_dom_sf"}]},{"database":"InterPro","id":"IPR041957","properties":[{"key":"EntryName","value":"CT_Nitrate-R-NapA-like"}]},{"database":"InterPro","id":"IPR006657","properties":[{"key":"EntryName","value":"MoPterin_dinucl-bd_dom"}]},{"database":"InterPro","id":"IPR006656","properties":[{"key":"EntryName","value":"Mopterin_OxRdtase"}]},{"database":"InterPro","id":"IPR006963","properties":[{"key":"EntryName","value":"Mopterin_OxRdtase_4Fe-4S_dom"}]},{"database":"InterPro","id":"IPR027467","properties":[{"key":"EntryName","value":"MopterinOxRdtase_cofactor_BS"}]},{"database":"InterPro","id":"IPR010051","properties":[{"key":"EntryName","value":"Periplasm_NO3_reductase_lsu"}]},{"database":"InterPro","id":"IPR006311","properties":[{"key":"EntryName","value":"TAT_signal"}]},{"database":"NCBIfam","id":"NF010055","properties":[{"key":"EntryName","value":"napA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01706","properties":[{"key":"EntryName","value":"NAPA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43105:SF11","properties":[{"key":"EntryName","value":"PERIPLASMIC NITRATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43105","properties":[{"key":"EntryName","value":"RESPIRATORY NITRATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04879","properties":[{"key":"EntryName","value":"Molybdop_Fe4S4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00384","properties":[{"key":"EntryName","value":"Molybdopterin"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01568","properties":[{"key":"EntryName","value":"Molydop_binding"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00926","properties":[{"key":"EntryName","value":"Molybdop_Fe4S4"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50692","properties":[{"key":"EntryName","value":"ADC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53706","properties":[{"key":"EntryName","value":"Formate dehydrogenase/DMSO reductase, domains 1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51669","properties":[{"key":"EntryName","value":"4FE4S_MOW_BIS_MGD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00551","properties":[{"key":"EntryName","value":"MOLYBDOPTERIN_PROK_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51318","properties":[{"key":"EntryName","value":"TAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDMKIDRRQMLKLEAAAIAAVAAGMPTPGLAANLVTEREASELKWDKAACRFCGTGCSVMVATKDNRVVATHGDIKSEVNRGLNCVKGYFLSKIMYGHDRLTHPMLRKTNGKYDKNGEFTPISWDEAFDIMASKFKDAMKKRGPSGVGMFGSGQWTVWEGYAALKLFKAGFRTNNIDPNARHCMASAVAGMMRTFGIDEPAGCYDDIEATDAFVLWGSNMAEMHPILWSRVTDRRLSAPHVQVAVLSTFEHRSFDLADIGMIFKPQTDLYLLNAIANHIIKTGRVNKDFVAAHAVFKRGQTDIGYGLRPEHPLEKKATGRTKANDATDISFDEYAKFVSDYTLEMAAEMSGVPLNRLEALADLYADPKTKVVSFWTMGFNQHTRGVWCNNLIYNIHLLTGKIAEAGNSPFSLTGQPSACGTAREVGTFSHRLPADMVVTNKEHRTKAEHIWQLPEGTIPDKPGYHAVLQSRMLKDGLLNAYWVQVNNNLQAGPNANEETYPGFRNPDNFIVVSDAYPSVTALAADLILPTAMWVEKEGAYGNAERRTQFWHQLVSAPGEARSDLWQLMEFSKRFKIEEVWPEELIAKKPDVRGKTLFDVLYKNGQVDKFPLDQIEPGYANDESKAFGFYVHKGLFEEYASFGRGHGHDLAPFEAYHKERGLRWPVVDGKETRWRFREGSDPYVKAGTGVQFYGFADGKARIFALPYEPPAESPDKDYPFWLSTGRVVEHWHSGTMTRRVPELYKAFPEAVCFMHPDDAEAASLRRGDEVKVASRRGFIRARVETRGRDKPPRGLVFVPWFDESKLINKVTLDATDPISLQTDYKKCAVRIERV","length":834,"molWeight":93666,"crc64":"2A8D2DB023E052F4","md5":"283BA38295F27B2300A18788C3FC2982"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":2,"Domain":1,"Binding site":21},"uniParcId":"UPI001E41410A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R9P4","uniProtkbId":"A0ABY3R9P4_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03934.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"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":"UFZ03934.1"}],"value":"LQG66_32865"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":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":107,"modifier":"EXACT"},"end":{"value":113,"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":149,"modifier":"EXACT"},"end":{"value":150,"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":176,"modifier":"EXACT"},"end":{"value":176,"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":182,"modifier":"EXACT"},"end":{"value":182,"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":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":455,"modifier":"EXACT"},"end":{"value":455,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"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":"UFZ03934.1"}],"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":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03934.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03934.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ03934.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231319947.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_32865","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKLHDLLGDEAGLDPQIAAVEVSGLAVDSRAVRPGDLFFALAGTRTDGARFIEAAIAAGAVVVAGAAAPATDLPVPFVVLPNARRALALAASRFFPRQPATIAAVTGTSGKTSVAAFTRQIWQMLGHSSASIGTIGLVSDKRTVYGSLTTPDPIALHRQIDEITQDGVTHLAFEASSHGLDQFRLDGVRVSAGGFTNLSRDHMDYHPDIAHYLNAKLRLFRDLVPPGGAAVISADHDCSAEVIAAAKARGLRLMTVGARGDGIGEGIRLVATAVSGFAQQLEVQHCGRMHALRLPLVGAFQIENALVAAGLAIGTGSDPQAVFESLEKLEGAKGRLELVGEHNGAPVFIDYSHKPDALAKALQALRPYAARKLAVVFGAGGDRDAGKRPLMGAIASAEADSVIVTDDNPRSEDPAAIRAAILAAAPGAREIGDRAEAIRVAIGELQPGDALVIAGKGHETGQIIGSTVLHFSDHEAVADALASRTS","length":486,"molWeight":50334,"crc64":"00D9138BB174D4D8","md5":"3710E1AEC36B54E899A115C7DCE4C2FD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI001E364B55"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RA12","uniProtkbId":"A0ABY3RA12_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03794.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00876"}],"value":"Transaldolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00876"}],"value":"2.2.1.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"value":"tal"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"pgi"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03794.1"}],"value":"LQG66_32080"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"value":"Transaldolase involved in the non-oxidative phase in the pentose phosphate pathway. Catalyzes the reversible conversion of sedoheptulose-7-phosphate and D-glyceraldehyde 3-phosphate into erythrose-4-phosphate and beta-D-fructose 6-phosphate. Transaldolase is important for the balance of metabolites in the pentose-phosphate pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-erythrose 4-phosphate + beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17053"},{"database":"ChEBI","id":"CHEBI:16897"},{"database":"ChEBI","id":"CHEBI:57483"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"2.2.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10019"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"value":"Carbohydrate degradation; pentose phosphate pathway; D-glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D-ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative stage): step 2/3"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Belongs to the GPI family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008426"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"value":"Belongs to the transaldolase family. Type 2 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}]},{"type":"Active site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10019"}]},{"type":"Active site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Nucleophile; Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}]},{"type":"Active site","location":{"start":{"value":660,"modifier":"EXACT"},"end":{"value":660,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":759,"modifier":"EXACT"},"end":{"value":759,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}},{"type":"Binding site","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:61527"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"ligand":{"name":"D-fructose 6-phosphate","id":"ChEBI:CHEBI:61527"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023126"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"id":"KW-0570","category":"Biological process","name":"Pentose shunt"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03794.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ03794.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ03794.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231319808.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_32080","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004347","properties":[{"key":"GoTerm","value":"F:glucose-6-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004801","properties":[{"key":"GoTerm","value":"F:transaldolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006098","properties":[{"key":"GoTerm","value":"P:pentose-phosphate shunt"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05015","properties":[{"key":"EntryName","value":"SIS_PGI_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05798","properties":[{"key":"EntryName","value":"SIS_TAL_PGI"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00955","properties":[{"key":"EntryName","value":"Transaldolase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10490","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase like protein, domain 1"},{"key":"MatchStatus","value":"3"}]},{"database":"HAMAP","id":"MF_00493","properties":[{"key":"EntryName","value":"Transaldolase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR001672","properties":[{"key":"EntryName","value":"G6P_Isomerase"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"InterPro","id":"IPR035476","properties":[{"key":"EntryName","value":"SIS_PGI_1"}]},{"database":"InterPro","id":"IPR001585","properties":[{"key":"EntryName","value":"TAL/FSA"}]},{"database":"InterPro","id":"IPR004732","properties":[{"key":"EntryName","value":"Transaldolase_2"}]},{"database":"InterPro","id":"IPR018225","properties":[{"key":"EntryName","value":"Transaldolase_AS"}]},{"database":"NCBIfam","id":"NF002881","properties":[{"key":"EntryName","value":"PRK03343.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF007080","properties":[{"key":"EntryName","value":"PRK09533.