{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JHP2","uniProtkbId":"A0ABX0JHP2_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83213.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"GTP cyclohydrolase II"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"4.1.99.12"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83213.1"}],"value":"ribB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"ribA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83213.1"}],"value":"GOB93_00965"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043932"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049295"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004853"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"value":"Belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"value":"Belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008976"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83213.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Active site","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}]},{"type":"Active site","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}]},{"type":"Binding site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":302,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":387,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Essential for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]},{"type":"Site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"Essential for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"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":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022619"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00180"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00179"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83213.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83213.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000001","properties":[{"key":"ProteinId","value":"NHN83213.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPASLARAVEAIRAGRMVIMVDDEDRENEGDLVMAAEFMTPAAMNFMVTYGRGLVCLPLTPERVDQLELPMMTRVNTAPRGTAFTVSIEATEGVTTGISAYDRAQTVLTAVAPEAKSSDLVSPGHIFPLRAAPGGVLERNGHTEGSIDLALLAGCRPAAVICEIMSADGTMARRPELEVFGAEHGLPIVSIAELCDWIGQHGKSPVETGEIDSAAILPSVLLDAVNGAQPALTAEVAEAALPGVFGGNDLIIHAFRDGEGIEHVALVKGNLSESDNVPLVRLHSECLTGDALGSLRCDCGAQLQTALRKISEADSGVLIYLRGHEGRGIGLGNKIRAYALQDQGLDTIDANHRLGFVADARDWSSAASILRDLGVGTLDLMTNNPEKVRALEERGFNVRQRIGLDIPPNPFNRAYLDAKRRRMGHSLKAESVRAGK","length":436,"molWeight":46407,"crc64":"B6FAC8508139F98B","md5":"0EA4CF9770B1BF099584D1B78AF24354"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":15,"Site":2},"uniParcId":"UPI0019FFE190"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JJQ0","uniProtkbId":"A0ABX0JJQ0_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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:0000313","source":"EMBL","id":"NHN83053.1"}],"value":"ispF"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"ispDF"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83053.1"}],"value":"GOB93_00095"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13429"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:57823"},{"database":"ChEBI","id":"CHEBI:58262"}],"ecNumber":"2.7.7.60","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001282"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23864"},{"database":"ChEBI","id":"CHEBI:57919"},{"database":"ChEBI","id":"CHEBI:58483"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"4.6.1.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000200"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001968"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004787"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004709"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009789"}],"value":"Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008480"}],"value":"Belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the C-terminal section; belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83053.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":384,"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":231,"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":232,"modifier":"EXACT"},"end":{"value":387,"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":238,"modifier":"EXACT"},"end":{"value":240,"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":238,"modifier":"EXACT"},"end":{"value":238,"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":240,"modifier":"EXACT"},"end":{"value":240,"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":264,"modifier":"EXACT"},"end":{"value":265,"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":272,"modifier":"EXACT"},"end":{"value":272,"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":286,"modifier":"EXACT"},"end":{"value":288,"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":362,"modifier":"EXACT"},"end":{"value":365,"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":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":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":"Site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":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":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83053.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000001","properties":[{"key":"ProteinId","value":"NHN83053.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581586.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000001.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008685","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050518","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019288","properties":[{"key":"GoTerm","value":"P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016114","properties":[{"key":"GoTerm","value":"P:terpenoid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02516","properties":[{"key":"EntryName","value":"CDP-ME_synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00554","properties":[{"key":"EntryName","value":"MECDP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.550.10:FF:000003","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1330.50","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00108","properties":[{"key":"EntryName","value":"IspD"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01520","properties":[{"key":"EntryName","value":"IspDF"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00107","properties":[{"key":"EntryName","value":"IspF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001228","properties":[{"key":"EntryName","value":"IspD"}]},{"database":"InterPro","id":"IPR026596","properties":[{"key":"EntryName","value":"IspD/F"}]},{"database":"InterPro","id":"IPR034683","properties":[{"key":"EntryName","value":"IspD/TarI"}]},{"database":"InterPro","id":"IPR018294","properties":[{"key":"EntryName","value":"ISPD_synthase_CS"}]},{"database":"InterPro","id":"IPR003526","properties":[{"key":"EntryName","value":"MECDP_synthase"}]},{"database":"InterPro","id":"IPR020555","properties":[{"key":"EntryName","value":"MECDP_synthase_CS"}]},{"database":"InterPro","id":"IPR036571","properties":[{"key":"EntryName","value":"MECDP_synthase_sf"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"NCBIfam","id":"TIGR00453","properties":[{"key":"EntryName","value":"ispD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00151","properties":[{"key":"EntryName","value":"ispF"},{"key":"MatchStatus","value":"1"}]},{"database":"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":"MRVAAILLAAGLGSRYAAATGHTIAKQFVTLAGRPVIRHAAEALLPHVALLQPVGDPDLLAEALHGLTFLPPVAGGAERQDSVRAGLEALDALPEDQKPDLVLVHDGARPYVTAALIEGVIAALADHPGAIPAVPVADTLKRGENGVIAGTVSREHLFRAQTPQGFRFPLLRDLHRSAAAQSGVTATDDALLLESSGFSVALVPGSEDNIKLTYEEDLVRLERLIGPALLPRTGFGYDVHAFAENRPLIICGITIPHTRGLAGHSDADVGIHALCDAIYGALAEGDIGRHFPPSQNEWKDADSARFLVHAGELVRSKGGMLVNADVTLICERPKIGPHAQAMRERMASLLQVDVGRISVKATTSERLGFTGREEGIACAATATVLVP","length":387,"molWeight":40751,"crc64":"44F26CAEAF3EC8B1","md5":"946C3D76952F259336CDA3B38D01C9D1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":9,"Site":6},"uniParcId":"UPI00156B53D7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JKY3","uniProtkbId":"A0ABX0JKY3_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83897.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN83897.1"}],"value":"GOB93_04465"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025153"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADHX = (6S)-NADHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32215"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:64075"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000013"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADPHX = (6S)-NADPHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32227"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:64077"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000909"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADHX + ADP = AMP + phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32223"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32235"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009524"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the C-terminal section; belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006001"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the N-terminal section; belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83897.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":65,"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":62,"modifier":"EXACT"},"end":{"value":62,"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":121,"modifier":"EXACT"},"end":{"value":121,"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":125,"modifier":"EXACT"},"end":{"value":131,"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":150,"modifier":"EXACT"},"end":{"value":150,"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":153,"modifier":"EXACT"},"end":{"value":153,"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":249,"modifier":"EXACT"},"end":{"value":249,"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":307,"modifier":"EXACT"},"end":{"value":307,"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":353,"modifier":"EXACT"},"end":{"value":353,"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":386,"modifier":"EXACT"},"end":{"value":390,"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":415,"modifier":"EXACT"},"end":{"value":415,"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":416,"modifier":"EXACT"},"end":{"value":416,"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":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83897.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83897.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000004","properties":[{"key":"ProteinId","value":"NHN83897.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173582292.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000004.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDKRNLLALPSPAEMGRVDHLASALVPVSVLMENAGRAVARAVRRFTRPCRVLVLCGPGNNGGDGYVAARYLAEAGWPVAAASLVAPRPGTDAAAVAARFRGPCVQFSPDEVARADMVIDAVFGAGLSRDVAGPVSEVLAVAKRIVAVDMPSGIDGATGQIRGYAPRADLTVTFFRAKPGHLLLPGREYVGALEVHDIGIPEAVMDSVGVLTWQNEPGLWKLPVPGLEAYKYSRGVVSVAAGEAMPGAARLAATAARRTGAGLVRIAAGKAAAVFRMNEPGLIIDENPLDDLLADKRRKVWICGPGLLPEEVGEVLPKLLSSGRCVLADAGAFAWAADNPEKLHGVAVVTPHAGEFKRVFGAPGADPLAAARAAAVRIGAVVVLKGATTIIAAPDGRAALNVHATSALGTAGSGDTLSGVIGALLAAGMEHWSAACAGVWLHGDAGIRAGNWLIAEDLDTHLGEARETATRLQDGLRVPSGVPCRS","length":487,"molWeight":50102,"crc64":"7C4581FADB78298A","md5":"27E7745575A487077F01573FAAD61839"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI00156ADCC4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JLI0","uniProtkbId":"A0ABX0JLI0_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83614.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN83614.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83614.1"}],"value":"GOB93_03030"}]}],"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83614.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":123,"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":235,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":18,"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":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"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":146,"modifier":"EXACT"},"end":{"value":146,"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":161,"modifier":"EXACT"},"end":{"value":161,"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":176,"modifier":"EXACT"},"end":{"value":176,"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":233,"modifier":"EXACT"},"end":{"value":233,"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":233,"modifier":"EXACT"},"end":{"value":233,"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":322,"modifier":"EXACT"},"end":{"value":322,"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":340,"modifier":"EXACT"},"end":{"value":340,"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":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"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":375,"modifier":"EXACT"},"end":{"value":376,"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":394,"modifier":"EXACT"},"end":{"value":394,"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":412,"modifier":"EXACT"},"end":{"value":412,"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":429,"modifier":"EXACT"},"end":{"value":429,"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83614.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83614.