{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JY01","uniProtkbId":"A0A3G9JY01_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50377.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase subunit PdxT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"4.3.3.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pdx2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase glutaminase subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"3.5.1.2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50377.1"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50377.1"}],"value":"Pcatena_09640"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054599"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS"}],"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"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31507"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"4.3.3.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047992"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Belongs to the glutaminase PdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"value":"Belongs to the glutamine amidotransferase pdxT/SNO family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50377.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH50377.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126422155.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JY01","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88849097","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_09640","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9810320at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00245","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"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"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MATAVLAVQGAFAEHEARLAELGETCVELRQASDLRQRFDRLVLPGGESTTQGKLLAELGMLEPLRERIEDGLPVLATCAGLILLARRLDAHDDRDTPRIATLDVLVRRNAYGRQLGSFRTSLELAGMGTVPATFIRAPFVMETGRGVETLATCDGNVVAVQQGKQLALAFHPELDEDPRIHQLFLDL","length":188,"molWeight":20527,"crc64":"EE43B2891BC666BD","md5":"13D96A47134860B30F7A53CC5E9347E0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI000F70A282"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9K339","uniProtkbId":"A0A3G9K339_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":26,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50956.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ATP-dependent zinc metalloprotease FtsH"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"3.4.24.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50956.1"}],"value":"ftsH_2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ftsH"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50956.1"}],"value":"Pcatena_15430"}]}],"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"}],"features":[{"type":"Transmembrane","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Transmembrane","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":639,"modifier":"EXACT"},"end":{"value":688,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":639,"modifier":"EXACT"},"end":{"value":648,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":657,"modifier":"EXACT"},"end":{"value":676,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":232,"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":447,"modifier":"EXACT"},"end":{"value":447,"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":451,"modifier":"EXACT"},"end":{"value":451,"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":523,"modifier":"EXACT"},"end":{"value":523,"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":"BBH50956.1"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50956.1"}],"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":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH50956.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126423178.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9K339","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88849683","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_15430","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9809379at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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":"3.40.50.300","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":"MSSNDENNNQPGGPQRGPNPPRTSAISLIIAIALVAYLVYSMVPSMFGVSGTDSIPTSDVVAAVQDNRVSTLTYRVSSGELTGTYWTDDSDKGNDDKLVSFKSTYAGTDNLAELMESHPEVRYTVDTSSDEWLDTLVFSVLPTLLMVGVFIYFMRGMQGQGGGAMGFGKTKAKTTEETRPKVKFSDVAGVDEAVEELKEIRDFLAEPERFHKMGAKIPRGVLLVGPPGTGKTLLAKAVAGEAGVPFFSISGSDFVEMFVGVGASRVRDLFKQAKAASPSIIFIDEIDAVGRQRGAGLGGGHDEREQTLNQLLVEMDGFEANDAVILIAATNRPDILDPALLRPGRFDRQVTVDRPDLSGREQIIRVHSEGKPLAGDVDFGRLAKLTPGFTGADLMNLMNESALLAARRHKSKITMDEVEEAMERVIAGPERKSRVMTESERKTIAYHESGHALVGHILENSDPVHKISIIARGQALGYTLQLPEEDHFLNTRDGMLDQIAVLLGGRTAEELFCDDITTGASNDLERATKIARQMVTRLGMSEALGTQVFGEAQHEVFLGRDYADHQDYSAETAKRIDDEVERIMREAHNRAREVLEARRDQMDTMAKVLLERETVEGDVVNALLDDEWDEYVAAHPEAAQAEAPAAKPGELDEDAAAEAAEAARAAVAAEEAGESAAPDDSSKTETSE","length":688,"molWeight":74643,"crc64":"57F9B11FAF67B22F","md5":"1E23C00C251B9888E3DFB54389C8DF1F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3},"countByFeatureType":{"Transmembrane":2,"Domain":1,"Region":2,"Compositional bias":2,"Active site":1,"Binding site":4},"uniParcId":"UPI000F70F43E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9K6L0","uniProtkbId":"A0A3G9K6L0_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49684.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"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":"BBH49684.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49684.1"}],"value":"Pcatena_02710"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":136,"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":238,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":371,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":12,"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":23,"modifier":"EXACT"},"end":{"value":23,"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":80,"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":85,"modifier":"EXACT"},"end":{"value":86,"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":110,"modifier":"EXACT"},"end":{"value":110,"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":147,"modifier":"EXACT"},"end":{"value":147,"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":162,"modifier":"EXACT"},"end":{"value":162,"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":178,"modifier":"EXACT"},"end":{"value":178,"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":236,"modifier":"EXACT"},"end":{"value":236,"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":236,"modifier":"EXACT"},"end":{"value":236,"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":341,"modifier":"EXACT"},"end":{"value":341,"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":374,"modifier":"EXACT"},"end":{"value":374,"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":385,"modifier":"EXACT"},"end":{"value":385,"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":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":395,"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":413,"modifier":"EXACT"},"end":{"value":413,"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":431,"modifier":"EXACT"},"end":{"value":431,"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":448,"modifier":"EXACT"},"end":{"value":448,"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":"UP000273154"}],"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-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49684.