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00876","properties":[{"key":"EntryName","value":"tal_mycobact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10683","properties":[{"key":"EntryName","value":"TRANSALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10683:SF31","properties":[{"key":"EntryName","value":"TRANSALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00342","properties":[{"key":"EntryName","value":"PGI"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00923","properties":[{"key":"EntryName","value":"TAL_FSA"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00662","properties":[{"key":"EntryName","value":"G6PISOMERASE"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51463","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01054","properties":[{"key":"EntryName","value":"TRANSALDOLASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00958","properties":[{"key":"EntryName","value":"TRANSALDOLASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNPVKALEEHGQAVWLDFLARGFVAKGDLKRLIDEDGVKGVTSNPAIFEKAIGSSDEYDAPIAKALKSGDRSPTQLFEAVAVEDIQNAADVLRTVYDRFDGNDGFVSLEVSPYLAMDTDGTTTEAEQLWKAVDRKNLMIKVPATDAGLPAIRHLISRGISVNITLLFSQDVYRQVAEAYLAGLEAYVAGGGDPSHIASVASFFVSRIDSVVDKQLDEKIAQANDPSEKERLAALKGKIAIANAKMAYQDYKQLFSGDRWERLAAKGARPQRLLWASTGTKNKDYSDVLYVEELIGPNTVNTVPPATLDAFRDHGKARDSLEEDVEAARAALDDLAKTGISLDEITADLVIDGVKQFADAADKLYGAVAYKRATVLGIELGQQTIAPGAPLEKKIAAATEEWRKAAKIRRLWHKDATVWTGRDEHKWLGWLTSATKADVADYEDYAQRVKGQKFSDAVVLGMGGSSLGPEVLAETFPRKTGFPKLHVLDSTDPAQVRAMEKTIDISRTVFIVSSKSGGTTEPNAMKDYFFARVSEAIGASKAGHRFIAVTDPGSSLEKAAQRQGFARIFHGDPTIGGRYSVLSPFGLVPAATAGIDVRRLITNALSMVRSCGPDVPPLQNPGVQLGLVMGLAGLEGRDKVTVFASPKVADFGAWAEQLIAESTGKEGKGLIPIDGEPIGDPSTYGSDRFFIDIRVEGDDVAHHDAKLAALEEAGHPVVRIVMSSIDQLGQEFFRFEMATAVAGAVLGINPFDQPDVEAAKIKTRELTAAFEQTGALPAEEPVVSIKDCELYTDAHNAESLREHGANGTLASWLKAHLGRTDEGDYVALLGYIERNSGNIDALQRIRLKLRDAKHLATCAEFGPRFLHSTGQAYKGGPDSGVFLQITADDADDLPIPGQKASFGVIKAAQARGDFDVLTERGRRALRVHLKGNLKSGLKMLDSAITEALS","length":948,"molWeight":102253,"crc64":"56F67BDE4CB292B6","md5":"EC58EB36B50F826F030B27047CCE8A23"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":6},"uniParcId":"UPI001E312FF1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RAZ6","uniProtkbId":"A0ABY3RAZ6_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ04386.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Bifunctional protein HldE"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 7-phosphate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"2.7.1.167"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 7-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-glycero-beta-D-manno-heptose-7-phosphate kinase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 1-phosphate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"2.7.7.70"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ04386.1"}],"value":"rfaE1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"hldE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ04386.1"}],"value":"LQG66_35260"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003753"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002319"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) = ADP-D-glycero-beta-D-manno-heptose + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27465"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:59967"},{"database":"ChEBI","id":"CHEBI:61593"}],"ecNumber":"2.7.7.70","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glycero-beta-D-manno-heptose 7-phosphate + ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27473"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:60204"},{"database":"ChEBI","id":"CHEBI:60208"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.167","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004713"}],"value":"Bacterial outer membrane biogenesis; LPS core biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"In the C-terminal section; belongs to the cytidylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"In the N-terminal section; belongs to the carbohydrate kinase PfkB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Domain","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"Cytidyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01467"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"Ribokinase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Region","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"Cytidylyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Active site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"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_01603"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ04386.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ04386.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ04386.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231320630.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_35260","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033785","properties":[{"key":"GoTerm","value":"F:heptose 7-phosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033786","properties":[{"key":"GoTerm","value":"F:heptose-1-phosphate adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016773","properties":[{"key":"GoTerm","value":"F:phosphotransferase activity, alcohol group as acceptor"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01172","properties":[{"key":"EntryName","value":"RfaE_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01603","properties":[{"key":"EntryName","value":"HldE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023030","properties":[{"key":"EntryName","value":"Bifunc_HldE"}]},{"database":"InterPro","id":"IPR002173","properties":[{"key":"EntryName","value":"Carboh/pur_kinase_PfkB_CS"}]},{"database":"InterPro","id":"IPR004821","properties":[{"key":"EntryName","value":"Cyt_trans-like"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR011913","properties":[{"key":"EntryName","value":"RfaE_dom_I"}]},{"database":"InterPro","id":"IPR011914","properties":[{"key":"EntryName","value":"RfaE_dom_II"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR00125","properties":[{"key":"EntryName","value":"cyt_tran_rel"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02198","properties":[{"key":"EntryName","value":"rfaE_dom_I"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02199","properties":[{"key":"EntryName","value":"rfaE_dom_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46969","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN HLDE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46969:SF1","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN HLDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01467","properties":[{"key":"EntryName","value":"CTP_transf_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00583","properties":[{"key":"EntryName","value":"PFKB_KINASES_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFDFDDLSQAIARQTVLCVGDLMLDEFVYGEVSRISPEAPAPVIAVQRSETNIGGAGNVARNIAALGARCIFVGLVGHDAAGDQLEVELAREAGIESVLVRDPSRPTTRKVRFVSEHFSTHMLRADWERAAPAAADIEQKLIEKILPLLDRADIVLLSDYAKGVLTTRVIRNVIDAARKAGKRVIVDPKSANFAIYRGATLLTPNRKEFSEATRSRAETEQEIASAAQDAIYLADCEAILVTQSERGMTLVPRQGDPIHVPAYPVKVSDVSGAGDTVVAVLAATLAAGAAWEDSLRMASAAAAVAVGKQGTASVTSAELRQKILPHAYLAAEEKIIANDDELLARVAAWRRDGLRVGFTNGCFDILHPGHVKVLTAARAACDRLVVGLNSDTSVKRLKGESRPVQDERARAEVLAALEAVDLVAIFAEDTPLRLIELIRPSVLVKGGDYTREQVVGHEVVEAGGGEVILIDILQGHSTTALVDRARSDGQ","length":490,"molWeight":52475,"crc64":"CBF3C405D546BFCB","md5":"E1CA745E5CC169695E0670008E69B22F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":1},"uniParcId":"UPI001E53C859"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RFM6","uniProtkbId":"A0ABY3RFM6_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05633.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"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":"UFZ05633.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05633.1"}],"value":"LQG66_04780"}]}],"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:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":14,"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":25,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"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":83,"modifier":"EXACT"},"end":{"value":84,"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":108,"modifier":"EXACT"},"end":{"value":108,"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":144,"modifier":"EXACT"},"end":{"value":144,"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":158,"modifier":"EXACT"},"end":{"value":158,"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":173,"modifier":"EXACT"},"end":{"value":173,"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":230,"modifier":"EXACT"},"end":{"value":230,"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":230,"modifier":"EXACT"},"end":{"value":230,"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":319,"modifier":"EXACT"},"end":{"value":319,"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":337,"modifier":"EXACT"},"end":{"value":337,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":363,"modifier":"EXACT"},"end":{"value":363,"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: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":372,"modifier":"EXACT"},"end":{"value":373,"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":409,"modifier":"EXACT"},"end":{"value":409,"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":426,"modifier":"EXACT"},"end":{"value":426,"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":"UP001431010"}],"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":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05633.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05633.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ05633.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231323946.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_04780","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR018357","properties":[{"key":"EntryName","value":"Hexapep_transf_CS"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010933","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00101","properties":[{"key":"EntryName","value":"HEXAPEP_TRANSFERASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTARSSLTIVLAAGEGTRMRTSLPKVLHPIAGESLLAHVLAAAPKGEGAGIAVVVGPDHQAVERETKRLRPEADIFVQRERLGTAHAVLAARQAIARGADDLLVAFGDTPLISAETFARLRAALAQGAALAVLGFRAADPTGYGRLLMDGARLVAIREQADASEAERAITLCNAGVMAMDGRHALAILDKIGNANKKGEYYLVDAVAIARELGLEAVVIETSEDEVRGINTKAQLAEAEAVMQNRLRRAAMDAGVTLIAPETVYLAADTKFGTDVTIEPFVVIGPGVSIGDGAVIHSFSHIVQSTLGRNTQLGPYARLRPGTSLGDGAKIGNFVEAKAAVLEAGVKVNHLSYIGDAHVGANSNIGAGTITCNYDGFSKHKTTIGEGAFIGTNTSLVAPIKIGARAYIGSGSVITRDVPDDALALERSPQTTREGAAARFRNAKSRHKK","length":448,"molWeight":46812,"crc64":"DC3DDAAD61AF110F","md5":"528A2B0B0507248A22023A849AB5AD89"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":4,"Active site":1,"Binding site":18},"uniParcId":"UPI001E50E5F3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RFY9","uniProtkbId":"A0ABY3RFY9_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05972.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"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":"UFZ05972.1"}],"value":"LQG66_06585"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":302,"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":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":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":54,"modifier":"EXACT"},"end":{"value":54,"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":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":238,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05972.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05972.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ05972.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231324611.