{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G782","uniProtkbId":"A0A291G782_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":32,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46103.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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":"ATG46103.1"}],"value":"CEW89_00045"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":385,"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":409,"modifier":"EXACT"},"end":{"value":412,"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":457,"modifier":"EXACT"},"end":{"value":457,"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":461,"modifier":"EXACT"},"end":{"value":461,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46103.1"}],"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46103.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46103.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46103.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804445.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G782","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00820","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00045","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9800958at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MMKSLSELGLTAQSGREAQITGLSVDSRKVEEGHLFAALPGARAHGAEYLPMALSMGARAVLTDPEGARIAAGAIAEYEPALVVVEDPRQALAYAAALYYGAQPEVMVAVTGTNGKTSVATFTRQIWQLLGARAINVGTTGVEGDWQAPSPHTTPEPITLHRMLSEAAHAGVTHGAMEASSHGLAQRRLDGVRLTAAAFTNFTQDHLDYHATFEAYFSAKAGLFTRVLPEDGVAIVNIDDARGMEVEGLCAERGIDVMRVGRSDAADLRIVGQRFDATGQDLRVDFVGNIYQIRLDLIGGFQAENVMAAAGLVMASGADPEEVFSCLPELVGVRGRMQHAATRDNGAAVFVDYAHTPDAVSTAITALRPHVMGRIIAIVGAGGDRDKTKRPLMGKAAAETADLVIVTDDNPRSEDPASIRAEVLAGAPEAMEVGDRAEAILRGVDALHPGDALLICGKGHESGQTVGDTVYPFDDVEQASLAVSALDGAL","length":490,"molWeight":51482,"crc64":"2B1FE37D2A4A0442","md5":"05506DB2C9EBEB41B5A9B5A2C6D1C88B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI000BBEA6AE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GAE6","uniProtkbId":"A0A291GAE6_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":33,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47513.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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":"ATG47513.1"}],"value":"CEW89_07965"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059148"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"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":302,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":519,"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":521,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":474,"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47513.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47513.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG47513.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096805517.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GAE6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00242","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_07965","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801107at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"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":"MARYVFITGGVVSSLGKGLASAALGALLQARGYSVRLRKLDPYLNVDPGTMSPFEHGEVFVTDDGAETDLDLGHYERFTGVSARMTDSVSSGRIYTNVLEKERRGDYLGKTIQVIPHVTNEIKDFIEIGDDEVDFMLCEIGGTVGDIEGLPFFEAIRQFAQDRPRGQCIFMHLTLLPYIAASGELKTKPTQHSVKELRTIGLQPNVLVCRSEHPIPEKEREKIALFCNVRKEDVIAAPDLKSIYEAPLAYHREGLDQAVLDAFNIAPAPKPDLSVWHDVADRIFNPEGEVKVAIVGKYVQLEDAYKSVSEALTHGGMANRVKVKVEWVDAETFEHEDPAPYLEGFDAILVPGGFGERGTEGKIKAAQFARERKVPYLGICLGMQMAVIEAARHLAGIESAGSEEFDHEAGKKRFEPVVYHLKEWVQGNHTVQRKADDAKGGTMRLGAYTASLKEGSKVAEIYGSTEIEERHRHRYEVDIKYKDKLEACGLVFSGMSPDGRLPEIVEAKDHPWYIGVQYHPELKSKPFAPAPLFRDFIRAAKENSRLV","length":547,"molWeight":60842,"crc64":"E7C28151DF835E0C","md5":"61D81588C99FDBE2C8F48D6D2790F1BE"},"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":16},"uniParcId":"UPI000BBEB995"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GAF4","uniProtkbId":"A0A291GAF4_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":36,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46996.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme IspD/IspF"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2.7.7.60"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4-diphosphocytidyl-2C-methyl-D-erythritol synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MEP cytidylyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MCT"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECDP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4.6.1.12"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"ispDF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46996.1"}],"value":"CEW89_05080"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13429"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:57823"},{"database":"ChEBI","id":"CHEBI:58262"}],"ecNumber":"2.7.7.60","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001282"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23864"},{"database":"ChEBI","id":"CHEBI:57919"},{"database":"ChEBI","id":"CHEBI:58483"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"4.6.1.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000200"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001968"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004787"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004709"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009789"}],"value":"Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008480"}],"value":"Belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the C-terminal section; belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":394,"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":241,"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":242,"modifier":"EXACT"},"end":{"value":397,"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":248,"modifier":"EXACT"},"end":{"value":250,"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":248,"modifier":"EXACT"},"end":{"value":248,"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":250,"modifier":"EXACT"},"end":{"value":250,"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":274,"modifier":"EXACT"},"end":{"value":275,"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":282,"modifier":"EXACT"},"end":{"value":282,"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":296,"modifier":"EXACT"},"end":{"value":298,"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":375,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"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":382,"modifier":"EXACT"},"end":{"value":382,"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":16,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"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":274,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46996.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46996.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46996.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096805145.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GAF4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00565","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_05080","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804336at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00056","properties":[{"key":"RectionId","value":"UER00093"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0008685","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050518","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019288","properties":[{"key":"GoTerm","value":"P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016114","properties":[{"key":"GoTerm","value":"P:terpenoid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02516","properties":[{"key":"EntryName","value":"CDP-ME_synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00554","properties":[{"key":"EntryName","value":"MECDP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"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":"TIGR00151","properties":[{"key":"EntryName","value":"ispF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006899","properties":[{"key":"EntryName","value":"PRK09382.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181:SF1","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01128","properties":[{"key":"EntryName","value":"IspD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02542","properties":[{"key":"EntryName","value":"YgbB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69765","properties":[{"key":"EntryName","value":"IpsF-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01295","properties":[{"key":"EntryName","value":"ISPD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01350","properties":[{"key":"EntryName","value":"ISPF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTKIAALIVAAGRGTRAGGEMPKQWQRLGTAPTALRVIDHAISAFRPHVARIVVVHHADDFDLAQSLENVTLVSGGATRSASVKAGLEALSGQDFDRVLIHDAARALIPTEVIEGVLTALETHEGAAPALMVTDALWLGASSQNAAETGILVEGTRDRSGLYRAQTPQGFVFDAILTAHRAFQGEAADDVEVARAHGLAVAITEGSEENFKITHPGDFARADAVLRQRQQEKAAMEIRPDIRLGNGYDVHRFGEGDHVWLCGVKLPHGRSLQGHSDADVGMHALTDAIYGALARGDIGQHFPPSDPQWKGAESHIFLRHAIGLAREMGYEMMNCDVTLVCERPKVGPHAASMRAALADIMGVDVEKVSVKATTSERLGFTGREEGIASLATAALIKS","length":397,"molWeight":42337,"crc64":"9897B90C19D2863D","md5":"CC910BA97614C0F6955696AF7E019004"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":9,"Site":6},"uniParcId":"UPI000BBEB48D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GAW4","uniProtkbId":"A0A291GAW4_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47192.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein nucleotidyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein adenylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.108"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein uridylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"ydiU"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"selO"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47192.1"}],"value":"CEW89_06180"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Nucleotidyltransferase involved in the post-translational modification of proteins. It can catalyze the addition of adenosine monophosphate (AMP) or uridine monophosphate (UMP) to a protein, resulting in modifications known as AMPylation and UMPylation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-[protein] + UTP = N(tele)-(5'-uridylyl)-L-histidyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83891"},{"database":"Rhea","id":"RHEA-COMP:9745"},{"database":"Rhea","id":"RHEA-COMP:20239"},{"database":"ChEBI","id":"CHEBI:29979"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:233474"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58120"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:15073"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:142516"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + UTP = O-(5'-uridylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64604"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:16635"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:156051"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54292"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:13847"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:138113"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-(5'-adenylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54288"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:13846"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + UTP = O-(5'-uridylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83887"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20238"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:90602"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009747"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Belongs to the SELO family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"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_00692"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47192.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47192.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG47192.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096805303.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GAW4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_03229","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_06180","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9776281at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0070733","properties":[{"key":"GoTerm","value":"F:AMPylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO: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":"HAMAP","id":"MF_00692","properties":[{"key":"EntryName","value":"YdiU_SelO"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003846","properties":[{"key":"EntryName","value":"SelO"}]},{"database":"NCBIfam","id":"NF000658","properties":[{"key":"EntryName","value":"PRK00029.