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000003","properties":[{"key":"ProteinId","value":"NHN83614.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173582056.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000003.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR018357","properties":[{"key":"EntryName","value":"Hexapep_transf_CS"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010933","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00101","properties":[{"key":"EntryName","value":"HEXAPEP_TRANSFERASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MINSQVPAPSTAVLLAAGLGTRMRSALPKAMQPLAGQPMLSHLIVSAAEVFSRVVVVIGPGMDDVAALAAPHATVIQHDRLGTAHAALQAESFFGEGDVAVLYADNPLITPETLSRLLATRRAGTGAERTDLALLAMRPVDPARYGRVITAPDGTVGKIVEWADATEAERDVDLCNAGVLCAEAGHFREWLHRVGNANAKGEYYLTDVVAIARDEGAIVRAVEAPESELRGINSRPELAEAEAIVQARLRQNAMLAGVTLTAPETVFFSFDTLLEPDVVVQPNVVFGPGVTVRSGAEIRAFSHLEGCEVGPRALVGPYARLRPGSSLGEASHVGNFVELKATTLGAGAKANHLTYLGDSSIGAGSNVGAGTITCNYDGVFKHRTTIGENTFIGSDSILVAPVTIGDGALIAAGSVITHDVAPDALAVARGTQVNKPGWAARFRAALRAKKEQS","length":453,"molWeight":47279,"crc64":"127DA8EF8727AE17","md5":"94F91762C0F25065E92C534C9A8E5EE4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":19},"uniParcId":"UPI00156B543A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JLK0","uniProtkbId":"A0ABX0JLK0_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83629.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Xanthine-guanine phosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"XGPRT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"2.4.2.22"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Xanthine phosphoribosyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"gpt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83629.1"}],"value":"GOB93_03105"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Purine salvage pathway enzyme that catalyzes the transfer of the ribosyl-5-phosphate group from 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to the N9 position of the 6-oxopurines guanine and xanthine to form the corresponding ribonucleotides GMP (guanosine 5'-monophosphate) and XMP (xanthosine 5'-monophosphate), with the release of PPi. To a lesser extent, also acts on hypoxanthine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25424"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58115"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17973"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XMP + diphosphate = xanthine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10800"},{"database":"ChEBI","id":"CHEBI:17712"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.22","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Purine metabolism; GMP biosynthesis via salvage pathway; GMP from guanine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Purine metabolism; XMP biosynthesis via salvage pathway; XMP from xanthine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family. XGPT subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83629.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58115"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"GMP","id":"ChEBI:CHEBI:58115"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16235"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"guanine","id":"ChEBI:CHEBI:16235"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17712"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"xanthine","id":"ChEBI:CHEBI:17712"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58115"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"GMP","id":"ChEBI:CHEBI:58115"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16235"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"guanine","id":"ChEBI:CHEBI:16235"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17712"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"ligand":{"name":"xanthine","id":"ChEBI:CHEBI:17712"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022726"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0660","category":"Biological process","name":"Purine salvage"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01903"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83629.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83629.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000003","properties":[{"key":"ProteinId","value":"NHN83629.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173582068.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000003.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004422","properties":[{"key":"GoTerm","value":"F:hypoxanthine phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000310","properties":[{"key":"GoTerm","value":"F:xanthine phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032263","properties":[{"key":"GoTerm","value":"P:GMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032264","properties":[{"key":"GoTerm","value":"P:IMP salvage"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032265","properties":[{"key":"GoTerm","value":"P:XMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01903","properties":[{"key":"EntryName","value":"XGPRT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR023747","properties":[{"key":"EntryName","value":"Xanthine_Guanine_PRibTrfase"}]},{"database":"NCBIfam","id":"NF006613","properties":[{"key":"EntryName","value":"gpt"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39563","properties":[{"key":"EntryName","value":"XANTHINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR39563:SF1","properties":[{"key":"EntryName","value":"XANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATNYATVTWDQLHRDARLLAENLMPRAPFRGIVAVTRGGLIPAAIIARELDCRLIESISVVTYQNEEERGEPTIIKDPEAAGDGEGFLVIDDLVDSGITAQVVRRRLPKAVFACLYAKPSGKPLTDLFVVEVPQDTWVLFPWDTAPLFVPPLARKPVPTE","length":161,"molWeight":17779,"crc64":"CF02FEFCA00B9434","md5":"9EB5FAFD8E81F3456A05046F7CA3441A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":9},"uniParcId":"UPI00156AA360"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JMC8","uniProtkbId":"A0ABX0JMC8_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84631.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Asp/Glu-ADT subunit B"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"6.3.5.6"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"6.3.5.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Glutamyl-tRNA(Gln) amidotransferase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Glu-ADT subunit B"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84631.1"}],"value":"gatB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84631.1"}],"value":"GOB93_08225"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Catalytic subunit of the Asp/Glu-tRNA(Asn/Gln) amidotransferase complex GatCAB. GatCAB allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the multi-step transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). This subunit specifically recognizes tRNA(Gln) and tRNA(Asn), and mediates the transamidation of misloaded Glu and Asp respectively by catalyzing formation of the activated gamma-phospho-intermediate and its subsequent aminolysis using ammonia produced by the gatA subunit. Recognizes the first base pair and the D-loop of its specific tRNA substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-phospho-L-aspartyl-tRNA(Asn) + NH4(+) = L-asparaginyl-tRNA(Asn) + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57920"},{"database":"Rhea","id":"RHEA-COMP:9674"},{"database":"Rhea","id":"RHEA-COMP:15033"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:78515"},{"database":"ChEBI","id":"CHEBI:142450"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-phospho-L-glutamyl-tRNA(Gln) + NH4(+) = L-glutaminyl-tRNA(Gln) + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57912"},{"database":"Rhea","id":"RHEA-COMP:9681"},{"database":"Rhea","id":"RHEA-COMP:15032"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:78521"},{"database":"ChEBI","id":"CHEBI:142449"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-tRNA(Asn) + ATP = 4-phospho-L-aspartyl-tRNA(Asn) + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57916"},{"database":"Rhea","id":"RHEA-COMP:9677"},{"database":"Rhea","id":"RHEA-COMP:15033"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:78516"},{"database":"ChEBI","id":"CHEBI:142450"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-tRNA(Asn) + L-glutamine + ATP + H2O = L-asparaginyl-tRNA(Asn) + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14513"},{"database":"Rhea","id":"RHEA-COMP:9674"},{"database":"Rhea","id":"RHEA-COMP:9677"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:78515"},{"database":"ChEBI","id":"CHEBI:78516"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097075"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamyl-tRNA(Gln) + ATP = 5-phospho-L-glutamyl-tRNA(Gln) + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57908"},{"database":"Rhea","id":"RHEA-COMP:9684"},{"database":"Rhea","id":"RHEA-COMP:15032"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:78520"},{"database":"ChEBI","id":"CHEBI:142449"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl-tRNA(Gln) + L-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17521"},{"database":"Rhea","id":"RHEA-COMP:9681"},{"database":"Rhea","id":"RHEA-COMP:9684"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:78520"},{"database":"ChEBI","id":"CHEBI:78521"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047407"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Binds 2 Mg(2+) ions, a primary Mg(2+) ion involved in positioning of the gamma-carbonyl group of the amino acid in Glu-tRNA(Gln), and a secondary transient Mg(2+) ion that participates in phosphoryl transfer by polarizing the gamma-phosphate group of ATP."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Component of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase complex composed of GatA, GatB and GatC"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"The C-terminal tail domain, an anti-parallel amphiphilic helix bundle, is involved in discriminating and binding specific tRNAs. Probably recognizes the tRNA(Gln)-specific D-loop structure"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"The N-terminal cradle domain recognizes the first base of the acceptor tRNA stem"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Belongs to the GatB/GatE family. GatB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84631.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":482,"modifier":"EXACT"}},"description":"Asn/Gln amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00845"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"Cradle","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Region","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"Tail","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Binding site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"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_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84631.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84631.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000008","properties":[{"key":"ProteinId","value":"NHN84631.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173583016.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000008.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050567","properties":[{"key":"GoTerm","value":"F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070681","properties":[{"key":"GoTerm","value":"P:glutaminyl-tRNAGln biosynthesis via transamidation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006412","properties":[{"key":"GoTerm","value":"P:translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.10.410:FF:000001","properties":[{"key":"EntryName","value":"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.410","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.380","properties":[{"key":"EntryName","value":"GatB domain, N-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00121","properties":[{"key":"EntryName","value":"GatB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017959","properties":[{"key":"EntryName","value":"Asn/Gln-tRNA_amidoTrfase_suB/E"}]},{"database":"InterPro","id":"IPR006075","properties":[{"key":"EntryName","value":"Asn/Gln-tRNA_Trfase_suB/E_cat"}]},{"database":"InterPro","id":"IPR018027","properties":[{"key":"EntryName","value":"Asn/Gln_amidotransferase"}]},{"database":"InterPro","id":"IPR003789","properties":[{"key":"EntryName","value":"Asn/Gln_tRNA_amidoTrase-B-like"}]},{"database":"InterPro","id":"IPR004413","properties":[{"key":"EntryName","value":"GatB"}]},{"database":"InterPro","id":"IPR042114","properties":[{"key":"EntryName","value":"GatB_C_1"}]},{"database":"InterPro","id":"IPR023168","properties":[{"key":"EntryName","value":"GatB_Yqey_C_2"}]},{"database":"InterPro","id":"IPR017958","properties":[{"key":"EntryName","value":"Gln-tRNA_amidoTrfase_suB_CS"}]},{"database":"InterPro","id":"IPR014746","properties":[{"key":"EntryName","value":"Gln_synth/guanido_kin_cat_dom"}]},{"database":"NCBIfam","id":"NF004012","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004014","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004015","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00133","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11659","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11659:SF0","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02934","properties":[{"key":"EntryName","value":"GatB_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02637","properties":[{"key":"EntryName","value":"GatB_Yqey"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00845","properties":[{"key":"EntryName","value":"GatB_Yqey"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF89095","properties":[{"key":"EntryName","value":"GatB/YqeY motif"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55931","properties":[{"key":"EntryName","value":"Glutamine synthetase/guanido kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01234","properties":[{"key":"EntryName","value":"GATB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSYVIEGSTGPWEIVVGLEVHAQVISNSKLFSGASTLFGGEPNTHVSLIDAGFPGMLPVINRGCVAQAVRTGLGLKARINLESRFDRKNYFYADLPQGYQISQFAHPIIGEGKIEIELSDGSTREIGITRLHLEQDAGKLMHDQDPKRSFVDLNRAGVALMEIVSEPDIRTPEEAGAYLRKLRQILRYLGTCDGNMDEGSMRADVNVSVRKAGEPFRTRCEIKNVNSIRFVTQAIEIEAARQVEIWESGGEVDQETRLFDPGRGETRSLRSKEDAHDYRYFPDPDLLPLVIEQSWVDQLKACLPELPDEKRARLQKEYGITAYDAGVLVAEQAIADFYETVAKGRDGKSAAAWMTGDFFAALNRTGKSIEESPVGADKLGAMLDLIADGTINGKIAKEVLETMFETGEAPLEIVERKGLRQVTDTGAIEKAADEVLTKNADKLEQYLGGKDKLFGFFVGQVMKATQGKANPAMVNEILKKKIHG","length":484,"molWeight":53341,"crc64":"F16FC61D16126652","md5":"A09B1751502A7308FED61003630F43A7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":9},"uniParcId":"UPI00156B9661"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JNR9","uniProtkbId":"A0ABX0JNR9_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84250.