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_06585","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"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":"MARYIFITGGVVSSLGKGLASAALGALLQARGYKVRLRKLDPYLNLDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFTGRPATKADNITTGRIYQDILTKERRGDYLGATIQVVPHVTNAIKDFVLSGNDEYDFVLVEIGGTVGDIEGLPFFEAIRQLKNELPRDHAIYIHLTLLPYIPSAGELKTKPTQHSVKELRSIGIQPDILLCRTDRAIPKEERRKLGLFCNVRESAVIEARDVDNIYAVPEAYHAAGLDDEVLASFGIEPRVPPALASWHTINERVRNPEGDVTIAIVGKYTGMKDAYKSLIEALSHGGIANKVRVKLDWIESEVFENEDPAPFLEHVNGILVPGGFGQRGAEGKIRAAQFARERDVPYFGICFGMQMAVIEAARNLVGISGANSTEFGPTPEPLVGLMTEWLRGNELEKRSKSGDLGGTMRLGAYPAALKRGSRVSDVYGGATEISERHRHRYEVNTAYKDRLEQHGLKFSGLSPDGVLPEIVEYEDHPWFIGVQFHPELKSRPFEPHPLFASFIQAAMVQSRLV","length":543,"molWeight":60059,"crc64":"DD2DDDF31897D89B","md5":"FA9293AB00E498D823253FE7BD7ED6F3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":17},"uniParcId":"UPI001E34B064"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RGE0","uniProtkbId":"A0ABY3RGE0_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05778.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme IspD/IspF"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2.7.7.60"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4-diphosphocytidyl-2C-methyl-D-erythritol synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MEP cytidylyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MCT"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECDP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4.6.1.12"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"ispDF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05778.1"}],"value":"LQG66_05555"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13429"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:57823"},{"database":"ChEBI","id":"CHEBI:58262"}],"ecNumber":"2.7.7.60","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001282"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23864"},{"database":"ChEBI","id":"CHEBI:57919"},{"database":"ChEBI","id":"CHEBI:58483"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"4.6.1.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000200"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001968"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004787"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004709"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009789"}],"value":"Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008480"}],"value":"Belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the C-terminal section; belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02542"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Region","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":372,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0414","category":"Biological process","name":"Isoprene biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05778.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ05778.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ05778.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231324272.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_05555","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0008685","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050518","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019288","properties":[{"key":"GoTerm","value":"P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016114","properties":[{"key":"GoTerm","value":"P:terpenoid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02516","properties":[{"key":"EntryName","value":"CDP-ME_synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00554","properties":[{"key":"EntryName","value":"MECDP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.550.10:FF:000003","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1330.50","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00108","properties":[{"key":"EntryName","value":"IspD"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01520","properties":[{"key":"EntryName","value":"IspDF"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00107","properties":[{"key":"EntryName","value":"IspF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001228","properties":[{"key":"EntryName","value":"IspD"}]},{"database":"InterPro","id":"IPR026596","properties":[{"key":"EntryName","value":"IspD/F"}]},{"database":"InterPro","id":"IPR034683","properties":[{"key":"EntryName","value":"IspD/TarI"}]},{"database":"InterPro","id":"IPR018294","properties":[{"key":"EntryName","value":"ISPD_synthase_CS"}]},{"database":"InterPro","id":"IPR003526","properties":[{"key":"EntryName","value":"MECDP_synthase"}]},{"database":"InterPro","id":"IPR020555","properties":[{"key":"EntryName","value":"MECDP_synthase_CS"}]},{"database":"InterPro","id":"IPR036571","properties":[{"key":"EntryName","value":"MECDP_synthase_sf"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"NCBIfam","id":"TIGR00453","properties":[{"key":"EntryName","value":"ispD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00151","properties":[{"key":"EntryName","value":"ispF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006899","properties":[{"key":"EntryName","value":"PRK09382.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181:SF1","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01128","properties":[{"key":"EntryName","value":"IspD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02542","properties":[{"key":"EntryName","value":"YgbB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69765","properties":[{"key":"EntryName","value":"IpsF-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01295","properties":[{"key":"EntryName","value":"ISPD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01350","properties":[{"key":"EntryName","value":"ISPF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTSQRTAAILVAAGRGLRAGAGGPKQYRTIGGRTVIHRALAAFADHPEVAVVQPVVNPDDIDVFNAAVSGLRHEAPAHGGATRQASVLAGLEALVPQRPDIVLIHDAARAFVTPAVISRAIQAVGKTGAAIPVVPVTDTIKEVTAGGDITATPERARLRIAQTPQTFKFEVILEAHRRAAREGLTEFTDDAAIAEWAGLTVATFEGDVANMKLTTPEDFVREEARLAAELGDIRTGTGYDVHAFGEGDHVWLCGLRVPHSRGFLAHSDGDVGLHALVDAILGALADGDIGSHFPPSDMKWKGAASDQFLKYAIERVTARGGRIANLEVTMICERPKIGPLRDQMRARIAEISGVDISRIAVKATTSERLGFTGREEGIAATASATIRLPWSA","length":393,"molWeight":41605,"crc64":"B7E6CE048D6E72B6","md5":"4EAAE78DC60B54B585758A5722DF3BC4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":9,"Site":6},"uniParcId":"UPI001E412CCA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RGX1","uniProtkbId":"A0ABY3RGX1_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ06071.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"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":"UFZ06071.1"}],"value":"LQG66_07140"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":59,"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":56,"modifier":"EXACT"},"end":{"value":56,"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":116,"modifier":"EXACT"},"end":{"value":116,"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":120,"modifier":"EXACT"},"end":{"value":126,"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":149,"modifier":"EXACT"},"end":{"value":149,"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":152,"modifier":"EXACT"},"end":{"value":152,"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":251,"modifier":"EXACT"},"end":{"value":251,"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":314,"modifier":"EXACT"},"end":{"value":314,"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":369,"modifier":"EXACT"},"end":{"value":369,"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":407,"modifier":"EXACT"},"end":{"value":411,"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":436,"modifier":"EXACT"},"end":{"value":436,"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":437,"modifier":"EXACT"},"end":{"value":437,"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":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ06071.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ06071.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ06071.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231324823.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_07140","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"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":"MEVLTTSEMERADRLTIAAGTPGFSLMLSAGQAVAAAAMDLVEEGPILVVCGPGNNGGDGFVAAAELAAQGREVSVILMCERDALQGDAASAARGWKFPVLPFTPQAIGRPALIIDALFGAGLSRPITGEPHDVIAAVNANGAPVLAVDLPSGINGTTAAVMGIAVRATETVTFFRKKPAHLLLPGRQHCGRVVLADIGIDPQVLGEIRPHVFENEPELWHGRFPVPVIDGHKYARGHVLTVSGDMTATGAARMAARAALRAGAGLVTLASPRDALVVNAAALTAVMLRPTDTAIEFGELLGDHRYNTCIIGPGAGVGERTRDFVFTALSAQRHLVLDADALTSFADAPERLFEQIRATPEAQIVLTPHEGEFPRLFSDLSNKHPGRSKLERVRDAAARCGAVVLLKGADTTVAAPDGRAAIAANAPPWLATAGAGDVLAGIIAGLLAQGVPAFEAACIGVWMHGEAGAEAGPGLIAEDLTETMPAVFRRLYDRLGIEY","length":499,"molWeight":51873,"crc64":"9E69656AC199897D","md5":"B700E65BA5DFA34AB9A6A2F86058E167"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI001E40A62E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RHA8","uniProtkbId":"A0ABY3RHA8_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ06142.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine hydroxymethyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"SHMT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"2.1.2.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"glyA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ06142.1"}],"value":"LQG66_07530"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057572"}],"value":"Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = 2-methylserine + (6S)-5,6,7,8-tetrahydrofolate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:58275"}],"ecNumber":"2.1.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051216"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15481"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57453"}],"ecNumber":"2.1.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006376"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Belongs to the SHMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":397,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"Plays an important role in substrate specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]},{"type":"Modified residue","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ06142.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ06142.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ06142.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231324963.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_07530","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050413","properties":[{"key":"GoTerm","value":"F:D-alanine 2-hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00378","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000001","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000003","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00051","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"InterPro","id":"IPR001085","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase"}]},{"database":"InterPro","id":"IPR049943","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase-like"}]},{"database":"InterPro","id":"IPR019798","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase_PLP_BS"}]},{"database":"InterPro","id":"IPR039429","properties":[{"key":"EntryName","value":"SHMT-like_dom"}]},{"database":"NCBIfam","id":"NF000586","properties":[{"key":"EntryName","value":"PRK00011.