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32057","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32057:SF14","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02696","properties":[{"key":"EntryName","value":"SelO"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQFDNSYVRLPDRFFTRIAPERAPAPEMVLWNADLAAHLGVADWDAEICAGNVIPDGADPIAQVYGGHQFGNWSPQLGDGRAVMLGEVVTDKGRFDIHLKGAGRTPYSRNGDGRAWIGPVLREYIVSEFMHAVGVPTTRALAAVRTGGRVQRERAYPGGLLVRVAASHIRVGTFQYFTAREDYEAVRLLTDHARARHFPQATNTIEFYQEVVRAQARLIATWMGLGFVHGVMNTDNMAVSGETIDFGPCAFIDGYSPKAVYSSIDTHGRYAYEQQPSMAHWNLAQLGSCFVPQLEDELGGQQQAIDALTEVLNSFPGLYQAEWRKVFGAKLGIADAREDDLPLIQDLLGMMAKDGADFTNTFRGLLDGSARDWMLDREIFDDWSARWQARRSPDWQDIAAKATPAVIPRNHRIEEAIQASLAGDDSKAKRLAEVLSHPFDLAEADRDLGLPPREDQMVHMTFCGT","length":466,"molWeight":51709,"crc64":"E0BE2D2BCA636085","md5":"3E3E6B9E0D7A73642995A0F0C7D9DDE9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SIMILARITY":1},"countByFeatureType":{"Active site":1,"Binding site":11},"uniParcId":"UPI000BBE2C68"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GB22","uniProtkbId":"A0A291GB22_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2017-12-20","entryVersion":39,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47264.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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":"ATG47264.1"}],"value":"CEW89_06590"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025153"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADHX = (6S)-NADHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32215"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:64075"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000013"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADPHX = (6S)-NADPHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32227"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:64077"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000909"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADHX + ADP = AMP + phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32223"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32235"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009524"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the C-terminal section; belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006001"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the N-terminal section; belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":564,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"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":131,"modifier":"EXACT"},"end":{"value":137,"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":164,"modifier":"EXACT"},"end":{"value":164,"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":167,"modifier":"EXACT"},"end":{"value":167,"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":319,"modifier":"EXACT"},"end":{"value":319,"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":382,"modifier":"EXACT"},"end":{"value":382,"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":431,"modifier":"EXACT"},"end":{"value":431,"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":476,"modifier":"EXACT"},"end":{"value":480,"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":509,"modifier":"EXACT"},"end":{"value":509,"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":510,"modifier":"EXACT"},"end":{"value":510,"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47264.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47264.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG47264.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096805362.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GB22","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_06590","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9806925at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAELLTSAQMRAVERAAIDSGEVSGLELMERAGQGVVAAIFEEWPELALSSYKAVVLCGPGNNGGDGFVIARLLKQRGWEVEVFLYGDPEKLPPDAKANYERWREVGEVAPLNTREFRHSDCDVVVDALFGTGVSRALSGEALSTMSQLAGANGDRYDKIVCVDCPSGLCLDSGRVLAQPSNPALADLPIQLNQLPRSRYPYGGIGFAALTVTFDSPKCGHFLDDGPFLCGKLRVVDIGVQDFRENSRRDILDKSGQKTGRAAKLVRRPEVCLVHMSPIVKENRSFAQPLMLWGKDPQDHKYTHGHPLILSGLSGKTGAARLSARAALRVGAGLVTLGTPHEAVTEVAAQITTIMLTEIDTPEILTRVLTDKRLNALCIGPGFGVERAGEFLPYALAAKRATVLDADALTALSESETGFADLHANCVLTPHAGEFKRLFPDLATKLAEPPIKGPAYSKVDATREAAKRAGCTVLFKGPDTVIASPNGRCSINAAVYDRAAPWLATAGSGDVLAGLITGLLARGLAPHHAAETAAWLHVEAARSFGPGLIAEDLPEELPKVFRALGL","length":566,"molWeight":60350,"crc64":"9F427073A7AF6F49","md5":"A822D448A50FACA4A46AF8232CE0CFF5"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI000BBEE1DB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GBB2","uniProtkbId":"A0A291GBB2_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":35,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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":"ATG47438.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47438.1"}],"value":"CEW89_07565"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":133,"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":228,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":450,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"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":80,"modifier":"EXACT"},"end":{"value":81,"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":103,"modifier":"EXACT"},"end":{"value":105,"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":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"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":226,"modifier":"EXACT"},"end":{"value":226,"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":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"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":359,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI: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":368,"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":387,"modifier":"EXACT"},"end":{"value":387,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":422,"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG47438.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096805471.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GBB2","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00162","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_07565","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9775031at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00113","properties":[{"key":"RectionId","value":"UER00532"}]},{"database":"UniPathway","id":"UPA00973","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"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"}]}],"sequence":{"value":"MATALILLAAGQGTRMNSDLPKVLHPIGNAPLFAHALASGSALEPERTVLVVGHGGDLVAAEAARIDEDIVIARQEEQLGTAHAVLQAKDALAAFEGDAIVLYGDTPFISEDTILRMAEARKSADVVVLGFEAADPARYGRLVMEGDRLTRIVEYKDATEAQRAITFCNSGLIAAEASVLFELLDQVGNDNAAGEYYLPDIVEIAWKTGRTATAVACDEAETLGVNTRAELARAEAIFQSAKRAEALDNGVTLMAPETVFFSLDTYIGRDTVVEPNVIFGPGVTVESGARLRAFSHFEGCHVSMGATVGPFARLRPGAELANNAHIGNFVEVKNALIGEGTKVNHLTYIGDADIGDGTNIGAGTITCNYDGVFKHRTVVGRNAFIGSNTMLVAPVTVGDEAMTASGSVITSNVEAGALAIGRAKQVNKPMLAVRMFEKLKSLKAKKQKGQ","length":450,"molWeight":47495,"crc64":"417F6AF349C2131E","md5":"1780DDE9A42BA3B5EE38F5326A5AE442"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":20},"uniParcId":"UPI000BBE0B36"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GCR7","uniProtkbId":"A0A291GCR7_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47844.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47844.1"}],"value":"CEW89_09875"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":394,"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":188,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":306,"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":323,"modifier":"EXACT"},"end":{"value":323,"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":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47844.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG47844.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG47844.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096805796.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GCR7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_03385","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_09875","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802554at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"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":"MLNGKSILLIIGGGIAAFKSLDLIRRLREEGVRVVPVLTKAAEEFVTPLSVSALAAEKVYRDLFDLTDEAEMGHIELSRAADLVVVSPATADLLGKMAGGLANDLASTLLMATDKPVLVAPAMNVRMWEHPACQRNVATLMGDGVLFVGPEEGSMACGEFGPGRLSETPDIVAAIRAALTDGPLKGKHILVTSGPTHEPIDPVRYIANRSSGAQGTAIAIALRDLGADVSFVTGPADVPPPLGLRVIPVETAREMKAAVEAALPAEAAVFAAAVADWRVASESGSKIKKTQGKLPILEFSENPDILAGVSQMAEGRPRLVVGFAAETDDVIAHATEKRKRKGCDWIVANDVSPATGIMGGTENAVTLISERGADEWPRMGKDEVARQLAYRIADHLVQN","length":399,"molWeight":42055,"crc64":"95EC263E694FF797","md5":"87706CC7D71AB70B353546568A03D3B1"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":6},"uniParcId":"UPI000BBE5499"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GEL8","uniProtkbId":"A0A291GEL8_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":30,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48502.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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":"ATG48502.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48502.1"}],"value":"CEW89_13555"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"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":140,"modifier":"EXACT"},"end":{"value":140,"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":143,"modifier":"EXACT"},"end":{"value":143,"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":195,"modifier":"EXACT"},"end":{"value":196,"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":227,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":251,"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":326,"modifier":"EXACT"},"end":{"value":326,"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48502.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48502.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG48502.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096806247.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GEL8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_01746","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_13555","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000008","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDPSAPITQDVMTFPRKEMPSDKINLVGLTRDALRQTLIDNGTPEKQAKMRAGQIWQWIYQWGVRDFAEMTNLAKDYRAMLAEKFEVRVPEVVSKQVSEDGTRKYLVRIDGGHEVEVVYIPEEGRGTLCVSSQVGCTLTCSFCHTGTQKLVRNLTAGEIVGQVMMARDDLNEWPERGAPKDETRLLSNIVLMGMGEPLYNFENVRDAMKIVMDAEGIQLGRRRITLSTSGVVPEIHRTAQEIGCLLAVSFHATTDETRDVLVPINKKWNIEKLLEALREYPKATNSERITFEYVMLKDVNDTDEDAHRLVKLLDGIPAKVNLIPFNEWPGAPYQRSSNNRIRAFATILMQAGYASPIRTPRGEDIMAACGQLKSATERARKSRKEILKEAGQAI","length":394,"molWeight":44368,"crc64":"4D57833196CA9C0D","md5":"55D65D5D7F4BB16C9E7B5281F394172C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI000BBE9A73"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GFG7","uniProtkbId":"A0A291GFG7_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":34,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48908.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48908.1"}],"value":"glyA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48908.1"}],"value":"CEW89_15810"}]}],"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"}],"features":[{"type":"Domain","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Plays an important role in substrate specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]},{"type":"Modified residue","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48908.1"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48908.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG48908.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG48908.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096806544.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GFG7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_04156","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_15810","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9803846at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00193","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00288","properties":[{"key":"RectionId","value":"UER01023"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050413","properties":[{"key":"GoTerm","value":"F:D-alanine 2-hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"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":"MFDRLQKYEIADADIASAIGEELERQQTQIELIASENIVSPDVMAAQGSVLTNKYAEGYVGKRYYGGCEFVDKVEAVAIDRLKQLFGAEYANVQPHSGAQANQAVFLALLQPGDRIMGLSLAHGGHLTHGSPVTMSGKWFDVVSYEVDPETHLIDMEKVREKALETKPKLIVAGASAYPRVIDFEGFRKIADEVGAYLMVDMAHYAGLIAGGKYPNPVPHAHVTTSTTHKTLRGPRGGVILSNDEAIAKKLNSAVFPGNQGGPLMHVIAAKAVAFGEALQPSFSDYAGQVIENAKALADVLKVGGLGIVSGGTDCHMVLVDLRPKGVTGKVAEIALERAGLTCNKNSIPNDPEKPFVTSGIRLGTSAGTTRGFKEAEFEQIGSLILRVLDALSDNPEGDAAVEAEVLAEVKKLCADHPIYGA","length":422,"molWeight":44949,"crc64":"64EA52DE450D88BD","md5":"747E71FBE3ACED90967A2D207EDDD66F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":1,"Modified residue":1},"uniParcId":"UPI000BBE84C4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GGG8","uniProtkbId":"A0A291GGG8_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49268.