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN84250.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84250.1"}],"value":"GOB93_06270"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84250.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1084,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5051138441"},{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":684,"modifier":"EXACT"},"end":{"value":879,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":946,"modifier":"EXACT"},"end":{"value":1084,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":946,"modifier":"EXACT"},"end":{"value":1084,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":720,"modifier":"EXACT"},"end":{"value":720,"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":763,"modifier":"EXACT"},"end":{"value":763,"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":765,"modifier":"EXACT"},"end":{"value":765,"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":770,"modifier":"EXACT"},"end":{"value":770,"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":795,"modifier":"EXACT"},"end":{"value":795,"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":796,"modifier":"EXACT"},"end":{"value":796,"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":797,"modifier":"EXACT"},"end":{"value":797,"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":798,"modifier":"EXACT"},"end":{"value":798,"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":838,"modifier":"EXACT"},"end":{"value":838,"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":838,"modifier":"EXACT"},"end":{"value":838,"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":838,"modifier":"EXACT"},"end":{"value":838,"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":850,"modifier":"EXACT"},"end":{"value":850,"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":850,"modifier":"EXACT"},"end":{"value":850,"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":850,"modifier":"EXACT"},"end":{"value":850,"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":850,"modifier":"EXACT"},"end":{"value":850,"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":850,"modifier":"EXACT"},"end":{"value":850,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84250.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84250.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000006","properties":[{"key":"ProteinId","value":"NHN84250.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173582643.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000006.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRTDIRSILIIGAGPIVIGQACEFDYSGAQACKALKEEGYRVILLNSNPATIMTDPGLADATYVEPITPEFVERIILKEKPDAVLPTMGGQTALNAAMALDASGFLQKHGVELIGAKADVIDRAEDRQKFREAMDAIGIESPKSLIAHTLEEARTALKEIGLPTVIRPSFTMGGSGGGIAYNKEEFDQIVMSGLDASPTTEVLIEESVLGWKEFEMEVVRDRADNCIIVCSIENIDPMGVHTGDSITVAPALTLTDKEYQRMRDASIACLRAIGVETGGSNVQFGVNPKDGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELANDITGSTPASFEPTIDYVVVKIPRFTFEKFPGTPALLSTSMKSVGEAMAIGRSFPEALQKGLRSMETGLAGLDPVEAPGDGGPDAYRAALSQPRPERILMAAQALRAGLSVEEIAGACRFEPWFLRELEKIVQAEKHLLDHGLPEDARELRRLKAMGFSDVQLARLSGTQASEVRALREAAGVLPVYKRIDTCAGEFASATPYMYSTYEGGFGAPVCESGPTGAKKVVILGGGPNRIGQGIEFDYCCVHAAYALREAGIETIMVNCNPETVSTDYDTSDRLYFEPLTAEDVGALIRLEQSRGEILGCIVQYGGQTPLKLSRALEEAGIPLLGTPADAIDRAEDRERFQALLHKLGLRQPRNGIARSAAEAEDVAEQVGYPVVVRPSYVLGGRAMEIVYDRASLQRYLKVVLAAAGPEVSSGPVLIDHYLNDAIEADVDCIADGESVYVAGVLEHIEEAGIHSGDSACALPPYTLSPAIVAELKAQTEAMALELGIVGLMNVQYAMKGDDIYVLEVNPRASRTVPFVAKATGVPVAKIGARVMAGAKLGEFTLDDRAVVPHVAVKEAVFPFNRFQDVDVILGPEMRSTGEVMGLDTSFERAFAKSQLAAGVKLPLSGTVFLSVRDGDKAQLPRIGRQLAEMGFTIMATRGTAERLREAGVKVQVVNKVLEGRPHCVDAIRSGEVQMVINTAQGAQAVQDSYDIRRSALTMGIPHYTTMAGARAATHAISAMREGPLEVAPLQSYFHGSY","length":1084,"molWeight":116190,"crc64":"E3EF7F355C16FE68","md5":"751895D297A6E474837B802619C1C5B1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Chain":1,"Domain":3,"Region":2,"Binding site":38,"Lipidation":2},"uniParcId":"UPI00156B89CB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JNX6","uniProtkbId":"A0ABX0JNX6_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83752.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN83752.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83752.1"}],"value":"GOB93_03730"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83752.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":424,"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":217,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"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":333,"modifier":"EXACT"},"end":{"value":336,"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":353,"modifier":"EXACT"},"end":{"value":353,"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":367,"modifier":"EXACT"},"end":{"value":367,"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":371,"modifier":"EXACT"},"end":{"value":371,"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":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83752.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83752.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000003","properties":[{"key":"ProteinId","value":"NHN83752.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173582179.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000003.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKAAAARGDGAAQKRVLLIVSGGIAAYKALELVRLLKTSGVDVRCVLTKAATEFVTPLSLQALSGEPVGQDLFSLTDEQEMGHIVLSRSADLVVVAPATANILAKMAQGLADDLATTLLLATDTPVMVAPAMNVRMWEHPATQANMALLVDRGVMVVGPDEGEMACGEFGAGRFVEPPMLRDAILGWFGGQSSSGAAAASVGFQGAALGWEPLAGRRALVTAGPTHEPVDPVRYLGNRSSGLQGYAIAAALVVLGARVTLVSGPVSLADPAGVNVVRVETGLEMERAVRAALPVDIAVCAAAVADWRVDGISGRKLKKRADMAPPVLTLVPNPDILAILSAPGPERPTLVVGFAAETDDVEVNAVAKRTRKGCDWIVANDVSAGTNVMGGPDNRAVLITEDGIERWPLLPKADLARRLAQRIAARFEAPVMASGGERV","length":438,"molWeight":45515,"crc64":"F3A1F9F43987AFBF","md5":"2FD03AFA09FAD3FB12D9B89355F6FC8E"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":6},"uniParcId":"UPI00156AE8A1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JPF8","uniProtkbId":"A0ABX0JPF8_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83514.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Acireductone dioxygenase"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"1,2-dihydroxy-3-keto-5-methylthiopentene dioxygenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"DHK-MTPene dioxygenase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Acireductone dioxygenase (Fe(2+)-requiring)"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"ARD'"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Fe-ARD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"1.13.11.54"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Acireductone dioxygenase (Ni(2+)-requiring)"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"ARD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Ni-ARD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"1.13.11.53"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"mtnD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83514.1"}],"value":"GOB93_02525"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Catalyzes 2 different reactions between oxygene and the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene) depending upon the metal bound in the active site. Fe-containing acireductone dioxygenase (Fe-ARD) produces formate and 2-keto-4-methylthiobutyrate (KMTB), the alpha-ketoacid precursor of methionine in the methionine recycle pathway. Ni-containing acireductone dioxygenase (Ni-ARD) produces methylthiopropionate, carbon monoxide and formate, and does not lie on the methionine recycle pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 3-(methylsulfanyl)propanoate + CO + formate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14161"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:17245"},{"database":"ChEBI","id":"CHEBI:49016"},{"database":"ChEBI","id":"CHEBI:49252"}],"ecNumber":"1.13.11.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + O2 = 4-methylsulfanyl-2-oxobutanoate + formate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24504"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:16723"},{"database":"ChEBI","id":"CHEBI:49252"}],"ecNumber":"1.13.11.54","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Binds 1 Fe(2+) cation per monomer."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ni(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49786"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Binds 1 nickel ion per monomer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 5/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"value":"Belongs to the acireductone dioxygenase (ARD) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83514.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49786"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"ligand":{"name":"Ni(2+)","id":"ChEBI:CHEBI:49786"}},{"type":"Site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"May play a role in metal incorporation in vivo","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}]},{"type":"Site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"May play a role in transmitting local conformational changes","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}]},{"type":"Site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Important to generate the dianion","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022964"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"id":"KW-0223","category":"Molecular function","name":"Dioxygenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022596"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"id":"KW-0533","category":"Ligand","name":"Nickel"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01682"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83514.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83514.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000002","properties":[{"key":"ProteinId","value":"NHN83514.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581936.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000002.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0010308","properties":[{"key":"GoTerm","value":"F:acireductone dioxygenase (Ni2+-requiring) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010309","properties":[{"key":"GoTerm","value":"F:acireductone dioxygenase [iron(II)-requiring] 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:0016151","properties":[{"key":"GoTerm","value":"F:nickel cation binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006555","properties":[{"key":"GoTerm","value":"P:L-methionine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd02232","properties":[{"key":"EntryName","value":"cupin_ARD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.120.10","properties":[{"key":"EntryName","value":"Jelly Rolls"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01682","properties":[{"key":"EntryName","value":"Salvage_MtnD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004313","properties":[{"key":"EntryName","value":"ARD"}]},{"database":"InterPro","id":"IPR023956","properties":[{"key":"EntryName","value":"ARD_bac"}]},{"database":"InterPro","id":"IPR014710","properties":[{"key":"EntryName","value":"RmlC-like_jellyroll"}]},{"database":"InterPro","id":"IPR011051","properties":[{"key":"EntryName","value":"RmlC_Cupin_sf"}]},{"database":"PANTHER","id":"PTHR23418","properties":[{"key":"EntryName","value":"ACIREDUCTONE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23418:SF0","properties":[{"key":"EntryName","value":"ACIREDUCTONE DIOXYGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03079","properties":[{"key":"EntryName","value":"ARD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51182","properties":[{"key":"EntryName","value":"RmlC-like cupins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSLVVFDDTRPERPEFGTDDPEAIAARLKTIGVRFERWDGAEAPPREADEAAVLERYRPWLDRLMGETGAGSADVIRIDVNTPNREALRAKFLSEHVHTEDEVRFFVHGAGHFVLHVDEHVYDVGCTQGDLISVPAGTPHWFDAGETPDVVALRIFTNRDGWIADYTGDDIALRFPARAA","length":181,"molWeight":20198,"crc64":"B88180D2DC479034","md5":"65DD24656CC1C71907B0046FCDB54C12"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Binding site":8,"Site":3},"uniParcId":"UPI00156B192D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JPS0","uniProtkbId":"A0ABX0JPS0_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84022.