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680:SF35","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00464","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000412","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00096","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTASSAKPASSVDSFFSATLAEADPEIAAAIKGELGRQRHEIELIASENIVSRAVLEAQGSVMTNKYAEGYPGARYYGGCEWVDVAENLAIDRAKKLFGANFANVQPNSGSQMNQAVFLALLQPGDTFMGLDLAAGGHLTHGSPVNMSGKWFKASHYTVRREDQLIDMDAVASQAEQVKPKLIIAGGSAYSRPWDFKRFREIADHVGAYFLVDMAHFAGLVAGGVHASPLPHAHVVTTTTHKSLRGPRGGLILWNDEQFTKKLNSAIFPGLQGGPLMHVIAAKAVAFAEALRPEFKTYAKNIVENAKALAESLRAQGFDIVSGGTDNHLMLVDLRPKALKGNVSEKALVRAGITCNKNGIPFDPEKPFVTSGLRLGTPAATTRGFGVAEFQQVGGLIAEVLNAIAQAPDGSAPLVEAAVKEKVKALTDRFPIYQ","length":434,"molWeight":46348,"crc64":"16230D34C2D70303","md5":"A109823129E08FA717F6D409C698FDFE"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":1,"Modified residue":1},"uniParcId":"UPI001E605CB8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RHQ0","uniProtkbId":"A0ABY3RHQ0_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07015.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"ATP-dependent dethiobiotin synthetase BioD"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"6.3.3.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"DTB synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"DTBS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"Dethiobiotin synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07015.1"}],"value":"bioD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07015.1"}],"value":"LQG66_12240"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"Catalyzes a mechanistically unusual reaction, the ATP-dependent insertion of CO2 between the N7 and N8 nitrogen atoms of 7,8-diaminopelargonic acid (DAPA, also called 7,8-diammoniononanoate) to form a ureido ring"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(7R,8S)-7,8-diammoniononanoate + CO2 + ATP = (4R,5S)-dethiobiotin + ADP + phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15805"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:149469"},{"database":"ChEBI","id":"CHEBI:149473"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.3.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(7R,8S)-8-amino-7-(carboxyamino)nonanoate + ATP = (4R,5S)-dethiobiotin + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:63684"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:149470"},{"database":"ChEBI","id":"CHEBI:149473"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047386"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"Cofactor biosynthesis; biotin biosynthesis; biotin from 7,8-diaminononanoate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"Belongs to the dethiobiotin synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"ATP-dependent dethiobiotin synthetase BioD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5050324156"},{"type":"Active site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":18,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Lipidation","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022756"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"id":"KW-0093","category":"Biological process","name":"Biotin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"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"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00336"}],"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:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07015.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07015.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ07015.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231326468.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_12240","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004141","properties":[{"key":"GoTerm","value":"F:dethiobiotin synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009102","properties":[{"key":"GoTerm","value":"P:biotin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03109","properties":[{"key":"EntryName","value":"DTBS"},{"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_00336","properties":[{"key":"EntryName","value":"BioD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004472","properties":[{"key":"EntryName","value":"DTB_synth_BioD"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR00347","properties":[{"key":"EntryName","value":"bioD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43210:SF2","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DETHIOBIOTIN SYNTHETASE BIOD 2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43210","properties":[{"key":"EntryName","value":"DETHIOBIOTIN SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13500","properties":[{"key":"EntryName","value":"AAA_26"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006755","properties":[{"key":"EntryName","value":"DTB_synth"},{"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":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAQRIVVTGTDTGIGKTVFAAGLTALLGACYWKPVQAGLAEETDSRRVQRLAELPDDRVIPEAYRLAEPASPHLAARLEGIRIDPPGLDPPDAGGRPVVIEGAGGVMVPLDSDTLYLDVFTRWRFPVVLCARTSLGTINHSLLSLEALRSRGIDVLGIAFIGDANPDSEETICRLGGVRRLGRLPWLSPLTARSLQQAFVAQFRRTDFDR","length":210,"molWeight":22769,"crc64":"1A851E6ACA6F369E","md5":"CBBDD413C71F6966B4FC88DBC1C9B9E9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Active site":1,"Binding site":7,"Lipidation":2},"uniParcId":"UPI001E5F1602"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RLA3","uniProtkbId":"A0ABY3RLA3_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07665.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07665.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07665.1"}],"value":"LQG66_15745"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Region","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"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_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-90)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07665.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ07665.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ07665.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231327115.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_15745","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.520.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF0","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDDVSKCPFSGGLKGFSNKDWWPNQLNLSILHQHSKLTDPLGEAFDYTKEFKSLDLDALVKDLHALMTDSQDWWPADFGHYGPLFIRMAWHAAGTYRIGDGRGGAGAGQQRFAPLNSWPDNANLDKARRLLWPIKQKYGQKISWADLFVLTGNVALESMGFKTFGFGGGRADTWEPEQDIYWGPEGKWLADERYSGDRELAGSLAAVQMGLIYVNPEGPNGNPDPLASARDIRETFARMAMDDEETVALIAGGHTFGKTHGAGDASLVGAEPEGADIAQQGLGWASKYASGKGGDAITSGLEVIWTTTPTKWSNNFFWNLFGYEWELTKSPAGAHQWKPKHGAGADTVPDAHDKSKRHAPSMLTTDLALRMDPAYEKISRRFLENPDQFADAFARAWFKLTHRDMGPKVRYLGPLVPKEELIWQDPLPPVDHPLVDDKDVAALKAKILASGLSVSQLVSTAWASASTFRGSDKRGGANGARIRLAPQKDWAVNNPAELAKVLSSLEGIQTEFNTAAAGGKKISLADLIVLAGNAGVEAAAKKAGVEVTVPFAPGRTDASQEQTDVESFAVLEPTHDGFRNYISGKQFLSAEELLVDKAQLLTLSAPELTVLVGGLRVLGANANGAKHGVFTAQTETLSNDFFANLLDMGVVWRPVDQGEHTFEGRDRKSGAVKWTATRADLIFGSHAQLRALAEVYASSDAKQKFVKDFVAAWTKVTNLDRFELKA","length":726,"molWeight":79083,"crc64":"564C7C9C88939E53","md5":"61D752193A3F785EF1835507BE7C58B2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI001E2AB50E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3RN94","uniProtkbId":"A0ABY3RN94_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ08133.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"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":"UFZ08133.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ08133.1"}],"value":"LQG66_18385"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1154,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5049503408"},{"type":"Domain","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":739,"modifier":"EXACT"},"end":{"value":951,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1017,"modifier":"EXACT"},"end":{"value":1154,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":1017,"modifier":"EXACT"},"end":{"value":1154,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"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":219,"modifier":"EXACT"},"end":{"value":219,"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":225,"modifier":"EXACT"},"end":{"value":225,"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":226,"modifier":"EXACT"},"end":{"value":226,"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":258,"modifier":"EXACT"},"end":{"value":258,"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":260,"modifier":"EXACT"},"end":{"value":260,"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":265,"modifier":"EXACT"},"end":{"value":265,"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":291,"modifier":"EXACT"},"end":{"value":291,"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":292,"modifier":"EXACT"},"end":{"value":292,"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":293,"modifier":"EXACT"},"end":{"value":293,"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":335,"modifier":"EXACT"},"end":{"value":335,"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":335,"modifier":"EXACT"},"end":{"value":335,"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":335,"modifier":"EXACT"},"end":{"value":335,"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":349,"modifier":"EXACT"},"end":{"value":349,"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":349,"modifier":"EXACT"},"end":{"value":349,"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":349,"modifier":"EXACT"},"end":{"value":349,"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":349,"modifier":"EXACT"},"end":{"value":349,"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":349,"modifier":"EXACT"},"end":{"value":349,"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":351,"modifier":"EXACT"},"end":{"value":351,"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":351,"modifier":"EXACT"},"end":{"value":351,"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":775,"modifier":"EXACT"},"end":{"value":775,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":837,"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":842,"modifier":"EXACT"},"end":{"value":842,"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":867,"modifier":"EXACT"},"end":{"value":867,"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":868,"modifier":"EXACT"},"end":{"value":868,"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":869,"modifier":"EXACT"},"end":{"value":869,"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":870,"modifier":"EXACT"},"end":{"value":870,"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":910,"modifier":"EXACT"},"end":{"value":910,"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":910,"modifier":"EXACT"},"end":{"value":910,"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":910,"modifier":"EXACT"},"end":{"value":910,"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":922,"modifier":"EXACT"},"end":{"value":922,"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":922,"modifier":"EXACT"},"end":{"value":922,"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":922,"modifier":"EXACT"},"end":{"value":922,"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":922,"modifier":"EXACT"},"end":{"value":922,"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":922,"modifier":"EXACT"},"end":{"value":922,"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":924,"modifier":"EXACT"},"end":{"value":924,"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":924,"modifier":"EXACT"},"end":{"value":924,"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":"UP001431010"}],"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":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ08133.