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49268.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49268.1"}],"value":"CEW89_17815"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Active site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-98)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49268.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49268.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG49268.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096806812.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GGG8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_03082","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_17815","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9759743at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.520.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF6","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDGNEMKTAGKCPVMHGGNTAMGSNVMDWWPNALNLDILHQHDTKTDPMGEAFDYREAVKGLDFDALKADMHALMTESQEWWPADWGHYGGLMIRLSWHAAGSYRLADGRGGGGTGNQRFAPLNSWPDNVSLDKARRLLWPIKKKYGNKVSWADLIVLAGTIAYENMGLKTFGFGFGRKDIWHPEKDTYWGAEKEWLAPSDERYTDVDKPDTMENPLAAVQMGLIYVNPEGVNGKPDPMKTAAQVRETFARMAMNDEETAALTAGGHTVGKTHGNGDASVLGADPEAAGPEMQGLGWSNPNQHGKAANAVTSGLEGAWTTHPTQFDMGFFDMLFGHDWELRKSPAGAWQWEPVDIKEEDKPLDATDPSKRHNPMMTDADMAMKVDPIYNAICQKFMADPAYFADTFARAWFKLTHRDMGPKVRYIGPDVPSEDLIWMDPVPAGSTSYDVDAVKAKIAASGLSISEMVSTAWDSARTYRGSDMRGGANGARIRLAPQKDWEGNEPARLVKVLSVLEPIAAEAGASVADVIVLAGGVGIEQAAKAAGFDITVPFAPGRGDATDEMTDAASFDVLEPIADGYRNWLKKDYVVSPEELMLDRTQLMGLTAPEMTVLTGGMRVLGTNYGGTKHGVFTEREGALTPDFFVTLTDMDYKWVPVKGGVYEITERKSGAVKYTATRTDLVFGSNSILRAYAEVYAQDDNAEKFVEDFVKAWVKVMNADRFDLTA","length":725,"molWeight":79511,"crc64":"9287710A3FD80520","md5":"CD094EFAE8E63F50F63BCE585F05FDE5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI000BBEB512"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GGM3","uniProtkbId":"A0A291GGM3_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":34,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49212.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ATP-dependent zinc metalloprotease FtsH"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"3.4.24.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ftsH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49212.1"}],"value":"CEW89_17515"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Multi-pass membrane protein","id":"SL-9909"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003651"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010044"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the C-terminal section; belongs to the peptidase M41 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the central section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":636,"modifier":"EXACT"}},"description":"ATP-dependent zinc metalloprotease FtsH","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5053566994"},{"type":"Transmembrane","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":593,"modifier":"EXACT"},"end":{"value":636,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":201,"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":416,"modifier":"EXACT"},"end":{"value":416,"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":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":494,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49212.1"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49212.1"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49212.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49212.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG49212.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096806770.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GGM3","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_01037","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_17515","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9809379at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004222","properties":[{"key":"GoTerm","value":"F:metalloendopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19501","properties":[{"key":"EntryName","value":"RecA-like_FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.760:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.720.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.760","properties":[{"key":"EntryName","value":"Peptidase M41"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01458","properties":[{"key":"EntryName","value":"FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR041569","properties":[{"key":"EntryName","value":"AAA_lid_3"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR003960","properties":[{"key":"EntryName","value":"ATPase_AAA_CS"}]},{"database":"InterPro","id":"IPR005936","properties":[{"key":"EntryName","value":"FtsH"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011546","properties":[{"key":"EntryName","value":"Pept_M41_FtsH_extracell"}]},{"database":"InterPro","id":"IPR000642","properties":[{"key":"EntryName","value":"Peptidase_M41"}]},{"database":"InterPro","id":"IPR037219","properties":[{"key":"EntryName","value":"Peptidase_M41-like"}]},{"database":"NCBIfam","id":"TIGR01241","properties":[{"key":"EntryName","value":"FtsH_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076:SF97","properties":[{"key":"EntryName","value":"ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076","properties":[{"key":"EntryName","value":"METALLOPROTEASE M41 FTSH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17862","properties":[{"key":"EntryName","value":"AAA_lid_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06480","properties":[{"key":"EntryName","value":"FtsH_ext"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01434","properties":[{"key":"EntryName","value":"Peptidase_M41"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140990","properties":[{"key":"EntryName","value":"FtsH protease domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00674","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGNARNLAFWLVLLMLVLALFQVLGGNQSSMSSEVVPYSEFMTKVDDGTVTSVKVDGEKVYFTGADSRQKYTINPGDQNLVSELLAKDVNVEGKPQEESGIMPFVISFLPIFLIIGVWIYFMNRMQGGGKGGAMGFGKSRAKLLTEKQGRVTFDDVAGIDEAKEELEEIVEFLRNPQKFSALGGKIPKGALLVGPPGTGKTLLARAIAGEAGVPFFTISGSDFVEMFVGVGASRVRDMFEQAKKNAPCIVFIDEIDAVGRHRGAGYGGGNDEREQTLNQLLVEMDGFESNEGVIIIAATNRRDVLDPALLRPGRFDRQITVPNPDIKGREKILNVHARKVPLGPDVDLRIIARGTPGFSGADLANLVNEAALMAARVGRRQVTMEDFEQAKDKVMMGAERRSMVLTDEQKEKTAYHEAGHAIVGLKLPKCDPVYKATIIPRGGALGMVMSLPEMDKLQMFKDEARQRIAMTMAGKAAEIFKYGEEEVSSGPVGDIQQASQLARAMVMRYGMSDKVGNIDYAEAAEGYQGNTTGLSVSAHTKELIEEEVKRFIDEGYAEAYRIISEYEEEWERLAQGLLEYETLTGEEIKRVIAGLPPQADEDEGGSGGSGEASVTAIPKTKKKPKGDGGMEPEPMA","length":636,"molWeight":69169,"crc64":"D6D17845011C0311","md5":"619E755E41E5ED7C3756A9BB9F5D5D7A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":1,"Domain":1,"Region":1,"Active site":1,"Binding site":4},"uniParcId":"UPI000BBE6E94"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GGN1","uniProtkbId":"A0A291GGN1_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":35,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49328.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49328.1"}],"value":"CEW89_18145"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1119,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5049718487"},{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":727,"modifier":"EXACT"},"end":{"value":918,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":985,"modifier":"EXACT"},"end":{"value":1119,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":985,"modifier":"EXACT"},"end":{"value":1119,"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":182,"modifier":"EXACT"},"end":{"value":182,"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":188,"modifier":"EXACT"},"end":{"value":188,"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":189,"modifier":"EXACT"},"end":{"value":189,"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":221,"modifier":"EXACT"},"end":{"value":221,"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":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"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":255,"modifier":"EXACT"},"end":{"value":255,"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":256,"modifier":"EXACT"},"end":{"value":256,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":312,"modifier":"EXACT"},"end":{"value":312,"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":312,"modifier":"EXACT"},"end":{"value":312,"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":312,"modifier":"EXACT"},"end":{"value":312,"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":312,"modifier":"EXACT"},"end":{"value":312,"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":312,"modifier":"EXACT"},"end":{"value":312,"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":314,"modifier":"EXACT"},"end":{"value":314,"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":314,"modifier":"EXACT"},"end":{"value":314,"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":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":802,"modifier":"EXACT"},"end":{"value":802,"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":804,"modifier":"EXACT"},"end":{"value":804,"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":809,"modifier":"EXACT"},"end":{"value":809,"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":834,"modifier":"EXACT"},"end":{"value":834,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":836,"modifier":"EXACT"},"end":{"value":836,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":877,"modifier":"EXACT"},"end":{"value":877,"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":877,"modifier":"EXACT"},"end":{"value":877,"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":877,"modifier":"EXACT"},"end":{"value":877,"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":889,"modifier":"EXACT"},"end":{"value":889,"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":889,"modifier":"EXACT"},"end":{"value":889,"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":889,"modifier":"EXACT"},"end":{"value":889,"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":889,"modifier":"EXACT"},"end":{"value":889,"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":889,"modifier":"EXACT"},"end":{"value":889,"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":891,"modifier":"EXACT"},"end":{"value":891,"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":891,"modifier":"EXACT"},"end":{"value":891,"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49328.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49328.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG49328.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096806857.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GGN1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_03141","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_18145","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804197at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00171"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_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":"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":"2"}]},{"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":"MPKRTDISSIMIIGAGPIIIGQACEFDYSGAQACKALREEGYRVILVNSNPATIMTDPDMADATYIEPITPEVVAKIIEKERPDALLPTMGGQTGLNTSLALADMGVLDKFNVELIGAKREAIEMAEDRKLFREAMDRLGIENPKADIVAAPKREDGRYDIAAGMKIAMEALEHIGLPAIIRPAFTLGGTGGGVAYNRDDYEKICRSGLEASPVAQILVDESLLGWKEYEMEVVRDKADNAIIVCSIENVDPMGVHTGDSVTVAPALTLTDKEYQIMRTHSINVLREIGVETGGSNVQWAVNPADGRMVVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDELDNDITKVTPASFEPTIDYVVTKIPKFAFEKFPGAKPELTTAMKSVGEAMAIGRTFHESMQKALASMESGLTGFDEIELPDMPKAAQIVEADGAEDSLPRILLGADESAQQMIDKTVTRELAKATPDRLRVIAQAMRFGFTDEEINEINSFDPWFLARIREIMVAECEIKKDGLPVTEEGLRKLKMLGFTDARLAKLTGRDEANVRRARHNLGVTAVFKRIDTCAAEFEAQTPYMYSTYEMPMMGEVECEARPSDRKKVVILGGGPNRIGQGIEFDYCCCHACFSLTEQGYETIMVNCNPETVSTDYDTSDRLYFEPLTFEHVMEILRVEQDKGTLHGVIVQFGGQTPLKLANALEAEGIPILGTTPDAIDLAEDRERFQDLVNRLDLKQPHNGIAHSDDEAIEIASDIGFPLVIRPSYVLGGRAMEIVRDMEGLKRYIRDAVVVSGDSPVLLDSYLSGATEIDVDALCDGEKVHVAGIMQHIEEAGVHSGDSACSLPPYSLKPEIIEELKRQTEALALALNVVGLMNVQYAVKDDVIFLIEVNPRASRTVPFVAKAVNSPIASIAARLMAGEKLDTFELVDPASTGRYAVKEAVLPFARFPGVDTILGPEMRSTGEVMGADKSFARAFLKAQMGAGTNLPSSGKVFVSVKNYDKKPKMVEAIKTLSDLGFEIIATRGTAKFLKENGVESKVVNKVYEGRPNIVDMMKDGEIALVLNTTEGNQALEDSREIRSVALYDKIPYFTTAAASHAAAMAIKARLEGEIEVLSLQDV","length":1119,"molWeight":122006,"crc64":"D15741F87E698CBC","md5":"22BD9F37B4FEAD340F58132D72274E56"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":1,"Domain":3,"Region":2,"Binding site":38,"Lipidation":2},"uniParcId":"UPI000BBF2382"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291GH79","uniProtkbId":"A0A291GH79_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":34,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49376.