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN84022.1"}],"value":"GOB93_05110"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057572"}],"value":"Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = 2-methylserine + (6S)-5,6,7,8-tetrahydrofolate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:58275"}],"ecNumber":"2.1.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051216"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15481"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57453"}],"ecNumber":"2.1.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006376"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Belongs to the SHMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84022.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":131,"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":251,"modifier":"EXACT"},"end":{"value":251,"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":235,"modifier":"EXACT"},"end":{"value":235,"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":236,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84022.1"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84022.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84022.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000005","properties":[{"key":"ProteinId","value":"NHN84022.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173582420.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000005.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050413","properties":[{"key":"GoTerm","value":"F:D-alanine 2-hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00378","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000001","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00051","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"InterPro","id":"IPR001085","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase"}]},{"database":"InterPro","id":"IPR049943","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase-like"}]},{"database":"InterPro","id":"IPR019798","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase_PLP_BS"}]},{"database":"InterPro","id":"IPR039429","properties":[{"key":"EntryName","value":"SHMT-like_dom"}]},{"database":"NCBIfam","id":"NF000586","properties":[{"key":"EntryName","value":"PRK00011.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680:SF35","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00464","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000412","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00096","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDTDLHRFFGSSLGEVDADVASAIGDELVRQRDGIELIASENMVSRAVLEAQGSVLTNKYAEGYPGRRYYGGCVDVDKVEVLAIERVKQIFGAGFANVQPHSGANANQAAFMAVVAPGDTVLGMSLAAGGHLTHGAAPNYSGKWFNAVQYGVRRQDGLLDYDEMEALAREHKPKLIVAGSSAYPRVIDFVRFRKVADEVGAKLMVDMAHFAGLVAAGLYPSPLPYADVVTSTTHKTLRGPRGGLILTNDEALAKKINSAVFPGLQGGPLMHVIAAKAVAFGEALRPEFADYQKAVAANAKVLGEVLLERGFDLVTGGTDSHLLLVDLRPKKVTGKAAEKALERAGITANKNAVPFDPEKPAVTSGIRLGSPAATARGFSEAEFRAVGEMIDEVLTALAASGGEGDAAVENAVHERVKALCARFPIYK","length":428,"molWeight":45259,"crc64":"E54E84CB693B23F7","md5":"BE321ECC9ABDD1591BE8707EEF2BB009"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":1,"Modified residue":1},"uniParcId":"UPI00156BC100"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JQ28","uniProtkbId":"A0ABX0JQ28_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN85199.1"}],"value":"GOB93_11170"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85199.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":416,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"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":194,"modifier":"EXACT"},"end":{"value":194,"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":392,"modifier":"EXACT"},"end":{"value":392,"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":416,"modifier":"EXACT"},"end":{"value":419,"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":464,"modifier":"EXACT"},"end":{"value":464,"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":468,"modifier":"EXACT"},"end":{"value":468,"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":226,"modifier":"EXACT"},"end":{"value":226,"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":"NHN85199.1"}],"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":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85199.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000013","properties":[{"key":"ProteinId","value":"NHN85199.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173583580.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000013.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSMKLSSLLAAAGLSLPDGITNDPDIVSVTADSRAVTPGTLFVAVPGVKQDGRDFIPAAVQAGAAAVLAPEGTKPFDGVPMVTVGEPRRALALMAAVLAGPQPERIVAVTGTNGKTSTVDFLRQIWTGMGRQAASFGTLGLIAPEDVLSALPFEIPALTTPDPVTLARGLAALRGAGVTDVALEASSHGLDQRRLDGVRITAAGFTNLTRDHLDYHGDIDAYRTAKMRLFEMLLPDDGFAAANADMDRDTLEVLREITQRRGLELRLTGEKGDAVRLVAQKFLPEGQRLMLEAWGKPFDVTIALPGRFQADNVMLAAALAAADRDDMAAVIARLPHLQGVRGRMERAALLPSGAAVYVDYAHTPDALARVLDSLRPHAKGRLIVVFGAGGDRDRGKRPLMAHEAALRADAVIVTDDNPRSEDPAAIRKDVLLGAPEATEIGDRREAIAAGIGMLDAGDVLLVAGKGHEQGQTIAGVVHPFDDVSVVQSLVASA","length":493,"molWeight":51803,"crc64":"CF16B8A13C0CD9EC","md5":"D9022EA4266CFD5A8D2459C096D5B197"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI00156A7C66"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JQB3","uniProtkbId":"A0ABX0JQB3_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84666.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"2.7.1.71"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"3-dehydroquinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"DHQS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"4.2.3.4"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"aroB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"aroK"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84666.1"}],"value":"GOB93_08415"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"Catalyzes the conversion of 3-deoxy-D-arabino-heptulosonate 7-phosphate (DAHP) to dehydroquinate (DHQ)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21968"},{"database":"ChEBI","id":"CHEBI:32364"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58394"}],"ecNumber":"4.2.3.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001393"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + ATP = 3-phosphoshikimate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13121"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:145989"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048567"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}},{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"Binds 1 divalent metal cation per subunit. Can use either Co(2+) or Zn(2+)."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"NAD(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001911"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57540"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004661"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"value":"Belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005412"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"Belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84666.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01761"}]},{"type":"Domain","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":574,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24621"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":492,"modifier":"EXACT"},"end":{"value":492,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":510,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023285"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00109"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"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_00110"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"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_00109"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00110"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84666.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN84666.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000009","properties":[{"key":"ProteinId","value":"NHN84666.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173583064.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000009.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003856","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate 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:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009073","properties":[{"key":"GoTerm","value":"P:aromatic amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd08195","properties":[{"key":"EntryName","value":"DHQS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1970:FF:000001","properties":[{"key":"EntryName","value":"3-dehydroquinate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1090.10","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like - alpha domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00110","properties":[{"key":"EntryName","value":"DHQ_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00109","properties":[{"key":"EntryName","value":"Shikimate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050071","properties":[{"key":"EntryName","value":"Dehydroquinate_synthase"}]},{"database":"InterPro","id":"IPR016037","properties":[{"key":"EntryName","value":"DHQ_synth_AroB"}]},{"database":"InterPro","id":"IPR030960","properties":[{"key":"EntryName","value":"DHQS/DOIS_N"}]},{"database":"InterPro","id":"IPR056179","properties":[{"key":"EntryName","value":"DHQS_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"database":"InterPro","id":"IPR023000","properties":[{"key":"EntryName","value":"Shikimate_kinase_CS"}]},{"database":"NCBIfam","id":"TIGR01357","properties":[{"key":"EntryName","value":"aroB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010552","properties":[{"key":"EntryName","value":"PRK13946.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43622","properties":[{"key":"EntryName","value":"3-DEHYDROQUINATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43622:SF7","properties":[{"key":"EntryName","value":"3-DEHYDROQUINATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01761","properties":[{"key":"EntryName","value":"DHQ_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24621","properties":[{"key":"EntryName","value":"DHQS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01202","properties":[{"key":"EntryName","value":"SKI"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01100","properties":[{"key":"EntryName","value":"SHIKIMTKNASE"}]},{"database":"SUPFAM","id":"SSF56796","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-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":"PS01128","properties":[{"key":"EntryName","value":"SHIKIMATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSRPYSAERPEFPPAVPDPDADSATDAVASVRVADAVPSGVALSPSAPSSADPFPLNLDALRTSTGFGPLAGRSIVLIGLMGAGKSTIGRRLAQRLGLGFVDADAEIERAAGCSISDVFRMYGEGAFRDGERRVIRRLLDGPSRVLATGGGAFMNAETRAVIRERAISVWLRCPLDILVRRVAGRSHRPLLNHSRPRDVLERLITERHPVYAEADIIVQCGDDNVDNSTTRVIEALALNHRPRRLPVALDRASYDVVIGAGLIERAGALLAPVLPQKRVVVVTDATVAELWLPPLLESLGDSGFHVRTVVVPPGEKSKSLEEFGRVTDAILEQGVERRTTIIALGGGIVGDLAGFVAASTLRGLPFVQIPTTLLSQVDSSVGGKTGINTRWGKNLIGAFHQPAAVLADISTLATLPAREIRAGYAEIIKAGLIGDERFFAWCEMHGATVLSQEPEPLAEAVERACAFKAAVVTKDEFERSSEGGRALLNLGHTFGHALEAELGYDGRLLHGEAVSIGLRLAFLLSVRLGYCPQADLDRLTRHLESTGMPAWISDTGEAFAADTLLRHMTRDKKMHDGKLTFILVRGIGRAFTCRDVPEAAVRAVLIEEGCASDALQTPDNGRPK","length":624,"molWeight":66860,"crc64":"FD1CC97AB86969DE","md5":"B32AFEE7F0F315B5072D09F66E51CA31"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Binding site":14},"uniParcId":"UPI00156BC419"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JQE9","uniProtkbId":"A0ABX0JQE9_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85688.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN85688.1"}],"value":"GOB93_13700"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059148"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85688.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":533,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"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":354,"modifier":"EXACT"},"end":{"value":354,"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":382,"modifier":"EXACT"},"end":{"value":385,"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":405,"modifier":"EXACT"},"end":{"value":405,"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":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85688.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85688.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000019","properties":[{"key":"ProteinId","value":"NHN85688.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173584077.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000019.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTRFVFITGGVVSSLGKGIASAALAALLQSRGYKVRLRKLDPYLNVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFTGVNATRADNTTTGRIYSDVIARERRGDYLGGTVQVIPHITDAIKERVVADTEGLDFVLVEIGGTVGDIESLPFLESIRQLRNDLGVENTIVVHLTLLPWIPSAGELKTKPTQHSVKELQNVGLQPQILLCRCDRPIPDNERRKIANFCNVRPEAVIAARDVDTIYECPLSYHAEGLDTEVLRYFHLPFDKEPDLSAWRSIVDTIHEPEGEVRVGVVGKYTAMLDSYKSLSEALLHGGIANKVRVKLEWFESEEFEKSPETLKKLADMDAILVPGGFGERGSGGKIEAVRFARENNIPFLGICFGMQMAVIECARNLAGLPKASSTEFGPTSEPLVGLMTEWARGSEMLRRREGGELGGTMRLGGYPAKLAEGSRAAEIYGTTTIRERHRHRYEVNVHYRDRIETAGLKFSGMSPDGILPEVVEYPDHPWFMAVQYHPELISRPFAPHPLFSGFIGAANEKAKAGKKASA","length":548,"molWeight":60521,"crc64":"2BE4053D799D0B17","md5":"8A0F7BDD43C1F5D4FFB35C087D1622E0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":17},"uniParcId":"UPI00156B0865"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JQX7","uniProtkbId":"A0ABX0JQX7_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85410.