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ08133.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ08133.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231327582.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_18385","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"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":"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":"MPKRTDISTILIIGAGPIVIGQACEFDYSGTQAVKALKEEGYRVVLVNSNPATIMTDPELADATYIEPITPEIVARIIEKERHVIPGGFALLPTMGGQTALNCALSLRRQGTLEKFDVEMIGATADAIDKAEDRQLFRNAMEKIGLQTPKSRLANASALKKQYRDKYHAERDKLAGAERDELDRQWTLGENERRKRYQEHALGQALMALSEIGLPAIIRPSFTMGGTGGGIAYNKEEYLDIIERGLDASPTNEVLIEESVLGWKEYEMEVVRDKKDNCIIVCSIENLDPMGVHTGDSITVAPALTLTDKEYQIMRDASLAVLREIGVETGGSNVQFGVNPADGRMVVIEMNPRVSRSSALASKATGFPIAKVAAKLAIGYTLDEIANDITGGATPASFEPTIDYVVTKIPRFAFEKFPGASTTLTTSMKSVGEVMAIGRTFQESLQKALRGLETGLTGLDEIEIDGLGRGDDKNAIRAALGTPTPNRLLQVAQAMRLGWSDEEIFNSCKIDRWFLSQMRSIVEMEDKVRRYGLPPNATGMRTLKAMGFSDARLAVLANTTEAEIAAQRHALGVRPAFKRIDTCAAEFASPTAYMYSSYETPFAGNLADESAPSDKKKVIILGGGPNRIGQGIEFDYCCCHACFALADAGYETIMINCNPETVSTDYDTADRLYFEPLTAEDVLEIIATERKNGTVHGVIVQFGGQTPLKLARALEAADVPILGTSPEAIDLAEDRDRFKRILDKLRLKQPKNGIAYSVEQARLVAADLGLPLVVRPSYVLGGRAMQIIREDNQLGDYLLGTLPELVPADVKARYPNDKTGQINTVLGKNPLLFDRYLSDATEIDVDCLSDGKDTFIVGIMEHIEEAGIHSGDSACSLPPHSLDEATIAELERQTRELALGLDVVGLMNVQYAIKDGTIYVLEVNPRASRTVPFVAKVVGTPVAKIAARIMAGEKLADFGLKKRNLKHVGVKESVFPFARFPGVDTVLGPEMRSTGEVMGIDRSFAVAFAKSQLGGGTRVPRKGTVFVSVRESDKARITEVVRMLHALGFKVVATSGTQRFLTDQGVPTEKINKVLEGRPHIVDAITNGDIQLVFNTTEGPQALADSRSLRRAALLHKVPYYTTLSGAVAAAQGIRAYLGGDLEVRTLQSYFSEN","length":1154,"molWeight":125576,"crc64":"FE57FD31DBA0D596","md5":"45E2A83548E6B03BE7F669F12366F7A0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":1,"Domain":3,"Region":2,"Binding site":38,"Lipidation":2},"uniParcId":"UPI001E317500"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R1X4","uniProtkbId":"A0ABY3R1X4_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01373.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"N5-carboxyaminoimidazole ribonucleotide synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"N5-CAIR synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"6.3.4.18"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"5-(carboxyamino)imidazole ribonucleotide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"purK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01373.1"}],"value":"LQG66_18745"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"value":"Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)(-) to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"Catalyzes the ATP-dependent conversion of 5-aminoimidazole ribonucleotide (AIR) and HCO(3)- to N5-carboxyaminoimidazole ribonucleotide (N5-CAIR)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-amino-1-(5-phospho-beta-D-ribosyl)imidazole + hydrogencarbonate + ATP = 5-carboxyamino-1-(5-phospho-D-ribosyl)imidazole + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19317"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58730"},{"database":"ChEBI","id":"CHEBI:137981"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.18","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5-amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361200"}],"value":"Belongs to the PurK/PurT family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01928"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01373.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01373.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01373.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317171.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_18745","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034028","properties":[{"key":"GoTerm","value":"F:5-(carboxyamino)imidazole ribonucleotide synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004638","properties":[{"key":"GoTerm","value":"F:phosphoribosylaminoimidazole carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.30.1490.20:FF:000015","properties":[{"key":"EntryName","value":"N5-carboxyaminoimidazole ribonucleotide synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000029","properties":[{"key":"EntryName","value":"N5-carboxyaminoimidazole ribonucleotide synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000016","properties":[{"key":"EntryName","value":"N5-carboxyaminoimidazole ribonucleotide synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01928","properties":[{"key":"EntryName","value":"PurK"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR003135","properties":[{"key":"EntryName","value":"ATP-grasp_carboxylate-amine"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"InterPro","id":"IPR005875","properties":[{"key":"EntryName","value":"PurK"}]},{"database":"InterPro","id":"IPR040686","properties":[{"key":"EntryName","value":"PurK_C"}]},{"database":"InterPro","id":"IPR054350","properties":[{"key":"EntryName","value":"PurT/PurK_preATP-grasp"}]},{"database":"InterPro","id":"IPR011054","properties":[{"key":"EntryName","value":"Rudment_hybrid_motif"}]},{"database":"NCBIfam","id":"NF004676","properties":[{"key":"EntryName","value":"PRK06019.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004679","properties":[{"key":"EntryName","value":"PRK06019.1-5"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004675","properties":[{"key":"EntryName","value":"purK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01161","properties":[{"key":"EntryName","value":"purK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11609:SF5","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLAMINOIMIDAZOLE CARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11609","properties":[{"key":"EntryName","value":"PURINE BIOSYNTHESIS PROTEIN 6/7, PUR6/7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02222","properties":[{"key":"EntryName","value":"ATP-grasp"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17769","properties":[{"key":"EntryName","value":"PurK_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22660","properties":[{"key":"EntryName","value":"RS_preATP-grasp-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51246","properties":[{"key":"EntryName","value":"Rudiment single hybrid motif"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTGSNRVKLKPGDTIGILGGGQLGRMLALAAARLGLRCQVFSPDPDSPAFDVVLNATCAEYADVEALELFANDVDVVTYEFENVPSAAAMVLASRRPVLPSRSALETTQDRLTEKDFVTSLGIRTANYADVSSPATLREAILRIGLPAVLKTRRFGYDGKGQVKIRQGDDLERVWTELGTKSAILEAFIPFEREISVIAARAADGQVECFDVTENEHRDHILKVSRAPARIPDTLADEARDIASRIATALDYVGVLAVEMFVVSDDSNPGVLVNEIAPRVHNSGHWTLDGASISQFEQHIRAIAGWPLGKALRHGHVTMTNLIGDEIDSYEQWLTVPGATVHLYGKGAARPGRKMGHVTQVGPLPPKQG","length":369,"molWeight":39922,"crc64":"4E2E93D911E0D7D9","md5":"4B90E8C05E33843174D946B02CDEE1E6"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":7},"uniParcId":"UPI001E3CB754"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R269","uniProtkbId":"A0ABY3R269_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01435.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00228"}],"value":"Crossover junction endodeoxyribonuclease RuvC"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00228"}],"value":"3.1.21.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"value":"Holliday junction nuclease RuvC"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"value":"Holliday junction resolvase RuvC"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01435.1"}],"value":"ruvC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01435.1"}],"value":"LQG66_19065"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"value":"The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair. Endonuclease that resolves HJ intermediates. Cleaves cruciform DNA by making single-stranded nicks across the HJ at symmetrical positions within the homologous arms, yielding a 5'-phosphate and a 3'-hydroxyl group; requires a central core of homology in the junction. The consensus cleavage sequence is 5'-(A/T)TT(C/G)-3'. Cleavage occurs on the 3'-side of the TT dinucleotide at the point of strand exchange. HJ branch migration catalyzed by RuvA-RuvB allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage at a junction such as a reciprocal single-stranded crossover between two homologous DNA duplexes (Holliday junction).","ecNumber":"3.1.21.10","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029354"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"value":"Binds 2 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"value":"Homodimer which binds Holliday junction (HJ) DNA. The HJ becomes 2-fold symmetrical on binding to RuvC with unstacked arms; it has a different conformation from HJ DNA in complex with RuvA. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009518"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"value":"Belongs to the RuvC family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}]},{"type":"Active site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}]},{"type":"Active site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}]},{"type":"Binding site","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"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_00034"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00034"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01435.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01435.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01435.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317233.