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49376.1"}],"value":"glyA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49376.1"}],"value":"CEW89_18410"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057572"}],"value":"Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = 2-methylserine + (6S)-5,6,7,8-tetrahydrofolate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:58275"}],"ecNumber":"2.1.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051216"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15481"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57453"}],"ecNumber":"2.1.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006376"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Belongs to the SHMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"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":132,"modifier":"EXACT"},"end":{"value":134,"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":236,"modifier":"EXACT"},"end":{"value":236,"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":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49376.1"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49376.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG49376.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG49376.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_066708336.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291GH79","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_02395","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_18410","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9803846at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00193","properties":[{"key":"RectionId","value":"-"}]},{"database":"UniPathway","id":"UPA00288","properties":[{"key":"RectionId","value":"UER01023"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050413","properties":[{"key":"GoTerm","value":"F:D-alanine 2-hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00378","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000001","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.1150.10:FF:000003","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00051","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"InterPro","id":"IPR001085","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase"}]},{"database":"InterPro","id":"IPR049943","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase-like"}]},{"database":"InterPro","id":"IPR019798","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase_PLP_BS"}]},{"database":"InterPro","id":"IPR039429","properties":[{"key":"EntryName","value":"SHMT-like_dom"}]},{"database":"NCBIfam","id":"NF000586","properties":[{"key":"EntryName","value":"PRK00011.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680:SF35","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00464","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000412","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00096","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTANVRDSGFFTEALASRDPELFDSITKELGRQRHEIELIASENIVSAAVMEAQGTVLTNKYAEGYPGRRYYGGCEYVDITENLARDRAKELFDVKYVNVQPNSGSQANQGVYNALLQPGDTILGMNLASGGHLTHGASVNQSGKWFNAIQYGVRQQDQRLDYDQVRELALEHKPKLIVAGGSAIPRQIDFAKFREIADEVGALLMVDMAHFAGLVAGGAHPSPFPYADVATTTTHKTLRGPRGGMILTNDVEIAKKVNSAIFPGIQGGPLMHVIAAKAVAFGEALRPEFKEYAKQVITNAQALADQLMKGGLDIVTGGTDTHVLLVDLRPKNVTGKDTEKALERAHITCNKNGIPFDPQPPMITSGVRLGTPAGTTRGFGEAEFRQIADWIVEVVDGLAANGEEGNAEVEAKVKAEVEALCEKFPLYPNL","length":431,"molWeight":46588,"crc64":"84497E944D952D18","md5":"13DA8400719F0760D3A0DE9776B599CD"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":2,"Site":1,"Modified residue":1},"uniParcId":"UPI0008354888"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7B8","uniProtkbId":"A0A291G7B8_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":35,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46109.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"L-lactate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"L-LDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"1.1.1.27"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"ldh"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46109.1"}],"value":"CEW89_00080"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Catalyzes the conversion of lactate to pyruvate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003966"}],"value":"Catalyzes the reversible oxidation of malate to oxaloacetate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-lactate + NAD(+) = pyruvate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23444"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16651"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.1.1.27","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049258"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10002"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Allosterically activated by fructose 1,6-bisphosphate (FBP)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004843"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Fermentation; pyruvate fermentation to lactate; (S)-lactate from pyruvate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006054"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Belongs to the LDH/MDH superfamily. LDH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Lactate/malate dehydrogenase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00056"}]},{"type":"Domain","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"Lactate/malate dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02866"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000102-1"}]},{"type":"Binding site","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000102-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000102-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000102-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"beta-D-fructose 1,6-bisphosphate","id":"ChEBI:CHEBI:32966","note":"allosteric activator"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:32966"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"beta-D-fructose 1,6-bisphosphate","id":"ChEBI:CHEBI:32966","note":"allosteric activator"}},{"type":"Binding site","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Phosphotyrosine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00488"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46109.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46109.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46109.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_066705531.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7B8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00812","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00080","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802969at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00554","properties":[{"key":"RectionId","value":"UER00611"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004459","properties":[{"key":"GoTerm","value":"F:L-lactate dehydrogenase (NAD+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006089","properties":[{"key":"GoTerm","value":"P:lactate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd05292","properties":[{"key":"EntryName","value":"LDH_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.110.10","properties":[{"key":"EntryName","value":"Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal"},{"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_00488","properties":[{"key":"EntryName","value":"Lactate_dehydrog"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001557","properties":[{"key":"EntryName","value":"L-lactate/malate_DH"}]},{"database":"InterPro","id":"IPR011304","properties":[{"key":"EntryName","value":"L-lactate_DH"}]},{"database":"InterPro","id":"IPR018177","properties":[{"key":"EntryName","value":"L-lactate_DH_AS"}]},{"database":"InterPro","id":"IPR022383","properties":[{"key":"EntryName","value":"Lactate/malate_DH_C"}]},{"database":"InterPro","id":"IPR001236","properties":[{"key":"EntryName","value":"Lactate/malate_DH_N"}]},{"database":"InterPro","id":"IPR015955","properties":[{"key":"EntryName","value":"Lactate_DH/Glyco_Ohase_4_C"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR01771","properties":[{"key":"EntryName","value":"L-LDH-NAD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43128","properties":[{"key":"EntryName","value":"L-2-HYDROXYCARBOXYLATE DEHYDROGENASE (NAD(P)(+))"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43128:SF16","properties":[{"key":"EntryName","value":"L-LACTATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02866","properties":[{"key":"EntryName","value":"Ldh_1_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00056","properties":[{"key":"EntryName","value":"Ldh_1_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000102","properties":[{"key":"EntryName","value":"Lac_mal_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00086","properties":[{"key":"EntryName","value":"LLDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF56327","properties":[{"key":"EntryName","value":"LDH C-terminal domain-like"},{"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":"PS00064","properties":[{"key":"EntryName","value":"L_LDH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIGIVGAGMVGSAAGYAIALKGTASKIVFVDYNAGLARAQAEDIAHAVPFASSTVVTAGDYAELKGAGVVILAAGVGQKPGESRLELLTRNAEVFRQIIGKVLDAAPDAILLVATNPVDIMTQIATRLSGLPPARVIGSGTILDTARFRHLIGEHLGVAPRSVHAYVLGEHGDSEVLCWSSARAGTLSVKDFAAQMRVPLTEGVKARIDDGVRNAAYTIINGKGATWYGIGAGLERLVRAIARDEQTVLSVSIVTPKVEGVQDVALSIPRIVGAQGVVSDLFPELDDGEHEALGASARLLKETLDALEY","length":310,"molWeight":32295,"crc64":"A48FD2BBFA72705F","md5":"A05D2A0AFFE25B61186139AF42878C4B"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":15,"Modified residue":1},"uniParcId":"UPI0008335ABA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7D0","uniProtkbId":"A0A291G7D0_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":34,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46263.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"ATP-dependent Clp protease proteolytic subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000549"}],"value":"3.4.21.92"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Endopeptidase Clp"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46263.1"}],"value":"clpP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46263.1"}],"value":"CEW89_00950"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000550"}],"value":"Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).","ecNumber":"3.4.21.92","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034021"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10086"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007039"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"Belongs to the peptidase S14 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10085"}]},{"type":"Active site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}]},{"type":"Active site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10086"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46263.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46263.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46263.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_066711133.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7D0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_03443","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00950","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802800at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009368","properties":[{"key":"GoTerm","value":"C:endopeptidase Clp complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051117","properties":[{"key":"GoTerm","value":"F:ATPase binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07017","properties":[{"key":"EntryName","value":"S14_ClpP_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent Clp protease proteolytic subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00444","properties":[{"key":"EntryName","value":"ClpP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001907","properties":[{"key":"EntryName","value":"ClpP"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR023562","properties":[{"key":"EntryName","value":"ClpP/TepA"}]},{"database":"InterPro","id":"IPR033135","properties":[{"key":"EntryName","value":"ClpP_His_AS"}]},{"database":"InterPro","id":"IPR018215","properties":[{"key":"EntryName","value":"ClpP_Ser_AS"}]},{"database":"NCBIfam","id":"NF001368","properties":[{"key":"EntryName","value":"PRK00277.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009205","properties":[{"key":"EntryName","value":"PRK12553.