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN85410.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85410.1"}],"value":"GOB93_12265"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85410.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"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":149,"modifier":"EXACT"},"end":{"value":149,"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":152,"modifier":"EXACT"},"end":{"value":152,"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":202,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"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":256,"modifier":"EXACT"},"end":{"value":258,"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":333,"modifier":"EXACT"},"end":{"value":333,"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85410.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85410.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000015","properties":[{"key":"ProteinId","value":"NHN85410.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173583795.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000015.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable 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":"MSDSAFAPDATDRERILAKSALFSPPPVQLADGRRELIGLSREEITEELISIGEKPFRTKQLWHWIYHQGVTDFSRMSSIAKPLQKKLAERFIVGRPEPAVVQTSKDETRKFLFRFRDGQEAETVYIPDRREDRGAVCISSQVGCTLSCTFCHTGTQKLVRNLGAAEIVGQFMAARDSYGEWPSPKGETPRLLSTIVLMGMGEPLYNYENVAKAMRIIMDGEGIALSRRRITLSTSGVVPLMDRCGDELGINLAVSLHAVRDDLRDQIVPLNRKYPIAEVLAACRRYPAASNARRITFEYIMLRDINDSEADARELVRLISGIPAKVNLIPFNPWPGSEYKPSTREQLAKFAKIVMDAGFASPIRMPRGRDILAACGQLKTESERQRPVRESV","length":393,"molWeight":44069,"crc64":"A18AF0E3E98F0DA6","md5":"4A249CF8F89AD85F32A3887D1A7045D2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI00156AD90B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JTT4","uniProtkbId":"A0ABX0JTT4_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86173.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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:0000313","source":"EMBL","id":"NHN86173.1"}],"value":"hflB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ftsH"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86173.1"}],"value":"GOB93_16205"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Multi-pass membrane protein","id":"SL-9909"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003651"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010044"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the C-terminal section; belongs to the peptidase M41 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the central section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86173.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":606,"modifier":"EXACT"},"end":{"value":643,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":606,"modifier":"EXACT"},"end":{"value":617,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":419,"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":423,"modifier":"EXACT"},"end":{"value":423,"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":497,"modifier":"EXACT"},"end":{"value":497,"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86173.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86173.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000027","properties":[{"key":"ProteinId","value":"NHN86173.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004222","properties":[{"key":"GoTerm","value":"F:metalloendopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19501","properties":[{"key":"EntryName","value":"RecA-like_FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.760:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.720.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.760","properties":[{"key":"EntryName","value":"Peptidase M41"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01458","properties":[{"key":"EntryName","value":"FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR041569","properties":[{"key":"EntryName","value":"AAA_lid_3"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR003960","properties":[{"key":"EntryName","value":"ATPase_AAA_CS"}]},{"database":"InterPro","id":"IPR005936","properties":[{"key":"EntryName","value":"FtsH"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011546","properties":[{"key":"EntryName","value":"Pept_M41_FtsH_extracell"}]},{"database":"InterPro","id":"IPR000642","properties":[{"key":"EntryName","value":"Peptidase_M41"}]},{"database":"InterPro","id":"IPR037219","properties":[{"key":"EntryName","value":"Peptidase_M41-like"}]},{"database":"NCBIfam","id":"TIGR01241","properties":[{"key":"EntryName","value":"FtsH_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076:SF97","properties":[{"key":"EntryName","value":"ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076","properties":[{"key":"EntryName","value":"METALLOPROTEASE M41 FTSH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17862","properties":[{"key":"EntryName","value":"AAA_lid_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06480","properties":[{"key":"EntryName","value":"FtsH_ext"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01434","properties":[{"key":"EntryName","value":"Peptidase_M41"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140990","properties":[{"key":"EntryName","value":"FtsH protease domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00674","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MINNFGRNLALWVCVIVLLLLLFNMFQPGSVQHATEQLPYSDFVADVDQGRVRSVTIQEHNVAGKLTDGTAFETYAPDDPRLVSRLTDKGVEVIAKPLEAEGNPFLRYLLNWSPFLVLIGLWFFMMRQMPSGGGRAMGFGKSRARMLTEKQGRVTFADVAGIDEAKAELEEIVEFLKDPQKFTRLGGKIPKGVLLVGPPGTGKTLLARAIAGEANVPFFTISGSDFVEMFVGVGASRVRDMFEQGKKAAPCIIFIDEIDAVGRHRGAGLGGGNDEREQTLNQMLVEMDGFESNEGVILIAATNRPDVLDPALLRPGRFDRQVVVPNPDVNGREQILRVHMRKVPLASDVDPKVIARGTPGFSGADLANLVNEAALLAARQGKRTVAMSEFENAKDKVLMGTERRSLVMSEDEKKMTAYHEGGHALVSILTPGTDPVHKATIIPRGRALGMVMSLPEGDRYSKSKFKCLAELDLAMGGRAAEEIIFGSENVCTGASGDIKMATDQARRMVTEWGMSEKLGMIAYGDNGQEVFLGHSVTQSKNVSEETAREIDAEVKKLIDAAYVRARTLLIDHIDELHRLAEALLEYETLSGEEIRQVLRGEPIERVEVDDAMPENRRSSVPPVIGKPGGRPVPPLEGASAQPG","length":643,"molWeight":70139,"crc64":"EFC6F623C2B3EAA7","md5":"1F76CFE2F938663FF8AD622B57299F56"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":2},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":4},"uniParcId":"UPI00156B2855"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JUS3","uniProtkbId":"A0ABX0JUS3_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85284.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN85284.1"}],"value":"GOB93_11610"}]}],"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"}]}},{"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85284.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00493"}]},{"type":"Active site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"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":668,"modifier":"EXACT"},"end":{"value":668,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":767,"modifier":"EXACT"},"end":{"value":767,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":25,"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":52,"modifier":"EXACT"},"end":{"value":52,"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":148,"modifier":"EXACT"},"end":{"value":148,"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":170,"modifier":"EXACT"},"end":{"value":170,"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":209,"modifier":"EXACT"},"end":{"value":209,"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":214,"modifier":"EXACT"},"end":{"value":214,"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85284.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85284.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000014","properties":[{"key":"ProteinId","value":"NHN85284.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173583672.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000014.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO: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":"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"}]}],"sequence":{"value":"MNATPSVGKSPLRDLEKFDQSPWLDFVRRGYTRDGSMEKLITEDGVKGVTSNPTIFQKAMGEGTDYDAQMKDILAHDIVSAGQLYERLAITDIQEVARLLKPVFDATKGVDGYVSLEVSPYLARDTQGTEHEAARLWKAVHEPNLMIKIPGTDEGVPAIEKSIADGINTNVTLLFSLNAYKKVVEAWLSGLEARLKAGEKVSGVASVASFFVSRIDGKIDAEIDRRVKAGDAESKALSAIRGKVAIANAKMAYQYWLGVMKSDRWAKLKAAGAQPQRLLWASTGTKDKAYSDVLYLEELIGPETVNTIPPVTLDAFRDHGKLRASLTENVAEAEAVMKEAERLGLDLEGVTRTLVDEGVASFADAFDGLLGSVGAKQNAILGKKLTETKLSLPAAFDEAVKKGLDTWRKAGLIRKLWARDASVWTNSDESKWLKWLDIADDRYAHLKELEAFQAEVKARGFKQILLLGMGGSSLGPEVLAETFGRHDGFPHLYVLDSTDPQQVRTFEKKIDPAHTLFIVSSKSGSTLEPNIMLAYFFDVAKKALGEKAGQHFVAVTDPGSKLEALAKKDGFWKVFSGEKQIGGRYSVLSNFGMVPAAASGVPLKLFLEDALHGVRACDSSVPPAINPGVLLGAVFGVGATEFGRDKITIIATKQVADFGAWAEQLIAESTGKSGKGLIPIDDETLAGPKHYGKDRLFIYFRLVSEHSHEQDEAVRTLIDAGEPVVTIDLHDRRQIAQEFFRWEIATAVAGAYLKINPFDQPDVEASKIETKKLTAAYNETGHLPEEAPFATDGDLAFFADPKNAAAVKGESAQAVLKAHFGRVKAGDYVGLLAYIERDRATIEWIQHTRLAIRDAKTVATAAEFGPRFLHSTGQAYKGGPDTGVFLQITADDAHDLPVPGERYSFGVVKAAQARGDFDVLAERGRRALRVHIKGDLKTGLAALASAIRAAL","length":951,"molWeight":103363,"crc64":"E71B2F6E9C51B8CE","md5":"EB618881E8973A5C05739C9AD2F7CEBD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Active site":4,"Binding site":6},"uniParcId":"UPI00156AADE6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JV00","uniProtkbId":"A0ABX0JV00_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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:0000256","source":"HAMAP-Rule","id":"MF_01603"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85702.1"}],"value":"hldE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85702.1"}],"value":"GOB93_13770"}]}],"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":"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85702.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Domain","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"Cytidyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01467"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"Ribokinase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Region","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"Cytidylyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Active site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":198,"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":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN85702.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000019","properties":[{"key":"ProteinId","value":"NHN85702.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173584089.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000019.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO: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":"FunFam","id":"3.40.1190.20:FF:000002","properties":[{"key":"EntryName","value":"Bifunctional protein HldE"},{"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":"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":"NF008454","properties":[{"key":"EntryName","value":"hldE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02198","properties":[{"key":"EntryName","value":"rfaE_dom_I"},{"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":"MDFSRITVLCVGDVMLDRFVYGDMERISPEAPVPVLLLNKRTEMPGGAGNVASNVISLGGRAILIGLVGEDDAAITLRDTLRLRAQVSEMLVPTPRRPTICKTRFIAAHQQVVRADEESRLPLQADEAELLCQAIDARLEEADVVILSDYGKGVCDQMVVHHLIGEARLRDIPVFVDPKTPDFRHYRGATCITPNVKELAAASGMPVSDNASVEAAARKVMARAEADAILATRSEKGMMLVPAEGEAIAVPARAREVFDVSGAGDTVIATMALAVGSGMAFDQAMRIANAAAGVVVAKLGTATADIGEVMRELQAQDEPEEAPHLLTLTQAKMQVADWKAHGLTVGFTNGCFDIIHPGHISLLAAARSACDRLIVALNDDASVRRLKGDTRPVNTLASRAAVMAAIRSVDAVAAFSEDTPLEIIRELMPDILIKGSDYRPEDVVGAAEVIAAGGRLVLADLRDGHSTTATIGRIQGL","length":477,"molWeight":50712,"crc64":"ACC7448453831C37","md5":"4AE06A32F0D82DE5BDBC1B495F560EE4"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":1},"uniParcId":"UPI00156B6694"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JWI7","uniProtkbId":"A0ABX0JWI7_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86212.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"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":"NHN86212.1"}],"value":"cysC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86212.1"}],"value":"GOB93_16415"}]}],"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86212.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"Tr-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51722"}]},{"type":"Region","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"G1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"G2","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"G3","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"G4","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"G5","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Active site","location":{"start":{"value":539,"modifier":"EXACT"},"end":{"value":539,"modifier":"EXACT"}},"description":"Phosphoserine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]},{"type":"Binding site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":472,"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":"NHN86212.1"}],"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":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"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":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86212.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86212.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000028","properties":[{"key":"ProteinId","value":"NHN86212.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173584588.