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_19065","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0048476","properties":[{"key":"GoTerm","value":"C:Holliday junction resolvase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008821","properties":[{"key":"GoTerm","value":"F:crossover junction DNA endonuclease 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:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009432","properties":[{"key":"GoTerm","value":"P:SOS response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd16962","properties":[{"key":"EntryName","value":"RuvC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.420.10:FF:000002","properties":[{"key":"EntryName","value":"Crossover junction endodeoxyribonuclease RuvC"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.10","properties":[{"key":"EntryName","value":"Ribonuclease H-like superfamily/Ribonuclease H"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00034","properties":[{"key":"EntryName","value":"RuvC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012337","properties":[{"key":"EntryName","value":"RNaseH-like_sf"}]},{"database":"InterPro","id":"IPR036397","properties":[{"key":"EntryName","value":"RNaseH_sf"}]},{"database":"InterPro","id":"IPR020563","properties":[{"key":"EntryName","value":"X-over_junc_endoDNase_Mg_BS"}]},{"database":"InterPro","id":"IPR002176","properties":[{"key":"EntryName","value":"X-over_junc_endoDNase_RuvC"}]},{"database":"NCBIfam","id":"TIGR00228","properties":[{"key":"EntryName","value":"ruvC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30194","properties":[{"key":"EntryName","value":"CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE RUVC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30194:SF3","properties":[{"key":"EntryName","value":"CROSSOVER JUNCTION ENDODEOXYRIBONUCLEASE RUVC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02075","properties":[{"key":"EntryName","value":"RuvC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00696","properties":[{"key":"EntryName","value":"RSOLVASERUVC"}]},{"database":"SUPFAM","id":"SSF53098","properties":[{"key":"EntryName","value":"Ribonuclease H-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01321","properties":[{"key":"EntryName","value":"RUVC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKAQPIRAAVRIIGIDPGLRRTGWGVIESEGNRLIYVGCGSVEPPDDLPLASRLLAIHEGLSAVLGRFSPMEAAVEQTFVNKDGVATLKLGQARGIAMLAPAMFGISVAEYAPNQVKKTVVGAGHADKGQIAVMLKILLPKADPPSADAADALAIAITHAHHRQGTALRMKVAGL","length":175,"molWeight":18283,"crc64":"544C5AB08D23279A","md5":"846C321F189981494C16E22EA2A6F784"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3,"Binding site":3},"uniParcId":"UPI001E5553ED"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R274","uniProtkbId":"A0ABY3R274_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01434.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"value":"Holliday junction branch migration complex subunit RuvA"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01434.1"}],"value":"ruvA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01434.1"}],"value":"LQG66_19060"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"value":"The RuvA-RuvB-RuvC complex processes Holliday junction (HJ) DNA during genetic recombination and DNA repair, while the RuvA-RuvB complex plays an important role in the rescue of blocked DNA replication forks via replication fork reversal (RFR). RuvA specifically binds to HJ cruciform DNA, conferring on it an open structure. The RuvB hexamer acts as an ATP-dependent pump, pulling dsDNA into and through the RuvAB complex. HJ branch migration allows RuvC to scan DNA until it finds its consensus sequence, where it cleaves and resolves the cruciform DNA"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"value":"Homotetramer. Forms an RuvA(8)-RuvB(12)-Holliday junction (HJ) complex. HJ DNA is sandwiched between 2 RuvA tetramers; dsDNA enters through RuvA and exits via RuvB. An RuvB hexamer assembles on each DNA strand where it exits the tetramer. Each RuvB hexamer is contacted by two RuvA subunits (via domain III) on 2 adjacent RuvB subunits; this complex drives branch migration. In the full resolvosome a probable DNA-RuvA(4)-RuvB(12)-RuvC(2) complex forms which resolves the HJ"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"value":"Has three domains with a flexible linker between the domains II and III and assumes an 'L' shape. Domain III is highly mobile and contacts RuvB"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"value":"Belongs to the RuvA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Helix-hairpin-helix DNA-binding motif class 1","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00278"}]},{"type":"Domain","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Helix-hairpin-helix DNA-binding motif class 1","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00278"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"Domain I","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}]},{"type":"Region","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"Domain III","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00031"}],"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_00031"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01434.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01434.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01434.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317232.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_19060","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009379","properties":[{"key":"GoTerm","value":"C:Holliday junction helicase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0048476","properties":[{"key":"GoTerm","value":"C:Holliday junction resolvase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000400","properties":[{"key":"GoTerm","value":"F:four-way junction DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009378","properties":[{"key":"GoTerm","value":"F:four-way junction helicase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.10.150.20","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.10","properties":[{"key":"EntryName","value":"DNA helicase RuvA subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00031","properties":[{"key":"EntryName","value":"DNA_HJ_migration_RuvA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013849","properties":[{"key":"EntryName","value":"DNA_helicase_Holl-junc_RuvA_I"}]},{"database":"InterPro","id":"IPR060101","properties":[{"key":"EntryName","value":"HHH_SAM-like"}]},{"database":"InterPro","id":"IPR003583","properties":[{"key":"EntryName","value":"Hlx-hairpin-Hlx_DNA-bd_motif"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR000085","properties":[{"key":"EntryName","value":"RuvA"}]},{"database":"InterPro","id":"IPR010994","properties":[{"key":"EntryName","value":"RuvA_2-like"}]},{"database":"InterPro","id":"IPR011114","properties":[{"key":"EntryName","value":"RuvA_C"}]},{"database":"InterPro","id":"IPR036267","properties":[{"key":"EntryName","value":"RuvA_C_sf"}]},{"database":"NCBIfam","id":"TIGR00084","properties":[{"key":"EntryName","value":"ruvA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14520","properties":[{"key":"EntryName","value":"HHH_5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07499","properties":[{"key":"EntryName","value":"RuvA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01330","properties":[{"key":"EntryName","value":"RuvA_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00278","properties":[{"key":"EntryName","value":"HhH1"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF46929","properties":[{"key":"EntryName","value":"DNA helicase RuvA subunit, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50249","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47781","properties":[{"key":"EntryName","value":"RuvA domain 2-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIGKLKGLIDSTSEDFVILDVGGVGYQVHCSARTLQALPSPGEAATLSIETYVREDQIKLFGFRSDVEREWFRLLQTVQGVGAKVALAVLGTLPPADLANAIALRDKAAVARTPGVGPKVAERIVTELKDKAPAFANVDPGAVRLSGAIEESRAPQPVADAISALINLGYGQPQAAAAIAAASRAAGDKAETAQLIRLGLKELAK","length":205,"molWeight":21364,"crc64":"812F1B87F630C5AA","md5":"22DED8A5C583050503055868CCE7FDB3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2},"uniParcId":"UPI001E472B73"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R289","uniProtkbId":"A0ABY3R289_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01450.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01389"}],"value":"DNA helicase RecQ"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01389"}],"value":"5.6.2.4"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01450.1"}],"value":"recQ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01450.1"}],"value":"LQG66_19170"}]}],"comments":[{"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"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005446"}],"value":"Belongs to the helicase family. RecQ subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":375,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Domain","location":{"start":{"value":541,"modifier":"EXACT"},"end":{"value":621,"modifier":"EXACT"}},"description":"HRDC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50967"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01450.1"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01450.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01450.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01450.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317248.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_19170","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0043590","properties":[{"key":"GoTerm","value":"C:bacterial nucleoid"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030894","properties":[{"key":"GoTerm","value":"C:replisome"},{"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-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009378","properties":[{"key":"GoTerm","value":"F:four-way junction helicase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006260","properties":[{"key":"GoTerm","value":"P:DNA replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009432","properties":[{"key":"GoTerm","value":"P:SOS response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd17920","properties":[{"key":"EntryName","value":"DEXHc_RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18794","properties":[{"key":"EntryName","value":"SF2_C_RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.10:FF:000175","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000156","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase recQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001389","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.80","properties":[{"key":"EntryName","value":"HRDC 