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381:SF70","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00574","properties":[{"key":"EntryName","value":"CLP_protease"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00127","properties":[{"key":"EntryName","value":"CLPPROTEASEP"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00382","properties":[{"key":"EntryName","value":"CLP_PROTEASE_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00381","properties":[{"key":"EntryName","value":"CLP_PROTEASE_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKDPIDTYMNTLVPMVVEQTSRGERAYDIFSRLLKERIIFLNGPVHDGMSSLICAQLLFLEAENPKKEIAMYINSPGGVVTSGLSIYDTMQYIRPKVSTLVMGQAASMGSLLLTAGEKGMRFSLPNSRVMVHQPSGGYQGQATDIMIHAQETQKLKDRLNQIYVKHTGQELQTVVDALERDNFMSPEDAKDFGLIDEIVESRAPVED","length":207,"molWeight":23072,"crc64":"FF5DAF55CA5571D6","md5":"DD16F8127E11DE617D6AFDA5B57FE64D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI0008333934"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7E0","uniProtkbId":"A0A291G7E0_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":32,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46283.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acetyl-coenzyme A synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"AcCoA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acs"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"6.2.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acetate--CoA ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acyl-activating enzyme"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46283.1"}],"value":"acs"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"acsA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46283.1"}],"value":"CEW89_01060"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23176"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.2.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Belongs to the ATP-dependent AMP-binding enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Acetyl-coenzyme A synthetase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16177"}]},{"type":"Domain","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"AMP-dependent synthetase/ligase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00501"}]},{"type":"Domain","location":{"start":{"value":530,"modifier":"EXACT"},"end":{"value":608,"modifier":"EXACT"}},"description":"AMP-binding enzyme C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13193"}]},{"type":"Binding site","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":499,"modifier":"EXACT"},"end":{"value":499,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":514,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":522,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":525,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":536,"modifier":"EXACT"},"end":{"value":536,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":538,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":541,"modifier":"EXACT"},"end":{"value":541,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":583,"modifier":"EXACT"},"end":{"value":583,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Modified residue","location":{"start":{"value":608,"modifier":"EXACT"},"end":{"value":608,"modifier":"EXACT"}},"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46283.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46283.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46283.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804583.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7E0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_03419","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_01060","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9803968at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003987","properties":[{"key":"GoTerm","value":"F:acetyl-CoA synthetase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006085","properties":[{"key":"GoTerm","value":"P:acetyl-CoA biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd05966","properties":[{"key":"EntryName","value":"ACS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.300.30:FF:000004","properties":[{"key":"EntryName","value":"Acetyl-coenzyme A synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.12780:FF:000001","properties":[{"key":"EntryName","value":"Acetyl-coenzyme A synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12780","properties":[{"key":"EntryName","value":"N-terminal domain of ligase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01123","properties":[{"key":"EntryName","value":"Ac_CoA_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011904","properties":[{"key":"EntryName","value":"Ac_CoA_lig"}]},{"database":"InterPro","id":"IPR032387","properties":[{"key":"EntryName","value":"ACAS_N"}]},{"database":"InterPro","id":"IPR045851","properties":[{"key":"EntryName","value":"AMP-b_sf"}]},{"database":"InterPro","id":"IPR025110","properties":[{"key":"EntryName","value":"AMP-bd_C"}]},{"database":"InterPro","id":"IPR020845","properties":[{"key":"EntryName","value":"AMP-binding_CS"}]},{"database":"InterPro","id":"IPR000873","properties":[{"key":"EntryName","value":"AMP-dep_synth/lig_dom"}]},{"database":"InterPro","id":"IPR042099","properties":[{"key":"EntryName","value":"ANL_N_sf"}]},{"database":"NCBIfam","id":"TIGR02188","properties":[{"key":"EntryName","value":"Ac_CoA_lig_AcsA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001208","properties":[{"key":"EntryName","value":"PRK00174.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24095","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24095:SF14","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A SYNTHETASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16177","properties":[{"key":"EntryName","value":"ACAS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00501","properties":[{"key":"EntryName","value":"AMP-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13193","properties":[{"key":"EntryName","value":"AMP-binding_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56801","properties":[{"key":"EntryName","value":"Acetyl-CoA synthetase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00455","properties":[{"key":"EntryName","value":"AMP_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDIYPPSESFASDALISTTDYEDLYRRSVEDPVSFWAEQGKILDWMEPYTQVKKTCFDFGRVDIKWYSDGVLNVSANCIDRHLARKSLQTAIIFEPDDPNEPARHITYKELSDKVNRMANVLLSQGVMRGDRVVIYLPMIPEAAYAMLACARIGAIHSIVFAGFSPDALANRINDCGAKLVITSDTAPRGGRRTPLKANTDAALLHCSDKVRCLVVKHTGDQISWVQGRDVDVKYLMEHASPDCPPRPMNAEDPLFILYTSGSTGKPKGVVHSSGGYLAYAALTHKYVFDYHDGDVFWCTADVGWVTGHSYIVYGPLANGATTVMFEGVPTYPDAGRFWAVCEKHKVNQFYTAPTALRSLMGQGNEWVEKYDLSSLKVLGSVGEPINPEAWNWYNEVVGKGNCPIVDTWWQTETGGHLLTPLPGAIPTKPGSATLPFFGVQPVILDATTGEEMTETEAEGVLCLKDSWPGQMRTVWGDHERFQETYFQQYKGYYFSGDGCRRDADGYYWITGRVDDVINVSGHRMGTAEVESALVAHAKVAEAAVVGMPHELKGQGIYAYVTLMNDVEPSDALRAELEKWVRTEIGPIAKPDFIQWAPGLPKTRSGKIMRRILRKIAENDTGSLGDISTLAEPQVVDELIQNSLYHLKK","length":650,"molWeight":72162,"crc64":"C5EBF15C41FCCB40","md5":"EC25336919A8567E9415CCCC151F176D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Binding site":17,"Modified residue":1},"uniParcId":"UPI000BBEEC70"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7J7","uniProtkbId":"A0A291G7J7_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46105.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00445"}],"value":"Phospho-N-acetylmuramoyl-pentapeptide-transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00445"}],"value":"2.7.8.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"value":"UDP-MurNAc-pentapeptide phosphotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"value":"mraY"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46105.1"}],"value":"CEW89_00055"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"value":"Catalyzes the initial step of the lipid cycle reactions in the biosynthesis of the cell wall peptidoglycan: transfers peptidoglycan precursor phospho-MurNAc-pentapeptide from UDP-MurNAc-pentapeptide onto the lipid carrier undecaprenyl phosphate, yielding undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide, known as lipid I"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + di-trans,octa-cis-undecaprenyl phosphate = di-trans,octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UMP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28386"},{"database":"ChEBI","id":"CHEBI:57865"},{"database":"ChEBI","id":"CHEBI:60392"},{"database":"ChEBI","id":"CHEBI:61386"},{"database":"ChEBI","id":"CHEBI:61387"}],"ecNumber":"2.7.8.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600715-1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"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:0000256","source":"ARBA","id":"ARBA00005583"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"value":"Belongs to the glycosyltransferase 4 family. MraY subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":263,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":288,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Transmembrane","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}]},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600715-1"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600715-1"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"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_00038"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"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_00038"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600715-1"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600715-1"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"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_00038"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00038"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46105.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46105.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46105.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804447.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7J7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00818","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00055","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9805475at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0008963","properties":[{"key":"GoTerm","value":"F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051992","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine:undecaprenyl-phosphate transferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0071555","properties":[{"key":"GoTerm","value":"P:cell wall organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06852","properties":[{"key":"EntryName","value":"GT_MraY"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00038","properties":[{"key":"EntryName","value":"MraY"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000715","properties":[{"key":"EntryName","value":"Glycosyl_transferase_4"}]},{"database":"InterPro","id":"IPR003524","properties":[{"key":"EntryName","value":"PNAcMuramoyl-5peptid_Trfase"}]},{"database":"InterPro","id":"IPR018480","properties":[{"key":"EntryName","value":"PNAcMuramoyl-5peptid_Trfase_CS"}]},{"database":"NCBIfam","id":"TIGR00445","properties":[{"key":"EntryName","value":"mraY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22926","properties":[{"key":"EntryName","value":"PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22926:SF5","properties":[{"key":"EntryName","value":"PHOSPHO-N-ACETYLMURAMOYL-PENTAPEPTIDE-TRANSFERASE HOMOLOG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00953","properties":[{"key":"EntryName","value":"Glycos_transf_4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10555","properties":[{"key":"EntryName","value":"MraY_sig1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01347","properties":[{"key":"EntryName","value":"MRAY_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01348","properties":[{"key":"EntryName","value":"MRAY_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLYWISSLSDGGDLFNLFRYITMRSGGAFFTALIFAMVFGRPLIDLLRRRQGRGQPIRDDGPETHFAKAGTPTMGGLLILTALLISTLLWARLDNPYVWIVMFVTFGYGLIGFADDYAKVSKSNTKGVSGKVRLVLGFLIAFIASVWSTMVHPAELQFQLALPVFKDLLINLWWFFIPFAMIVIVGAANAVNLTDGLDGLAIMPVMIAAGTLGAIAYVVGRVDFTNYLGLHYVPGTGEILVFTAALIGGGLGFLWFNAPPAAVFMGDTGSLALGGALGAIAVATKHEIVLAIVGGLFVVEALSVIIQVAYFKRTGKRVFLMAPIHHHYEKKGWSEPTIVIRFWIISLVLALIGLATLKLR","length":360,"molWeight":39100,"crc64":"FC50A6750BF41E9D","md5":"E99F5B98485C8A2CBDA44BC3B99F4E1B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":10,"Binding site":2},"uniParcId":"UPI000BBE240E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7J9","uniProtkbId":"A0A291G7J9_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":28,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46111.