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000028.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"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":"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":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"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":"IPR005225","properties":[{"key":"EntryName","value":"Small_GTP-bd"}]},{"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":"NF003013","properties":[{"key":"EntryName","value":"PRK03846.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00231","properties":[{"key":"EntryName","value":"small_GTP"},{"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":"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":"MSETLTATTVIDPIDRDVALESATPIVIVGHVDHGKSTLIGRLLYDTDNLEEGKVAQIIESSKKRGLTIEWSFLLDSLQIERDQGVTVDSTRIPFRLGNRQFVIVDAPGHRQFLRNMITGAADADAAVLVVDANEGAQEQTRRHAMLLRLIGIRHIIVLLNKVDLLNFDEQKVRAVEQSVTSLLAQLDLTPSLFIPASARDGDNIASRSERSPWYKGPILTEALAEVPDGNIRATLPFRLPVQDVYRFDDKRYVVGRIERGVVRVGDELSIGSQNGTARVASIERWSAPVRDEAAAGESVALVLEPDVIPARGDFLYSPHQAPEKSARIRANLFWLRQEPLRAGETFRLRLATAEHQVTVASIDSVLRLDDLTEQQADEVGPEGFAEITLVAGEAIQFDPFSPGTSDGRGVLVDRNQRIVGGAPLLGPATVAAGSHAIHPSGGEVSTGERARGKGHKACVIWLTGLSGAGKSTIARLAERKLYSDGIDAYVLDGDTLRMGLCSDLGFTEADRHENVRRAAEVAKILAQTGQVVLVALISPLRADRALARKIIGEEFEEVFIDTSLATCEERDSKGLYRAAREGKIENFTGISAPYEAPEKPDLHIAADKGDAGQNATKLTDYILSKVR","length":628,"molWeight":68322,"crc64":"42345FA0C84E4371","md5":"33B1065CEE7E35E894394E9797628E05"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":5,"Active site":1,"Binding site":1},"uniParcId":"UPI00156BB149"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JZ37","uniProtkbId":"A0ABX0JZ37_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"4: Predicted","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044985"}],"value":"Lysosomal dipeptide transporter MFSD1"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045018"}],"value":"Major facilitator superfamily domain-containing protein 1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86769.1"}],"value":"GOB93_19410"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045709"}],"value":"Lysosomal dipeptide uniporter that selectively exports lysine, arginine or histidine-containing dipeptides with a net positive charge from the lysosome lumen into the cytosol. Could play a role in a specific type of protein O-glycosylation indirectly regulating macrophages migration and tissue invasion. Also essential for liver homeostasis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanyl-L-lysine(out) = L-alanyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79415"},{"database":"ChEBI","id":"CHEBI:192470"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044919"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-arginine(out) = L-alpha-aminoacyl-L-arginine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79367"},{"database":"ChEBI","id":"CHEBI:229968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044881"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-histidine(out) = L-alpha-aminoacyl-L-histidine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79375"},{"database":"ChEBI","id":"CHEBI:229967"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044884"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alpha-aminoacyl-L-lysine(out) = L-alpha-aminoacyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79383"},{"database":"ChEBI","id":"CHEBI:229966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044893"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-L-alpha-amino acid(out) = L-arginyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79371"},{"database":"ChEBI","id":"CHEBI:84315"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044899"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-arginyl-glycine(out) = L-arginyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79391"},{"database":"ChEBI","id":"CHEBI:229955"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044903"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-L-lysine(out) = L-aspartyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79411"},{"database":"ChEBI","id":"CHEBI:229953"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044898"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-L-alpha-amino acid(out) = L-histidyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79379"},{"database":"ChEBI","id":"CHEBI:229964"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044912"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-glycine(out) = L-histidyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79395"},{"database":"ChEBI","id":"CHEBI:229957"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044878"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alanine(out) = L-lysyl-L-alanine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79399"},{"database":"ChEBI","id":"CHEBI:229954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044876"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-alpha-amino acid(out) = L-lysyl-L-alpha-amino acid(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79387"},{"database":"ChEBI","id":"CHEBI:229965"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044891"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-L-lysine(out) = L-lysyl-L-lysine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79403"},{"database":"ChEBI","id":"CHEBI:229956"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044900"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-glycine(out) = L-lysyl-glycine(in)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:79407"},{"database":"ChEBI","id":"CHEBI:191202"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044924"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00046376"}],"value":"Homodimer. Interacts with lysosomal protein GLMP (via lumenal domain); the interaction starts while both proteins are still in the endoplasmic reticulum and is required for stabilization of MFSD1 in lysosomes but has no direct effect on its targeting to lysosomes or transporter activity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86769.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Major facilitator superfamily (MFS) profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50850"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023228"}],"id":"KW-0458","category":"Cellular component","name":"Lysosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN86769.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000051","properties":[{"key":"ProteinId","value":"NHN86769.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173585086.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000051.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0022857","properties":[{"key":"GoTerm","value":"F:transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06174","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1250.20","properties":[{"key":"EntryName","value":"MFS general substrate transporter like domains"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR011701","properties":[{"key":"EntryName","value":"MFS"}]},{"database":"InterPro","id":"IPR020846","properties":[{"key":"EntryName","value":"MFS_dom"}]},{"database":"InterPro","id":"IPR036259","properties":[{"key":"EntryName","value":"MFS_trans_sf"}]},{"database":"InterPro","id":"IPR052187","properties":[{"key":"EntryName","value":"MFSD1"}]},{"database":"InterPro","id":"IPR005829","properties":[{"key":"EntryName","value":"Sugar_transporter_CS"}]},{"database":"PANTHER","id":"PTHR23512","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23512:SF3","properties":[{"key":"EntryName","value":"MAJOR FACILITATOR SUPERFAMILY DOMAIN-CONTAINING PROTEIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07690","properties":[{"key":"EntryName","value":"MFS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF103473","properties":[{"key":"EntryName","value":"MFS general substrate transporter"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50850","properties":[{"key":"EntryName","value":"MFS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00216","properties":[{"key":"EntryName","value":"SUGAR_TRANSPORT_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPPINSPARSPASTAAPAGTPAPQPQKLQPLYVLAWFLCALFYFYQYAIRSAPGIMQNELTAAWGNSHLGLMIASYYIVYALMALVVGVLLDRYGAHAVLPGFIAITGMGCLIFAQGSAAAGVGGYIIQAIGAICAFVGASYVAARYLPARTLALFVGLTQCLGMAGAAFGSKPTRMLIDPQGSWHVSWEHIWLGFGIIGLALAAAVWVIMPRDSGDSARHHGPLTAANLLNPFKIIFSNPQSWCAGIIGGLLFVPTTIGALGWGASMLSSGEHTTMAFAASDVSMVPIGWVIGCPLLGWISDKIGRRKPVLLGGAVLLLAASLCALFVPVGIMPKYLVALIMGIASGAAMIPFSSMKEVNPPQVKGTAAGVMNFLVFGTTGVMSPLVSALMGKGTVLTMAQYREAFMPLIIGIVIAIGLSFFLRETGWAARKA","length":434,"molWeight":45436,"crc64":"8C4FEC1DF32C5BA6","md5":"620633D4243EF19C79250DCDFC4CCFE0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":13,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":12,"Domain":1,"Region":1,"Compositional bias":1},"uniParcId":"UPI00156B9388"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JGI4","uniProtkbId":"A0ABX0JGI4_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83039.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"value":"Aconitate hydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"value":"Aconitase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"value":"4.2.1.3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83039.1"}],"value":"acnA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83039.1"}],"value":"GOB93_00025"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"value":"Catalyzes the isomerization of citrate to isocitrate via cis-aconitate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002737"}],"value":"Involved in the catabolism of short chain fatty acids (SCFA) via the tricarboxylic acid (TCA)(acetyl degradation route) and probably the 2-methylcitrate cycle I (propionate degradation route). Catalyzes the reversible isomerization of citrate to isocitrate via cis-aconitate. Could catalyze the hydration of 2-methyl-cis-aconitate to yield (2R,3S)-2-methylisocitrate. The apo form of AcnA functions as a RNA-binding regulatory protein"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-aconitate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17941"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:57429"},{"database":"ChEBI","id":"CHEBI:57872"}],"ecNumber":"4.2.1.99","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000118"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"citrate = D-threo-isocitrate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10336"},{"database":"ChEBI","id":"CHEBI:15562"},{"database":"ChEBI","id":"CHEBI:16947"}],"ecNumber":"4.2.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023501"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001966"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004717"}],"value":"Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate from oxaloacetate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005026"}],"value":"Organic acid metabolism; propanoate degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007185"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"value":"Belongs to the aconitase/IPM isomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83039.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":565,"modifier":"EXACT"}},"description":"Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00330"}]},{"type":"Domain","location":{"start":{"value":697,"modifier":"EXACT"},"end":{"value":824,"modifier":"EXACT"}},"description":"Aconitase A/isopropylmalate dehydratase small subunit swivel","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00694"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU361275"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022532"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83039.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83039.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000001","properties":[{"key":"ProteinId","value":"NHN83039.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581575.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000001.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0047456","properties":[{"key":"GoTerm","value":"F:2-methylisocitrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0003994","properties":[{"key":"GoTerm","value":"F:aconitate hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd01586","properties":[{"key":"EntryName","value":"AcnA_IRP"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01580","properties":[{"key":"EntryName","value":"AcnA_IRP_Swivel"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.19.10:FF:000001","properties":[{"key":"EntryName","value":"Aconitate hydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.499.10:FF:000002","properties":[{"key":"EntryName","value":"Aconitate hydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.499.10:FF:000020","properties":[{"key":"EntryName","value":"Aconitate hydratase A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.190.