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":"2"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011545","properties":[{"key":"EntryName","value":"DEAD/DEAH_box_helicase_dom"}]},{"database":"InterPro","id":"IPR004589","properties":[{"key":"EntryName","value":"DNA_helicase_ATP-dep_RecQ"}]},{"database":"InterPro","id":"IPR006293","properties":[{"key":"EntryName","value":"DNA_helicase_ATP-dep_RecQ_bac"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR010997","properties":[{"key":"EntryName","value":"HRDC-like_sf"}]},{"database":"InterPro","id":"IPR002121","properties":[{"key":"EntryName","value":"HRDC_dom"}]},{"database":"InterPro","id":"IPR044876","properties":[{"key":"EntryName","value":"HRDC_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR032284","properties":[{"key":"EntryName","value":"RecQ_Zn-bd"}]},{"database":"InterPro","id":"IPR018982","properties":[{"key":"EntryName","value":"RQC_domain"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"NCBIfam","id":"TIGR01389","properties":[{"key":"EntryName","value":"recQ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00614","properties":[{"key":"EntryName","value":"recQ_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13710:SF105","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE Q1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13710","properties":[{"key":"EntryName","value":"DNA HELICASE RECQ FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00270","properties":[{"key":"EntryName","value":"DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00271","properties":[{"key":"EntryName","value":"Helicase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00570","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16124","properties":[{"key":"EntryName","value":"RecQ_Zn_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09382","properties":[{"key":"EntryName","value":"RQC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00341","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00956","properties":[{"key":"EntryName","value":"RQC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47819","properties":[{"key":"EntryName","value":"HRDC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50967","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPPAPNATTDTADRALSVLHSVFGLPGFRGAQEKVVRHVADGGNCLVLMPTGGGKSLCYQLPALLRKGCGIVVSPLIALMRDQVAGLLEAGVNAAVLNSTLSREEAHEVERRLISGDLDLLYVAPERLVTPRCLSLLERAEIALFAIDEAHCVSQWGHDFRPEYIGLSVIAERFPDVPRIALTATADELTRKEIAERLSLTDAPQFVASFDRPNIRYEIVDKNNGPAQLKAFIKDRHAGDAGVVYCLSRAKVEDTAAALTEAGITALPYHAGLDAGVRARNQDRFINEDGIVVVATVAFGMGIDKPDVRFVAHLDLPKSIEAYYQETGRAGRDGKPSTAWMAYGLSDIVQQRRMIDESNGAEAFKRVSIRKLDALVALAETAGCRRRLLLSYFGESPAAETCGNCDNCLSPPKVRDGKVIAQKLLSCAYRTGQRFGAMHLIDVLVGRATERVKQFGHDQLSVFGIGRELNEKQWRAALRQVVAMGHLAPDSEAYGALKLTETSRGVLKGETAVMLREETASTARAIRSKSRRGDLVPRPGQAADAPLLASLRAWRSDIARKRGVPAYVVLHDATIDGIAAARPTTSGQLRDIPGIGDKKLEHYGDELLALIAAARPSGSGSPPDG","length":625,"molWeight":67440,"crc64":"C31345142CD93455","md5":"AA5BF84C688F02D11E1B6E1E33EE3136"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SIMILARITY":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI001E29E20B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R290","uniProtkbId":"A0ABY3R290_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01449.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013152"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00232"}],"value":"Transketolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013152"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00232"}],"value":"2.2.1.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01449.1"}],"value":"tkt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01449.1"}],"value":"LQG66_19165"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00096212"}],"value":"Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10508"},{"database":"ChEBI","id":"CHEBI:57483"},{"database":"ChEBI","id":"CHEBI:57737"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"2.2.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049473"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001913"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001941"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"value":"Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"value":"Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"value":"Binds 1 thiamine pyrophosphate per subunit. During the reaction, the substrate forms a covalent intermediate with the cofactor."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005215"}],"value":"Carbohydrate biosynthesis; Calvin cycle"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004959"}],"value":"Carbohydrate degradation; pentose phosphate pathway"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007131"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"value":"Belongs to the transketolase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":523,"modifier":"EXACT"}},"description":"Transketolase-like pyrimidine-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00861"}]},{"type":"Active site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-1"}]},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":155,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":467,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":471,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":518,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-5"}]},{"type":"Site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-5"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01449.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01449.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01449.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317247.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_19165","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004802","properties":[{"key":"GoTerm","value":"F:transketolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006098","properties":[{"key":"GoTerm","value":"P:pentose-phosphate shunt"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd07033","properties":[{"key":"EntryName","value":"TPP_PYR_DXS_TK_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02012","properties":[{"key":"EntryName","value":"TPP_TK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000003","properties":[{"key":"EntryName","value":"Transketolase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000004","properties":[{"key":"EntryName","value":"Transketolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.920","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR009014","properties":[{"key":"EntryName","value":"Transketo_C/PFOR_II"}]},{"database":"InterPro","id":"IPR055152","properties":[{"key":"EntryName","value":"Transketolase-like_C_2"}]},{"database":"InterPro","id":"IPR005475","properties":[{"key":"EntryName","value":"Transketolase-like_Pyr-bd"}]},{"database":"InterPro","id":"IPR005478","properties":[{"key":"EntryName","value":"Transketolase_bac-like"}]},{"database":"InterPro","id":"IPR020826","properties":[{"key":"EntryName","value":"Transketolase_BS"}]},{"database":"InterPro","id":"IPR049557","properties":[{"key":"EntryName","value":"Transketolase_CS"}]},{"database":"InterPro","id":"IPR033247","properties":[{"key":"EntryName","value":"Transketolase_fam"}]},{"database":"InterPro","id":"IPR005474","properties":[{"key":"EntryName","value":"Transketolase_N"}]},{"database":"NCBIfam","id":"TIGR00232","properties":[{"key":"EntryName","value":"tktlase_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43522","properties":[{"key":"EntryName","value":"TRANSKETOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43522:SF2","properties":[{"key":"EntryName","value":"TRANSKETOLASE 1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02779","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22613","properties":[{"key":"EntryName","value":"Transketolase_C_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00456","properties":[{"key":"EntryName","value":"Transketolase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00861","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52922","properties":[{"key":"EntryName","value":"TK C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00801","properties":[{"key":"EntryName","value":"TRANSKETOLASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00802","properties":[{"key":"EntryName","value":"TRANSKETOLASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQVEHSRMANAIRGLAMDAVEKAKSGHPGLPMGAADVATVLFTRFLKYDAAAPAWPDRDRFVLSAGHGSMLLYALLYLTGNEDMTLDQIKRFRQVDSLTPGHPENFRTKGIETTTGPLGQGISTAVGMALAEKMLQAEYGKKTVDHHTYVLASDGDLMEGISQEAIAMAGHWKLNKLIVLWDDNGISIDGPLSIADSVDQVKRFKACGWAAELIDGHDPQAIEAAITRAQKSSRPSLIACKTTIGYGAPTKAGTSKVHGEALGAEELKGAKEKLGISLEPFSVPDDVLAAWREAGRRGAAVRTEWETRLAEMGPRKRAEFERRLRHERPASLAKALKDHKKALLETPLNAATRKSSEAAIEVIAAAMPTEFLAGSADLTGSNNNKAKSVTAFSAKTPKGRFIHYGIREHGMAAAMNGIFLHGGFAPNGATFLVFSDYARGAMRLAALMGAGVVYVLTHDSIGLGEDGPTHQPVEHLAALRAIPNMRVFRPCDAVETAECWEIALNRTNGPTVLALTRQNLPQLRTSAPADNPCSRGGYELVAAQGEAKVSLFATGSEVEIAVAAQKQLAERGIPARVVSVPSLELLLEQPAETKAAIIGKAPVKIAIEAAVRWGWDAVIGQDGLFVGMHSFGESGPAKELYKHFGITAEAAVEAAVKRLG","length":661,"molWeight":70619,"crc64":"32363D5CDFC5CFE1","md5":"533D028787BE7EB5DA78778327C29E57"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":6,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":17,"Site":2},"uniParcId":"UPI001E5110B0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R2K0","uniProtkbId":"A0ABY3R2K0_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01453.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00016471"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"value":"Phosphoglycerate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013061"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"value":"2.7.2.3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"value":"pgk"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01453.1"}],"value":"LQG66_19185"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-3-phosphoglycerate + ATP = (2R)-3-phospho-glyceroyl phosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14801"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57604"},{"database":"ChEBI","id":"CHEBI:58272"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000642"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000532"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008982"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000532"}],"value":"Belongs to the phosphoglycerate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58272"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-1"}],"ligand":{"name":"(2R)-3-phosphoglycerate","id":"ChEBI:CHEBI:58272"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-1"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58272"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-1"}],"ligand":{"name":"(2R)-3-phosphoglycerate","id":"ChEBI:CHEBI:58272"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58272"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-1"}],"ligand":{"name":"(2R)-3-phosphoglycerate","id":"ChEBI:CHEBI:58272"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000724-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00145"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"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_00145"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01453.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01453.