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"UDP-N-acetylglucosamine--N-acetylmuramyl-(pentapeptide) pyrophosphoryl-undecaprenol N-acetylglucosamine transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"2.4.1.227"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Undecaprenyl-PP-MurNAc-pentapeptide-UDPGlcNAc GlcNAc transferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46111.1"}],"value":"murG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46111.1"}],"value":"CEW89_00090"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Cell wall formation. Catalyzes the transfer of a GlcNAc subunit on undecaprenyl-pyrophosphoryl-MurNAc-pentapeptide (lipid intermediate I) to form undecaprenyl-pyrophosphoryl-MurNAc-(pentapeptide)GlcNAc (lipid intermediate II)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"di-trans,octa-cis-undecaprenyl diphospho-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-glucosamine = di-trans,octa-cis-undecaprenyl diphospho-[N-acetyl-alpha-D-glucosaminyl-(1->4)]-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + UDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31227"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:58223"},{"database":"ChEBI","id":"CHEBI:61387"},{"database":"ChEBI","id":"CHEBI:61388"}],"ecNumber":"2.4.1.227","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Belongs to the glycosyltransferase 28 family. MurG subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"Glycosyltransferase family 28 N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03033"}]},{"type":"Domain","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"Glycosyl transferase family 28 C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04101"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":294,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"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_00033"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"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_00033"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00033"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"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_00033"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46111.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46111.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46111.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804451.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7J9","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00810","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00090","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9808936at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051991","properties":[{"key":"GoTerm","value":"F:UDP-N-acetyl-D-glucosamine:N-acetylmuramoyl-L-alanyl-D-glutamyl-meso-2,6-diaminopimelyl-D-alanyl-D-alanine-diphosphoundecaprenol 4-beta-N-acetylglucosaminlytransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0050511","properties":[{"key":"GoTerm","value":"F:undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"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":"CDD","id":"cd03785","properties":[{"key":"EntryName","value":"GT28_MurG"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00033","properties":[{"key":"EntryName","value":"MurG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006009","properties":[{"key":"EntryName","value":"GlcNAc_MurG"}]},{"database":"InterPro","id":"IPR007235","properties":[{"key":"EntryName","value":"Glyco_trans_28_C"}]},{"database":"InterPro","id":"IPR004276","properties":[{"key":"EntryName","value":"GlycoTrans_28_N"}]},{"database":"NCBIfam","id":"TIGR01133","properties":[{"key":"EntryName","value":"murG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21015:SF22","properties":[{"key":"EntryName","value":"GLYCOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21015","properties":[{"key":"EntryName","value":"UDP-N-ACETYLGLUCOSAMINE--N-ACETYLMURAMYL-(PENTAPEPTIDE) PYROPHOSPHORYL-UNDECAPRENOL N-ACETYLGLUCOSAMINE TRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04101","properties":[{"key":"EntryName","value":"Glyco_tran_28_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03033","properties":[{"key":"EntryName","value":"Glyco_transf_28"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQAPLLVIAAGGTGGHMFPAQSLAEVMLARGWRVKLSTDDRGARYTGAFPKAVEIDTVPSATFARGGILAKALVPFRIAGGVLSALTKFVSDKPAVVVGFGGYPAIPAVAAATLLKLPRMIHEQNGVLGRVNQAFAKRVNTVACGTWPTTLPQGVEGYYVGNPVRGAVLEKHAAPYIPPGDYPMELLIVGGSQGARILSDVVPDAISRLPEHMLSHLRVSQQARPEDLDRVTEFYHTQGIQADVRPFFDDIPTRMSEAQLVISRSGASTVADISVIGRPSILIPYAAAAGDHQTANARGLVEADAAVMIPESQLTPESLAEQIYNVLAHPQGATMMAHAALSVSKPMAAEELAALVEELAFNKQ","length":365,"molWeight":38596,"crc64":"F9496773A7EE2989","md5":"99A41F08778C9AAF5C83CFDFF6F2E191"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":5},"uniParcId":"UPI000BBE884E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7L1","uniProtkbId":"A0A291G7L1_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46399.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Heme A synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"HAS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"1.17.99.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Cytochrome aa3-controlling protein"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"ctaA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46399.1"}],"value":"CEW89_01735"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Catalyzes the conversion of heme O to heme A by two successive hydroxylations of the methyl group at C8. The first hydroxylation forms heme I, the second hydroxylation results in an unstable dihydroxymethyl group, which spontaneously dehydrates, resulting in the formyl group of heme A"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Fe(II)-heme o + 2 A + H2O = Fe(II)-heme a + 2 AH2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:63388"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:60530"},{"database":"ChEBI","id":"CHEBI:61715"}],"ecNumber":"1.17.99.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048044"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:63389"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048044"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001970"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044501"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Porphyrin-containing compound metabolism; heme A biosynthesis; heme A from heme O: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Interacts with CtaB"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"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:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"value":"Belongs to the COX15/CtaA family. Type 2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Transmembrane","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Transmembrane","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Transmembrane","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Transmembrane","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Transmembrane","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Transmembrane","location":{"start":{"value":316,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Transmembrane","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023133"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"id":"KW-0350","category":"Biological process","name":"Heme biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"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_01665"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01665"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46399.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46399.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46399.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804679.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7L1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_01588","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_01735","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793156at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00269","properties":[{"key":"RectionId","value":"UER00713"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0120547","properties":[{"key":"GoTerm","value":"F:heme A synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006784","properties":[{"key":"GoTerm","value":"P:heme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_01665","properties":[{"key":"EntryName","value":"HemeA_synth_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003780","properties":[{"key":"EntryName","value":"COX15/CtaA_fam"}]},{"database":"InterPro","id":"IPR054616","properties":[{"key":"EntryName","value":"HemA_synt_rhodobact"}]},{"database":"InterPro","id":"IPR023754","properties":[{"key":"EntryName","value":"HemeA_synthase_2"}]},{"database":"NCBIfam","id":"NF045570","properties":[{"key":"EntryName","value":"HemSynCtaAAlphapr"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23289","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX15"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23289:SF2","properties":[{"key":"EntryName","value":"CYTOCHROME C OXIDASE ASSEMBLY PROTEIN COX15 HOMOLOG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02628","properties":[{"key":"EntryName","value":"COX15-CtaA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATKRSIFEDVGTNEKPKETPKGGLIEKGRGGARKGIRAWLIVIFALVMAMIAVGGLTRLTDSGLSITEWKPVMGALPPMTAADWQVAFEKYQQTPEYRLQNEGMTLSEFKPLFLWEWGHRNLGRVIGLVWFLGYVRFAVAKKIPTGWHKRLIFIGALGGLQGAIGWWMVSSGLTGDRLDVASYRLAIHLGLAFIILGFIAWYVFLLGRTEPELMQARRAKDAKLFGMSTGMLHFAFLQILLGALVAGIDAGRGYTDWPLMGGQVLPPDPFYIEPLWRNFFENPALVQFLHRMAGYLLFIYGIVTWLKGRKSANRATASAFTLMAAVLFLQVILGITTLVHGAPLALGLAHQVGAVALFVAISRARFLSQYPQPQSVRSV","length":380,"molWeight":42066,"crc64":"76D3BF73D8B0D7E2","md5":"4EBF6D8A9AD19EF2F184745FCC4F3BA4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":8,"Region":1,"Compositional bias":1,"Binding site":2},"uniParcId":"UPI000BBE9226"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7L8","uniProtkbId":"A0A291G7L8_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":31,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46145.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthase small chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Carbamoyl phosphate synthetase glutamine chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"carA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46145.1"}],"value":"CEW89_00290"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Small 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 small subunit (glutamine amidotransferase) binds and cleaves glutamine to supply the large subunit with the substrate ammonia"}],"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":"ARBA","id":"ARBA00049285"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]}},{"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_01209"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"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_01209"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"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":"ARBA","id":"ARBA00007800"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"value":"Belongs to the CarA family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Carbamoyl-phosphate synthase small subunit N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01097"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"CPSase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}]},{"type":"Active site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":360,"modifier":"EXACT"},"end":{"value":360,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"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_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":321,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"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_01209"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01209"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46145.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46145.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46145.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804475.