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.499.10","properties":[{"key":"EntryName","value":"Aconitase, domain 3"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.20.19.10","properties":[{"key":"EntryName","value":"Aconitase, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR044137","properties":[{"key":"EntryName","value":"AcnA_IRP_Swivel"}]},{"database":"InterPro","id":"IPR015931","properties":[{"key":"EntryName","value":"Acnase/IPM_dHydase_lsu_aba_1/3"}]},{"database":"InterPro","id":"IPR001030","properties":[{"key":"EntryName","value":"Acoase/IPM_deHydtase_lsu_aba"}]},{"database":"InterPro","id":"IPR015928","properties":[{"key":"EntryName","value":"Aconitase/3IPM_dehydase_swvl"}]},{"database":"InterPro","id":"IPR006249","properties":[{"key":"EntryName","value":"Aconitase/IRP2"}]},{"database":"InterPro","id":"IPR018136","properties":[{"key":"EntryName","value":"Aconitase_4Fe-4S_BS"}]},{"database":"InterPro","id":"IPR036008","properties":[{"key":"EntryName","value":"Aconitase_4Fe-4S_dom"}]},{"database":"InterPro","id":"IPR000573","properties":[{"key":"EntryName","value":"AconitaseA/IPMdHydase_ssu_swvl"}]},{"database":"NCBIfam","id":"NF006757","properties":[{"key":"EntryName","value":"acnA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009520","properties":[{"key":"EntryName","value":"acnA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01341","properties":[{"key":"EntryName","value":"aconitase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11670","properties":[{"key":"EntryName","value":"ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00330","properties":[{"key":"EntryName","value":"Aconitase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00694","properties":[{"key":"EntryName","value":"Aconitase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00415","properties":[{"key":"EntryName","value":"ACONITASE"}]},{"database":"SUPFAM","id":"SSF53732","properties":[{"key":"EntryName","value":"Aconitase iron-sulfur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52016","properties":[{"key":"EntryName","value":"LeuD/IlvD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00450","properties":[{"key":"EntryName","value":"ACONITASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01244","properties":[{"key":"EntryName","value":"ACONITASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKAVGHDSLKTGRELKVDGKTYHYFSIPEAEKTIGDVSRLPVSLKVLLENILRFEDGRSYTQDDARKIAAWLPKGSSTKEVPFKPSRILMQDFTGVPGVVDLAAMRDGIVELKGNPDKVNPLVPVNLVIDHSVMVDVYGTKDALQENITIEFDRNGERYAFLRWGQEAFKNFSVVPPDTGICHQVNLEHIAQVAWTAEVGGKEYVYPDTLFGTDSHTTMVNGLGVLGWGVGGIEAEAAMLGQPIAMLIPDVIGFRLTGKLPEGATATDLVLTVTQMLRKKGVVGKFVEFFGPALDHLPVADRATIANMAPEYGATCGFFPVDKLTLDYLHETGRDAHRLKLVEEYYKAQGMFRTSETAEPVFTSTLELDLSTVVPSISGPKRPQDRVVLTDATSAFEKELVSGLGVPANDIDKKAKVAGTNYEIGHGDVVIAAITSCTNTSNPAVLIAAGLVARKARALGLKPKPWVKTSLAPGSQVVTDYLNRANLTEDLDALGFNTVGYGCTTCIGNSGPLADNIVDAIEGNNKLVAVSVLSGNRNFEGRISPNVRANYLASPPLVVAYSLLGTMRKDITKEPLGTSKDGKPVYLKDIWPTNKEIAALIGSSINREEFIKRYKDVSKGTKEWQDLKVATGSETYKWDPKSTYVQDPPYFKHMSAEPAAGGGDINGARVLALLGDNITTDHISPAGSIKKDSPAGKYLIEHGVQPKDFNSYGSRRGNDRIMVRGTFANIRIKNEMLPGTEGGLSKHFPDGKEGFIYDVAMEYKKEHVPLVVFGGKEYGMGSSRDWAAKGTLLLGIKAVIAESFERIHRSNLVGMGVLPLLFKEGTTRKTLGLKGDEVIDIKGLEKITPRMDVTMVIHRADGKTEEVPLLCRIDTLDEVEYYRHGGILHYVLRGMLKAA","length":899,"molWeight":97937,"crc64":"167FE596F818DF4C","md5":"411C08E012D4D93D5BFDB44B36E1CEA4"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2},"uniParcId":"UPI00156B4229"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JI01","uniProtkbId":"A0ABX0JI01_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"S-adenosylmethionine decarboxylase proenzyme"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"AdoMetDC"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"SAMDC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"4.1.1.50"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"S-adenosylmethionine decarboxylase beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"S-adenosylmethionine decarboxylase alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83371.1"}],"value":"speD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"speH"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83371.1"}],"value":"GOB93_01790"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-adenosyl-L-methionine + H(+) = S-adenosyl 3-(methylsulfanyl)propylamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15981"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57443"},{"database":"ChEBI","id":"CHEBI:59789"}],"ecNumber":"4.1.1.50","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83371.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"S-adenosylmethionine decarboxylase beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"featureId":"PRO_5044930037"},{"type":"Chain","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"S-adenosylmethionine decarboxylase alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"featureId":"PRO_5044930036"},{"type":"Active site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Active site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Proton acceptor; for processing activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Active site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Proton donor; for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Modified residue","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022813"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0068","category":"PTM","name":"Autocatalytic cleavage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023115"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0620","category":"Biological process","name":"Polyamine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023066"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0745","category":"Biological process","name":"Spermidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83371.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000002","properties":[{"key":"ProteinId","value":"NHN83371.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581809.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000002.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004014","properties":[{"key":"GoTerm","value":"F:adenosylmethionine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008295","properties":[{"key":"GoTerm","value":"P:spermidine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.160.750","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.360.110","properties":[{"key":"EntryName","value":"S-adenosylmethionine decarboxylase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00464","properties":[{"key":"EntryName","value":"AdoMetDC_1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR042286","properties":[{"key":"EntryName","value":"AdoMetDC_C"}]},{"database":"InterPro","id":"IPR003826","properties":[{"key":"EntryName","value":"AdoMetDC_fam_prok"}]},{"database":"InterPro","id":"IPR042284","properties":[{"key":"EntryName","value":"AdoMetDC_N"}]},{"database":"InterPro","id":"IPR016067","properties":[{"key":"EntryName","value":"S-AdoMet_deCO2ase_core"}]},{"database":"InterPro","id":"IPR017716","properties":[{"key":"EntryName","value":"S-AdoMet_deCOase_pro-enz"}]},{"database":"NCBIfam","id":"TIGR03330","properties":[{"key":"EntryName","value":"SAM_DCase_Bsu"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33866","properties":[{"key":"EntryName","value":"S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR33866:SF2","properties":[{"key":"EntryName","value":"S-ADENOSYLMETHIONINE DECARBOXYLASE PROENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02675","properties":[{"key":"EntryName","value":"AdoMet_dc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56276","properties":[{"key":"EntryName","value":"S-adenosylmethionine decarboxylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNALAQLGMVSELPSNNQISPVASYCEDERKDYFVERDGEKFAGTHLLIDLWEASNLDDPEKIDATLCEAAIAAGATILHSHFHHFTPNGGVSGVVVLAESHISIHTWPERSFAAVDIFMCGACDPNLSIPVMQRLFQAGRILVDEQRRGKVSL","length":154,"molWeight":16891,"crc64":"CFB1B1F4862D7C46","md5":"F1C4F1A71C583BD4790DCFE96AC04DC8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Active site":3,"Site":1,"Modified residue":1},"uniParcId":"UPI00156ABBF3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JI20","uniProtkbId":"A0ABX0JI20_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83386.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"ADP-L-glycero-D-manno-heptose-6-epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"5.1.3.20"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"ADP-L-glycero-beta-D-manno-heptose-6-epimerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"ADP-glyceromanno-heptose 6-epimerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"ADP-hep 6-epimerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"AGME"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83386.1"}],"value":"rfaD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"hldD"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83386.1"}],"value":"GOB93_01875"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"Catalyzes the interconversion between ADP-D-glycero-beta-D-manno-heptose and ADP-L-glycero-beta-D-manno-heptose via an epimerization at carbon 6 of the heptose"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ADP-D-glycero-beta-D-manno-heptose = ADP-L-glycero-beta-D-manno-heptose","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17577"},{"database":"ChEBI","id":"CHEBI:59967"},{"database":"ChEBI","id":"CHEBI:61506"}],"ecNumber":"5.1.3.20","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"NADP(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58349"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"Binds 1 NADP(+) per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"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 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"Homopentamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"Contains a large N-terminal NADP-binding domain, and a smaller C-terminal substrate-binding domain"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"Belongs to the NAD(P)-dependent epimerase/dehydratase family. HldD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83386.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"NAD-dependent epimerase/dehydratase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01370"}]},{"type":"Active site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}]},{"type":"Active site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01601"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83386.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83386.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000002","properties":[{"key":"ProteinId","value":"NHN83386.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581823.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000002.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008712","properties":[{"key":"GoTerm","value":"F:ADP-glyceromanno-heptose 6-epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"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":"cd05248","properties":[{"key":"EntryName","value":"ADP_GME_SDR_e"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.25.10","properties":[{"key":"EntryName","value":"UDP-galactose 4-epimerase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01601","properties":[{"key":"EntryName","value":"Heptose_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001509","properties":[{"key":"EntryName","value":"Epimerase_deHydtase"}]},{"database":"InterPro","id":"IPR011912","properties":[{"key":"EntryName","value":"Heptose_epim"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR02197","properties":[{"key":"EntryName","value":"heptose_epim"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43103:SF3","properties":[{"key":"EntryName","value":"ADP-L-GLYCERO-D-MANNO-HEPTOSE-6-EPIMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43103","properties":[{"key":"EntryName","value":"NUCLEOSIDE-DIPHOSPHATE-SUGAR EPIMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01370","properties":[{"key":"EntryName","value":"Epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIIVTGGAGFIGSCLVAALCDRGLDVVVVDWLGDTGKWRNLRNHPLVRIVPPDDLESLLGSASDVEAVFHMGAISSTTAHDGDLVWATNVALSETLWDWCARQGVRFIYASSAATYGAADRPELFSDDPKRLGTLKPLNLYGWSKHVFDLHVQARLDRGGMRPPQWAGLKFFNVYGPNEYHKGGMVSVVKVKYDEVHAGGAARLFRSDQAEIADGEQVRDFIWVGDVVKVLLWFLDNPGVDGLFNCGTGAARSYRHLAQAVCLAAGVPERIEFIDMPESLRGQYQSFTRADMSRLRAAGYTEPFVSLEEGIGLYVREYLSKSDPYL","length":326,"molWeight":35934,"crc64":"A1B53C3F48E43D64","md5":"1DB0597BFB790DE5995E967331A634D5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":12},"uniParcId":"UPI00156B109B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JI90","uniProtkbId":"A0ABX0JI90_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83363.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Phosphopantetheine adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"2.7.7.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Dephospho-CoA pyrophosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Pantetheine-phosphate adenylyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"PPAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83363.1"}],"value":"coaD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83363.1"}],"value":"GOB93_01745"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Reversibly transfers an adenylyl group from ATP to 4'-phosphopantetheine, yielding dephospho-CoA (dPCoA) and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantetheine + ATP + H(+) = 3'-dephospho-CoA + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19801"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57328"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"2.7.7.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029346"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 4/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"value":"Belongs to the bacterial CoaD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83363.