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01453.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317251.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_19185","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043531","properties":[{"key":"GoTerm","value":"F:ADP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004618","properties":[{"key":"GoTerm","value":"F:phosphoglycerate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.1260:FF:000006","properties":[{"key":"EntryName","value":"Phosphoglycerate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1260:FF:000031","properties":[{"key":"EntryName","value":"Phosphoglycerate kinase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1260","properties":[{"key":"EntryName","value":"Phosphoglycerate kinase, N-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00145","properties":[{"key":"EntryName","value":"Phosphoglyc_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001576","properties":[{"key":"EntryName","value":"Phosphoglycerate_kinase"}]},{"database":"InterPro","id":"IPR015911","properties":[{"key":"EntryName","value":"Phosphoglycerate_kinase_CS"}]},{"database":"InterPro","id":"IPR015824","properties":[{"key":"EntryName","value":"Phosphoglycerate_kinase_N"}]},{"database":"InterPro","id":"IPR036043","properties":[{"key":"EntryName","value":"Phosphoglycerate_kinase_sf"}]},{"database":"PANTHER","id":"PTHR11406","properties":[{"key":"EntryName","value":"PHOSPHOGLYCERATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11406:SF23","properties":[{"key":"EntryName","value":"PHOSPHOGLYCERATE KINASE 1, CHLOROPLASTIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00162","properties":[{"key":"EntryName","value":"PGK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000724","properties":[{"key":"EntryName","value":"Pgk"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00477","properties":[{"key":"EntryName","value":"PHGLYCKINASE"}]},{"database":"SUPFAM","id":"SSF53748","properties":[{"key":"EntryName","value":"Phosphoglycerate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00111","properties":[{"key":"EntryName","value":"PGLYCERATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKFRTLDDVDVKGKRVLLRVDLNVPMENGHVTDATRLERVAPTINEIATKGGKVILLAHFGRPKGRDLKESLKPVAAALSAVIKRPVAFADDCIGAPAATAIAAMKDGDVLCLENTRFHKEEEKNDPAFVAELAKLGDIWVNDAFSAAHRAHASTEGLGHKLPAYAGRTMQAELVALEKALGSPAKPVIAIVGGAKVSTKIDLLENLVTKVDALVIGGGMANTFLHAQGVQIGKSLAEKDLAATALRIMDKAEASNCAIILPVDATVSFHFAANSPSFAYGLDAIPPDSMILDVGPQSTARIHSAIDDAATLVWNGPLGAFELNPFDRGTMVAAKHAAERTKAKKLVSVAGGGDTVAALNQAGVASDFTYVSTAGGAFLEWMEGKPLPGVEVLKI","length":396,"molWeight":41534,"crc64":"98883C3C8DD765A0","md5":"97A45769518EDE673F07A9EF018E1697"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":11},"uniParcId":"UPI001E3F463D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY3R2K1","uniProtkbId":"A0ABY3R2K1_9BRAD","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Bradyrhizobium ontarionense","taxonId":2898149,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01531.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Nitrobacteraceae","Bradyrhizobium"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01792"}],"value":"Urease subunit alpha"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01792"}],"value":"3.5.1.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"}],"value":"Urea amidohydrolase subunit alpha"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01531.1"}],"value":"ureC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01531.1"}],"value":"LQG66_19595"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"urea + 2 H2O + H(+) = hydrogencarbonate + 2 NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20557"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16199"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"}],"ecNumber":"3.5.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000510"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ni cation","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000510"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:25516"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000510"}],"value":"Binds 2 nickel ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004897"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"}],"value":"Nitrogen metabolism; urea degradation; CO(2) and NH(3) from urea (urease route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"}],"value":"Heterotrimer of UreA (gamma), UreB (beta) and UreC (alpha) subunits. Three heterotrimers associate to form the active enzyme"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00700"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-50"}],"value":"Carbamylation allows a single lysine to coordinate two nickel ions"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"}],"value":"Carboxylation allows a single lysine to coordinate two nickel ions"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004158"}],"value":"Belongs to the metallo-dependent hydrolases superfamily. Urease alpha subunit family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":571,"modifier":"EXACT"}},"description":"Urease","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51368"}]},{"type":"Active site","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-52"}]},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","label":"1"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","label":"1"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","label":"1"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"via carbamate group","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","label":"2"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00700"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","label":"2"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","label":"2"}},{"type":"Binding site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-51"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786","label":"1"}},{"type":"Modified residue","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611612-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00700"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022596"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01953"}],"id":"KW-0533","category":"Ligand","name":"Nickel"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001431010"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"38647727","citationType":"journal article","authors":["Bromfield E.S.P.","Cloutier S."],"citationCrossReferences":[{"database":"PubMed","id":"38647727"}],"title":"Bradyrhizobium ontarionense sp. nov., a novel bacterial symbiont isolated from Aeschynomene indica (Indian jointvetch), harbours photosynthesis, nitrogen fixation and nitrous oxide (N2O) reductase genes.","publicationDate":"2024","journal":"Antonie Van Leeuwenhoek","firstPage":"69","lastPage":"69","volume":"117"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01531.1"}],"value":"A19","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"UFZ01531.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP088156","properties":[{"key":"ProteinId","value":"UFZ01531.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_231317328.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP088156.1"}]},{"database":"KEGG","id":"boy:LQG66_19595","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001431010","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0016151","properties":[{"key":"GoTerm","value":"F:nickel cation binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009039","properties":[{"key":"GoTerm","value":"F:urease activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043419","properties":[{"key":"GoTerm","value":"P:urea catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00375","properties":[{"key":"EntryName","value":"Urease_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.40.10","properties":[{"key":"EntryName","value":"Urease, subunit C, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01953","properties":[{"key":"EntryName","value":"Urease_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006680","properties":[{"key":"EntryName","value":"Amidohydro-rel"}]},{"database":"InterPro","id":"IPR011059","properties":[{"key":"EntryName","value":"Metal-dep_hydrolase_composite"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"database":"InterPro","id":"IPR011612","properties":[{"key":"EntryName","value":"Urease_alpha_N_dom"}]},{"database":"InterPro","id":"IPR017950","properties":[{"key":"EntryName","value":"Urease_AS"}]},{"database":"InterPro","id":"IPR005848","properties":[{"key":"EntryName","value":"Urease_asu"}]},{"database":"InterPro","id":"IPR017951","properties":[{"key":"EntryName","value":"Urease_asu_c"}]},{"database":"InterPro","id":"IPR029754","properties":[{"key":"EntryName","value":"Urease_Ni-bd"}]},{"database":"NCBIfam","id":"NF009685","properties":[{"key":"EntryName","value":"PRK13206.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009686","properties":[{"key":"EntryName","value":"PRK13207.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01792","properties":[{"key":"EntryName","value":"urease_alph"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43440","properties":[{"key":"EntryName","value":"UREASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43440:SF1","properties":[{"key":"EntryName","value":"UREASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01979","properties":[{"key":"EntryName","value":"Amidohydro_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00449","properties":[{"key":"EntryName","value":"Urease_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01752","properties":[{"key":"EntryName","value":"UREASE"}]},{"database":"SUPFAM","id":"SSF51338","properties":[{"key":"EntryName","value":"Composite domain of metallo-dependent hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01120","properties":[{"key":"EntryName","value":"UREASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00145","properties":[{"key":"EntryName","value":"UREASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51368","properties":[{"key":"EntryName","value":"UREASE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSVKIKRSVYADMFGPTTGDKVRLADTDLIIEVEKDFTIYGEEVKFGGGKVIRDGMGQSQATNKQGAADTVITNALIVDHWGVVKADVAIKEGMISAIGKAGNPDIQPGVTIVIGPGTDVIAGEGKILTAGGFDSHIHFICPQQIEHALMSGVTSLLGGGTGPSHGTFATTCTPGPWHIGRMMQSFDAFPVNLGISGKGNASRPAALVEMVKAGACALKLHEDWGTTPAAIDNCLSVADDYDVQVMLHSDTLNESGFVEDTIKAFKGRTIHAFHTEGAGGGHAPDIIKVAGLKNVLPSSTNPTRPFTRNTIDEHLDMLMVCHHLDPSIAEDLAFAESRIRKETIAAEDILHDLGALSMMSSDSQAMGRLGEVIIRTWQTADKMKKQRGALPQDKGKDNDNFRVKRYIAKYTINPAIAHGVSKLIGSVEKGKLADLVLWSPAFFGVKPDCVIKGGTIVAAPMGDPNASIPTPQPVHYQPMFGAFGKSLTASSVIFTSKAAVTGGLARKLGLSKKLYAVQNTRGRISKKSMIHNDATPDIEVDPETYEVRADGELLTCEPAEVLPMAQRYFMF","length":571,"molWeight":61004,"crc64":"058BFDC9752DDB87","md5":"7E5C19C6FDE6F28EB893814BE479AD13"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":2,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":8,"Modified residue":1},"uniParcId":"UPI001E5BADC6"}}]}