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7L8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00769","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00290","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804328at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00171"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"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:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050472","properties":[{"key":"EntryName","value":"Anth_synth/Amidotransfase"}]},{"database":"InterPro","id":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"NCBIfam","id":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418:SF7","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE SMALL CHAIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43418","properties":[{"key":"EntryName","value":"MULTIFUNCTIONAL TRYPTOPHAN BIOSYNTHESIS PROTEIN-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00097","properties":[{"key":"EntryName","value":"ANTSNTHASEII"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"PRINTS","id":"PR00096","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MASGQTTGKPTACLALADGTIFYGKGFGATGTTTAELCFNTAMTGYQEIMTDPSYAGQVVTFTFPHIGNVGVNSEDEETADPVAAGMIVKWDPTEPSNWRAQDELGPWLARHGRIGMGGIDTRRLTRAIRQQGAPHVAIAHDPEGNFDIEALVKQAREFSGLVGLDLAKDVTCAQSYKWDEMRWSWPDGFPKREGKGFKVVAVDFGAKRNILRCLASAGCDVTVLPAAATAEEVLAHDPDGVFLSNGPGDPAATGAYAVPMIKGVLERDLPVFGICLGHQMLALALGAKTIKMNHGHHGANHPVKDLDTGKVEITSMNHGFTVDTQTLPAGVKETHVSLFDGSNCGIAVEGKPVFSVQYHPEASPGPMDSYYLFERFAAAMAERAGAPA","length":389,"molWeight":41374,"crc64":"B5DF9FE2AE8EB76C","md5":"0DA4792C0CEDC1FC19F7F99BE2E315BD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Region":1,"Active site":3,"Binding site":8},"uniParcId":"UPI000BBF3806"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7M2","uniProtkbId":"A0A291G7M2_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":36,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46117.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015188"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"UDP-N-acetylenolpyruvoylglucosamine reductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012518"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"1.3.1.98"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031026"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"UDP-N-acetylmuramate dehydrogenase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"murB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46117.1"}],"value":"CEW89_00120"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003921"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"Cell wall formation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramate + NADP(+) = UDP-N-acetyl-3-O-(1-carboxyvinyl)-alpha-D-glucosamine + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12248"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:68483"},{"database":"ChEBI","id":"CHEBI:70757"}],"ecNumber":"1.3.1.98","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048914"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004752"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"value":"Belongs to the MurB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"FAD-binding PCMH-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51387"}]},{"type":"Region","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}]},{"type":"Active site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}]},{"type":"Active site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"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_00037"}],"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_00037"}],"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_00037"}],"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_00037"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00037"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46117.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46117.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46117.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804454.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7M2","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00804","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00120","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804753at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0071949","properties":[{"key":"GoTerm","value":"F:FAD binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008762","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramate dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071555","properties":[{"key":"GoTerm","value":"P:cell wall organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.465.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.78.10","properties":[{"key":"EntryName","value":"UDP-N-acetylenolpyruvoylglucosamine reductase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.43.10","properties":[{"key":"EntryName","value":"Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00037","properties":[{"key":"EntryName","value":"MurB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016166","properties":[{"key":"EntryName","value":"FAD-bd_PCMH"}]},{"database":"InterPro","id":"IPR036318","properties":[{"key":"EntryName","value":"FAD-bd_PCMH-like_sf"}]},{"database":"InterPro","id":"IPR016167","properties":[{"key":"EntryName","value":"FAD-bd_PCMH_sub1"}]},{"database":"InterPro","id":"IPR016169","properties":[{"key":"EntryName","value":"FAD-bd_PCMH_sub2"}]},{"database":"InterPro","id":"IPR003170","properties":[{"key":"EntryName","value":"MurB"}]},{"database":"InterPro","id":"IPR011601","properties":[{"key":"EntryName","value":"MurB_C"}]},{"database":"InterPro","id":"IPR036635","properties":[{"key":"EntryName","value":"MurB_C_sf"}]},{"database":"InterPro","id":"IPR006094","properties":[{"key":"EntryName","value":"Oxid_FAD_bind_N"}]},{"database":"NCBIfam","id":"NF010480","properties":[{"key":"EntryName","value":"murB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00179","properties":[{"key":"EntryName","value":"murB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21071","properties":[{"key":"EntryName","value":"UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21071:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLENOLPYRUVOYLGLUCOSAMINE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01565","properties":[{"key":"EntryName","value":"FAD_binding_4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02873","properties":[{"key":"EntryName","value":"MurB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56176","properties":[{"key":"EntryName","value":"FAD-binding/transporter-associated domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56194","properties":[{"key":"EntryName","value":"Uridine diphospho-N-Acetylenolpyruvylglucosamine reductase, MurB, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51387","properties":[{"key":"EntryName","value":"FAD_PCMH"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIYPETRGKLTENRTLSDLTWLRVGGPADALFQPADLEDLQGFLANLAPSVAVFPMGVGSNLIVRDGGIRAVVIRMGRGFNGIGIEGNRVTAGVAALDAHVARKAAEAGLDLTFLRTIPGAIGGAVRMNAGCYGSYVADHFVSARAVTRAGELVTLTAEDLSFQYRQTDLPEGWVIVEATFEAESADPEMLNSRMDDQLAKRDATQPVKERSAGSTFRNPAGFSSTGRADDVHDLKAWKVIDDAGLRGFSIGGAQMSEKHSNFMINMGAATAQDLELLGETVRKKVFQNAGLALQWEIKRIGEFSGDPIPDGLAEAQNSEA","length":321,"molWeight":34313,"crc64":"436465D1554D299E","md5":"4EB685E87245092B81C8748F3887EDEC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":3},"uniParcId":"UPI000BBF1D31"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7M5","uniProtkbId":"A0A291G7M5_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":34,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46155.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Octanoyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"2.3.1.181"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Lipoate-protein ligase B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Lipoyl/octanoyl transferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"lipB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46155.1"}],"value":"CEW89_00345"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024732"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octanoyl-[ACP] + L-lysyl-[protein] = N(6)-octanoyl-L-lysyl-[protein] + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17665"},{"database":"Rhea","id":"RHEA-COMP:9636"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:9928"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78463"},{"database":"ChEBI","id":"CHEBI:78809"}],"ecNumber":"2.3.1.181","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004821"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Belongs to the LipB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"BPL/LPL catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51733"}]},{"type":"Active site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-1"}]},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"Lowers pKa of active site Cys","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46155.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"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_00013"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46155.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46155.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46155.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A291G7M5","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00759","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00345","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9787061at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00538","properties":[{"key":"RectionId","value":"UER00592"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0033819","properties":[{"key":"GoTerm","value":"F:lipoyl(octanoyl) transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009249","properties":[{"key":"GoTerm","value":"P:protein lipoylation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16444","properties":[{"key":"EntryName","value":"LipB"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00013","properties":[{"key":"EntryName","value":"LipB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR004143","properties":[{"key":"EntryName","value":"BPL_LPL_catalytic"}]},{"database":"InterPro","id":"IPR000544","properties":[{"key":"EntryName","value":"Octanoyltransferase"}]},{"database":"InterPro","id":"IPR020605","properties":[{"key":"EntryName","value":"Octanoyltransferase_CS"}]},{"database":"NCBIfam","id":"NF010921","properties":[{"key":"EntryName","value":"lipB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF010925","properties":[{"key":"EntryName","value":"lipB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00214","properties":[{"key":"EntryName","value":"lipB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10993:SF7","properties":[{"key":"EntryName","value":"LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10993","properties":[{"key":"EntryName","value":"OCTANOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21948","properties":[{"key":"EntryName","value":"LplA-B_cat"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF016262","properties":[{"key":"EntryName","value":"LPLase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51733","properties":[{"key":"EntryName","value":"BPL_LPL_CATALYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01313","properties":[{"key":"EntryName","value":"LIPB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVEWRISEGLTDYDFAVAEMEARAEAIARGEAEELIWLVEHPPLYTAGTSAKREDLVDPDRFPVYESKRGGQYTYHGPGQRVAYAMLDLNTRGKDVRKFVADMEAWVIAALAEFNVTGEIREGRVGVWVVREDKPLTITGAKPEDKIAAIGLRVRKWVSFHGLSINVEPDLSHFGGIVPCGIRDHGVTSLVDLGLPVTMEDVDIALRRAFDEVFGD","length":216,"molWeight":24042,"crc64":"C32707B44DF52B61","md5":"CA44A31EF01251C61F6653A0BA49438E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":3,"Site":1},"uniParcId":"UPI0008331AD4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7N6","uniProtkbId":"A0A291G7N6_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2017-12-20","entryVersion":28,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46138.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"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"}],"value":"gatB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46138.1"}],"value":"CEW89_00240"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097267"},{"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"}],"features":[{"type":"Domain","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":503,"modifier":"EXACT"}},"description":"Asn/Gln amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00845"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"Cradle","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Region","location":{"start":{"value":444,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"Tail","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"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":31,"modifier":"EXACT"},"end":{"value":31,"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":144,"modifier":"EXACT"},"end":{"value":144,"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":172,"modifier":"EXACT"},"end":{"value":172,"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":175,"modifier":"EXACT"},"end":{"value":175,"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":214,"modifier":"EXACT"},"end":{"value":214,"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":218,"modifier":"EXACT"},"end":{"value":218,"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":238,"modifier":"EXACT"},"end":{"value":238,"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":240,"modifier":"EXACT"},"end":{"value":240,"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":242,"modifier":"EXACT"},"end":{"value":242,"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":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46138.