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Cytidyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01467"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022993"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0173","category":"Biological process","name":"Coenzyme A biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00151"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"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_00151"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83363.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83363.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000002","properties":[{"key":"ProteinId","value":"NHN83363.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581803.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000002.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004595","properties":[{"key":"GoTerm","value":"F:pantetheine-phosphate adenylyltransferase 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":"CDD","id":"cd02163","properties":[{"key":"EntryName","value":"PPAT"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00151","properties":[{"key":"EntryName","value":"PPAT_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004821","properties":[{"key":"EntryName","value":"Cyt_trans-like"}]},{"database":"InterPro","id":"IPR001980","properties":[{"key":"EntryName","value":"PPAT"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR01510","properties":[{"key":"EntryName","value":"coaD_prev_kdtB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00125","properties":[{"key":"EntryName","value":"cyt_tran_rel"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21342","properties":[{"key":"EntryName","value":"PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21342:SF1","properties":[{"key":"EntryName","value":"PHOSPHOPANTETHEINE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01467","properties":[{"key":"EntryName","value":"CTP_transf_like"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01020","properties":[{"key":"EntryName","value":"LPSBIOSNTHSS"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPEAARRVGFYPGTFDPVTFGHMDIIERAARLVDRLVIGVAKNAGKNPLLSVDERVAALRDEVPGLVARTGAEIEVVAFDELLVEAVRRQKATLIFRGLRLLVDFDYEAQMQGANRKLAPEIETVFLMATERTQFISSHMVREIAAYGGNISEFAPDGACRRVVARFAR","length":169,"molWeight":18748,"crc64":"B876FD884D533BBE","md5":"C4F721D520F5569901D018FD17297A37"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":9,"Site":1},"uniParcId":"UPI00156B35D0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JIG7","uniProtkbId":"A0ABX0JIG7_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83423.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"1-deoxy-D-xylulose 5-phosphate reductoisomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"DXP reductoisomerase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"1.1.1.267"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"1-deoxyxylulose-5-phosphate reductoisomerase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"2-C-methyl-D-erythritol 4-phosphate synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"dxr"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83423.1"}],"value":"GOB93_02060"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"Catalyzes the NADPH-dependent rearrangement and reduction of 1-deoxy-D-xylulose-5-phosphate (DXP) to 2-C-methyl-D-erythritol 4-phosphate (MEP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-C-methyl-D-erythritol 4-phosphate + NADP(+) = 1-deoxy-D-xylulose 5-phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13717"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57792"},{"database":"ChEBI","id":"CHEBI:58262"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.267","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048543"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:13719"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048543"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005094"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 1/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"value":"Belongs to the DXR family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83423.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"1-deoxy-D-xylulose 5-phosphate reductoisomerase","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5050481475"},{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"1-deoxy-D-xylulose 5-phosphate reductoisomerase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02670"}]},{"type":"Domain","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"1-deoxy-D-xylulose 5-phosphate reductoisomerase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08436"}]},{"type":"Domain","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"DXP reductoisomerase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13288"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":38,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57783"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"NADPH","id":"ChEBI:CHEBI:57783"}},{"type":"Binding site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57792"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"1-deoxy-D-xylulose 5-phosphate","id":"ChEBI:CHEBI:57792"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Lipidation","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"id":"KW-0414","category":"Biological process","name":"Isoprene biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00183"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83423.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83423.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000002","properties":[{"key":"ProteinId","value":"NHN83423.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581853.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000002.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030604","properties":[{"key":"GoTerm","value":"F:1-deoxy-D-xylulose-5-phosphate reductoisomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070402","properties":[{"key":"GoTerm","value":"F:NADPH binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019288","properties":[{"key":"GoTerm","value":"P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.720:FF:000045","properties":[{"key":"EntryName","value":"1-deoxy-D-xylulose 5-phosphate reductoisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1740.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00183","properties":[{"key":"EntryName","value":"DXP_reductoisom"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003821","properties":[{"key":"EntryName","value":"DXP_reductoisomerase"}]},{"database":"InterPro","id":"IPR013644","properties":[{"key":"EntryName","value":"DXP_reductoisomerase_C"}]},{"database":"InterPro","id":"IPR013512","properties":[{"key":"EntryName","value":"DXP_reductoisomerase_N"}]},{"database":"InterPro","id":"IPR026877","properties":[{"key":"EntryName","value":"DXPR_C"}]},{"database":"InterPro","id":"IPR036169","properties":[{"key":"EntryName","value":"DXPR_C_sf"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00243","properties":[{"key":"EntryName","value":"Dxr"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30525","properties":[{"key":"EntryName","value":"1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30525:SF0","properties":[{"key":"EntryName","value":"1-DEOXY-D-XYLULOSE 5-PHOSPHATE REDUCTOISOMERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08436","properties":[{"key":"EntryName","value":"DXP_redisom_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02670","properties":[{"key":"EntryName","value":"DXP_reductoisom"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13288","properties":[{"key":"EntryName","value":"DXPR_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006205","properties":[{"key":"EntryName","value":"Dxp_reductismrs"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69055","properties":[{"key":"EntryName","value":"1-deoxy-D-xylulose-5-phosphate reductoisomerase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKTVTVLGCTGSIGCSTVDLLHQAGEGVSVKALVGGRNVALLAEQAKALRAEMAVIADEQALPELKALLAGTGIAVSAGRSAVIEAAGVPADWTMAAITGAAGLEPTLAAVRNGRAIALANKEALVCAGDVMLRAVKEAGATLLPVDSEHNAVFQAMADRQENQVGKIILTASGGPFRTATTAEMEAATPAQALKHPTWSMGAKISIDSASMFNKGLEVIEAARIFGLPEDRIDVLVHPQSVVHGMVQYTDGSLIAQMGSADMRIPIAHCLAWPQRMATTSPQLDLATFGTLVFEAPDPVRFPALRLARQALREGGAASTVLSAANEIAVEAFLGGQIGFLDIPRLVEAVMDRLGAPPIDTLEAVLHWDNEARIAAQGYIAKQAA","length":385,"molWeight":40003,"crc64":"BE3C5A7DD43C19F0","md5":"4C6C0AF7042C5E3C56738C0669DE82EA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":1,"Domain":3,"Binding site":22,"Lipidation":2},"uniParcId":"UPI00156B2056"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABX0JII5","uniProtkbId":"A0ABX0JII5_9PROT","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Acetobacter musti","taxonId":864732,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Acetobacterales","Acetobacteraceae","Acetobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Acetylglutamate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"2.7.2.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"N-acetyl-L-glutamate 5-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"NAG kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"NAGK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83438.1"}],"value":"argB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83438.1"}],"value":"GOB93_02135"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-L-glutamate + ATP = N-acetyl-L-glutamyl 5-phosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14629"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:57936"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004828"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Belongs to the acetylglutamate kinase family. ArgB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83438.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"Aspartate/glutamate/uridylate kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00696"}]},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":37,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}]},{"type":"Site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"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_00082"}],"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_00082"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"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_00082"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"33052084","citationType":"journal article","authors":["Sombolestani A.S.","Cleenwerck I.","Cnockaert M.","Borremans W.","Wieme A.D.","De Vuyst L.","Vandamme P."],"citationCrossReferences":[{"database":"PubMed","id":"33052084"}],"title":"Novel acetic acid bacteria from cider fermentations: Acetobacter conturbans sp. nov. and Acetobacter fallax sp. nov.","publicationDate":"2020","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}],"value":"LMG 30640","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"NHN83438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000635278"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WOTB01000002","properties":[{"key":"ProteinId","value":"NHN83438.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_173581866.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WOTB01000002.1"}]},{"database":"Proteomes","id":"UP000635278","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003991","properties":[{"key":"GoTerm","value":"F:acetylglutamate 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:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd04250","properties":[{"key":"EntryName","value":"AAK_NAGK-C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1160.10:FF:000004","properties":[{"key":"EntryName","value":"Acetylglutamate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1160.10","properties":[{"key":"EntryName","value":"Acetylglutamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00082","properties":[{"key":"EntryName","value":"ArgB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036393","properties":[{"key":"EntryName","value":"AceGlu_kinase-like_sf"}]},{"database":"InterPro","id":"IPR004662","properties":[{"key":"EntryName","value":"AcgluKinase_fam"}]},{"database":"InterPro","id":"IPR037528","properties":[{"key":"EntryName","value":"ArgB"}]},{"database":"InterPro","id":"IPR001048","properties":[{"key":"EntryName","value":"Asp/Glu/Uridylate_kinase"}]},{"database":"InterPro","id":"IPR001057","properties":[{"key":"EntryName","value":"Glu/AcGlu_kinase"}]},{"database":"InterPro","id":"IPR041727","properties":[{"key":"EntryName","value":"NAGK-C"}]},{"database":"NCBIfam","id":"TIGR00761","properties":[{"key":"EntryName","value":"argB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23342","properties":[{"key":"EntryName","value":"N-ACETYLGLUTAMATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23342:SF0","properties":[{"key":"EntryName","value":"N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00696","properties":[{"key":"EntryName","value":"AA_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000728","properties":[{"key":"EntryName","value":"NAGK"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00474","properties":[{"key":"EntryName","value":"GLU5KINASE"}]},{"database":"SUPFAM","id":"SSF53633","properties":[{"key":"EntryName","value":"Carbamate kinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDKGLSPVGDAMQQAATLAGALPYLRRYAGDTIVVKYGGHAMGNAELAKGFGSDIGLLKLIGINPIVVHGGGPQINSMLERLQVRSHFVDGLRVTDESAIDIIEMVLCGSVNKQVAGLINRAGALAVGISGKDGGLIKARKLVRKVKDPASGIEQTLDLGFVGEPDRVDPQVLYALSGSGLIPVIAPIAAGYAGETYNVNADTIAGAVAGAVHATRLLMLTDVPGVLDADGKLIPELTAAQARKGIESGMISGGMIPKVETCLEAVRKGAKAAVIVDGRVPHACLLELFTEAGSGTMIRRDENEDYNPA","length":310,"molWeight":32098,"crc64":"1D9C712473BE458E","md5":"35B6E738ABF9B125B74ADAFADBA0D9C6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":2},"uniParcId":"UPI00156BB44C"}}]}