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46138.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46138.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46138.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804470.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7N6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00779","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00240","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804078at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0050566","properties":[{"key":"GoTerm","value":"F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"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":"FunFam","id":"1.10.150.380: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":"MLDHLEYSAPKPKVISGAKEDWELVIGMEIHAQVASEAKLFSGASTGFGAEPNSHVSFVDAAMPGMLPVINEYCVEQAVRTGLGLKADINLFSAFDRKNYFYPDLPQGYQISQLYHPIVGEGEVIVDMEPGVARKVRIERIHLEQDAGKSIHDMDPTMSFVDLNRTGVALMEIVSRPDIRGPEEAAAYVLKLRQILRYLGTCDGNMQNGNLRADVNVSVCRPGQYEKYQETQDFSHLGTRCEIKNMNSTRFIQAAIDYEARRQIAILEDGGTVDQETRLYDAAKNETRSMRSKEEAHDYRYFPCPDLLPLEIEQAWVDDIAKTLPELPDEKKARFVKDFGLSEYDAGVLTADTVNADFFEKVVAVGEDGKLSANWVINELFGRLKKDDTDITESPVTPEQLGEIVKLIKADTISGKIAKDLFEIVYTEGGNPAEIVEARGMKQVTDTGAIEAAVDEIIAANPAQVEKAKANPKLAGWFVGQVMKATGGKANPKAVDALVKSKLGL","length":505,"molWeight":55707,"crc64":"AA20CF0B372BF66F","md5":"09E7A89958C8C87E463B4F0A6612EA7A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":10},"uniParcId":"UPI000BBEAC0E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7Q2","uniProtkbId":"A0A291G7Q2_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":31,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46104.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"6.3.2.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"value":"D-alanyl-D-alanine-adding enzyme"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"value":"murF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46104.1"}],"value":"CEW89_00050"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"Involved in cell wall formation. Catalyzes the final step in the synthesis of UDP-N-acetylmuramoyl-pentapeptide, the precursor of murein"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-alanyl-D-alanine + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimeloyl-D-alanyl-D-alanine + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28374"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57822"},{"database":"ChEBI","id":"CHEBI:61386"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004136"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"value":"Belongs to the MurCDEF family. MurF subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":442,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"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_02019"}],"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_02019"}],"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_02019"}],"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_02019"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02019"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46104.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46104.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46104.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_096804446.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7Q2","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_00819","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00050","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9800958at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0047480","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoyl-tripeptide-D-alanyl-D-alanine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008766","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamyl-2,6-diaminopimelate-D-alanyl-D-alanine ligase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0071555","properties":[{"key":"GoTerm","value":"P:cell wall organization"},{"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":"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_02019","properties":[{"key":"EntryName","value":"MurF"},{"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":"IPR051046","properties":[{"key":"EntryName","value":"MurCDEF_CellWall_CoF430Synth"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005863","properties":[{"key":"EntryName","value":"UDP-N-AcMur_synth"}]},{"database":"NCBIfam","id":"TIGR01143","properties":[{"key":"EntryName","value":"murF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43024","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43024:SF1","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-TRIPEPTIDE--D-ALANYL-D-ALANINE LIGASE"},{"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":"MALWTSEEAAKATGGRATQAFDISGVSIDTRTIQPGDLFVALKDVRDGHEFVAQALDKGAAAALVSRIPEGVTADAPLLIVDEVLPALERLGAAARARMTGKVIGVTGSVGKTSTKEMLRAILSGQGKTHAAEASYNNHWGVPLTLARMPADTDFAVIEIGMNHPGEIAPLAKLARPDVAMITTVAPAHMAAFESLEGIAREKSDIFKGLVPGGVAVFNGDLEVSDILAAAWDGDTIRFGEDEACAAQLTSVELSDGATQGSAVIDTTHLEFRLSTAGRHFAANAVGCLAVAYALGLDLEKAAADLVLWAPPEGRGAREQVQLAVGAPVDLIDDAFNANPTSMAAALEVLAKAEPHDTGRRIAILGDMLELGEKERAIHEGLAALPWFAAVDAVHCVGPLMRALYDALPAERCGVWFETAKDAVPALQTLVGPGDVVLVKGSKGSKVSLLVDALRELGQVPQQTDER","length":467,"molWeight":48760,"crc64":"228DA8FCEA904D3A","md5":"FE3F41D7BB3FF8B03941555DED95CAD5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":3,"Binding site":1},"uniParcId":"UPI000BBE123C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A291G7R0","uniProtkbId":"A0A291G7R0_9RHOB","entryAudit":{"firstPublicDate":"2017-12-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2017-12-20","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Celeribacter ethanolicus","taxonId":1758178,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46201.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Rhodobacterales","Roseobacteraceae","Celeribacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"Glucose-1-phosphate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"2.7.7.27"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"ADP-glucose pyrophosphorylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"ADPGlc PPase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"ADP-glucose synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46201.1"}],"value":"glgC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46201.1"}],"value":"CEW89_00620"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"Involved in the biosynthesis of ADP-glucose, a building block required for the elongation reactions to produce glycogen. Catalyzes the reaction between ATP and alpha-D-glucose 1-phosphate (G1P) to produce pyrophosphate and ADP-Glc"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 1-phosphate + ATP + H(+) = ADP-alpha-D-glucose + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12120"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57498"},{"database":"ChEBI","id":"CHEBI:58601"}],"ecNumber":"2.7.7.27","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"Glycan biosynthesis; glycogen biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010443"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"Belongs to the bacterial/plant glucose-1-phosphate adenylyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Domain","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Glucose-1-phosphate adenylyltransferase/Bifunctional protein GlmU-like C-terminal hexapeptide","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24894"}]},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58601"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"ligand":{"name":"alpha-D-glucose 1-phosphate","id":"ChEBI:CHEBI:58601"}},{"type":"Binding site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58601"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"ligand":{"name":"alpha-D-glucose 1-phosphate","id":"ChEBI:CHEBI:58601"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58601"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"ligand":{"name":"alpha-D-glucose 1-phosphate","id":"ChEBI:CHEBI:58601"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58601"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"ligand":{"name":"alpha-D-glucose 1-phosphate","id":"ChEBI:CHEBI:58601"}},{"type":"Site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"Could play a key role in the communication between the regulatory and the substrate sites","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}]},{"type":"Site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Could play a key role in the communication between the regulatory and the substrate sites","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"id":"KW-0320","category":"Biological process","name":"Glycogen biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022600"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"id":"KW-0321","category":"Biological process","name":"Glycogen metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"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_00624"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-4N4BP055OVPC9","citationType":"submission","authors":["Woo J.-H.","Kim H.-S."],"title":"Celeribacter sp. TSPH2 complete genome sequence.","publicationDate":"JUN-2017","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46201.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}],"value":"TSPH2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"ATG46201.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000217935"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP022196","properties":[{"key":"ProteinId","value":"ATG46201.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_066711252.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP022196.1"}]},{"database":"AlphaFoldDB","id":"A0A291G7R0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1758178.GCA_001550095_03511","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"ceh:CEW89_00620","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801810at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00164","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000217935","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0008878","properties":[{"key":"GoTerm","value":"F:glucose-1-phosphate adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005978","properties":[{"key":"GoTerm","value":"P:glycogen biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02508","properties":[{"key":"EntryName","value":"ADP_Glucose_PP"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04651","properties":[{"key":"EntryName","value":"LbH_G1P_AT_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_00624","properties":[{"key":"EntryName","value":"GlgC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011831","properties":[{"key":"EntryName","value":"ADP-Glc_PPase"}]},{"database":"InterPro","id":"IPR005836","properties":[{"key":"EntryName","value":"ADP_Glu_pyroP_CS"}]},{"database":"InterPro","id":"IPR023049","properties":[{"key":"EntryName","value":"GlgC_bac"}]},{"database":"InterPro","id":"IPR056818","properties":[{"key":"EntryName","value":"GlmU/GlgC-like_hexapep"}]},{"database":"InterPro","id":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"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":"TIGR02091","properties":[{"key":"EntryName","value":"glgC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001947","properties":[{"key":"EntryName","value":"PRK00725.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002023","properties":[{"key":"EntryName","value":"PRK00844.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43523:SF2","properties":[{"key":"EntryName","value":"GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43523","properties":[{"key":"EntryName","value":"GLUCOSE-1-PHOSPHATE ADENYLYLTRANSFERASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24894","properties":[{"key":"EntryName","value":"Hexapep_GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"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":"PS00809","properties":[{"key":"EntryName","value":"ADP_GLC_PYROPHOSPH_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00810","properties":[{"key":"EntryName","value":"ADP_GLC_PYROPHOSPH_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPNSRNRLAPRTMAFVLAGGRGSRLKELTNDRVKPAVYFGGKNRIVDFALSNALNSGIRKMAIATQYKAHSLIRHIQRGWTFFRAERNEFLDILPASQRYEESTWYRGTADAVAQNIDIIDSYNVDYILILAGDHIYKMDYEVMIRQHVDTNADVTIGCLTVDRKEASAFGVMGVDATDRITSFLEKPVDPPAIPGEPSKSLASMGIYVFNWKFLRERLLEDMEDPNSSHDFGNDLIPELVKKGKAQAHRFTDSCVRPEGAEAYWRDVGTIDAYWKANIDLTDFTPELDLWDREWPIWTYSELTPPAKFIHDRPDRRGSAVSSMVSGGCIISGTEIRESLLFTHVRTNSYSSLERAVVLPYANIARHCQLKNVVIDRGVQVPEGLVVGEDPEVDAKWFRVSPGGVTLITQEMLDRRAQGL","length":420,"molWeight":47405,"crc64":"C0BD788DA8C172AB","md5":"98C22DCDA24312BD642A7B6D52CD73CD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Binding site":4,"Site":2},"uniParcId":"UPI0008296D20"}}]}