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420966.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9K6L0","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848418","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_02710","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":"UP000273154","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":"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":"PF14602","properties":[{"key":"EntryName","value":"Hexapep_2"},{"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":"MANATAIILAAGEGTRMKSNHAKVSHKILGKPMIRWVADAAIAGGCDRVVIVVGSHADEVRAIAEAAYADSDARVECVEQTERLGTGHAVKVALEATGIDAGPVVVLNGDLPLVTAETIRAFAESVSDGKAAATAFTITPPDPFGYGRIVLAADGTIERNIEQKDCTPEQAASLTECNAGCYAFDGALLAAHIGEVGCDNAQGEYYLPDMLEILKSHGQAVRAFHCDDYREGLGVNSRAQLAQLTAIARDRINEQLMDQGVTFIDPAQAWIGPDCTIGRDTVVWPQTHLIGECHVGADCQLGPNTRLTNTSAGDGCVIDETVAIDAKLENAVDCGPRAYLRPGTHMLNGSKAGTHVEIKKSTIGEGSKVPHLSYIGDTTMGSGVNMGAGSITCNYDGVHKHKTHIGNDVFVGSDTMIVAPGEIGDGALVAAGSVVTEPVPADALSVGRARQKNIEGWAHKHFEALRAQK","length":469,"molWeight":49175,"crc64":"329C094E57157A40","md5":"025FB98BBD2B718C8C29A9906D2D7A42"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":19},"uniParcId":"UPI000F6F80C2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9K8A1","uniProtkbId":"A0A3G9K8A1_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":31,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50904.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"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:0000313","source":"EMBL","id":"BBH50904.1"}],"value":"yjeF"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50904.1"}],"value":"Pcatena_14910"}]}],"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":12,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":62,"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":59,"modifier":"EXACT"},"end":{"value":59,"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":128,"modifier":"EXACT"},"end":{"value":128,"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":161,"modifier":"EXACT"},"end":{"value":161,"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:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"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":335,"modifier":"EXACT"},"end":{"value":335,"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":392,"modifier":"EXACT"},"end":{"value":392,"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":434,"modifier":"EXACT"},"end":{"value":438,"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":462,"modifier":"EXACT"},"end":{"value":462,"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":463,"modifier":"EXACT"},"end":{"value":463,"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:0000313","source":"EMBL","id":"BBH50904.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"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":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50904.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH50904.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A3G9K8A1","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_14910","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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":"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":"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":"MGMQPVLNVEDIKAVETRLSDAGVSISELMHRAGGAAAQEVLRLGDVSRAVVLAGFGNNGGDGWVAAEELKAAGVDVRVVTPCEPDQLHSDLARMVAKAAVEAGVVYVVGPARDELDVLLGGCDAVLDAMLGTGFHDAPVAPLSIWIDALNSSGARVVSVDVPSGLSAQTGHAPGAVVVADVTITMLALKPGLLSDDGRDVCGSIVVAPLAEQTAKLVYEADPVAWRCEATDYLDVLVPPTSVVDKYSRGSVLVVGGSTRFPGAAIMAAKSAARAGAGYVTLAVPEPIANLCRTHLLEIPVVGLPADADGTFSNEARAQVAQLAERRSAVLVGPGMCVTGGTVGVVSTLLESEAPLVIDADGLNSLARLTSNRLDEFPELLRRKAPLVLTPHRRELGRLVGLTDATPNSLTSALEAARRIVWADGGSELVVVAKGTATACVGVEIAMLPKPGPACLATAGSGDVLAGITAGLLARGVETESLPTLTAFACEVHGYAASIAQERFGTRGVMAADIIDCVGLAVDAVEDRAAFSGADDMAPSDEDDARN","length":547,"molWeight":55934,"crc64":"137D4ED37777DD72","md5":"96F4AC56E6491F209AC48D527D8CA0FB"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":11},"uniParcId":"UPI000F6BAE18"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9K8Z8","uniProtkbId":"A0A3G9K8Z8_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50989.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable 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":"BBH50989.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50989.1"}],"value":"Pcatena_15760"}]}],"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"}],"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":"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":107,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"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":125,"modifier":"EXACT"},"end":{"value":125,"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":128,"modifier":"EXACT"},"end":{"value":128,"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":168,"modifier":"EXACT"},"end":{"value":169,"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":200,"modifier":"EXACT"},"end":{"value":200,"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":223,"modifier":"EXACT"},"end":{"value":225,"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":299,"modifier":"EXACT"},"end":{"value":299,"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":"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":"UP000273154"}],"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-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH50989.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126423236.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9K8Z8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88849718","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_15760","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSIHDTESSSRKVDLRTLSHEQLVDLMEQLGYPKFRAKQVEDWVWKHNVSDFQEMTNVPAALRADLSARCTLGGTSEVARQVSSDGSRKYLLRYSDGTQAECVGMPTRNRLAVCVSTQAGCRMGCVFCATGQGGFTRSLKATEIYDQVMHVSEDFQTRASSVVMMGQGEPFNNYDEVIKALRMLNSPEGAGIGARHLTVSTCGVIPMIRRFSKEPEQFTLAVSLHSAIQSTRNAIMPGVKKHTLQRLHDVMGEYVEATGRRPTYEYALIGGVNDNNAELEALCDFTRGTLAHVNLIQLNDLEDSRLKPSTQERAELFVRRLAQVGVEATIRNSRGNDIDAACGQLSQKHQE","length":351,"molWeight":38933,"crc64":"21B8BD3C88938B3D","md5":"E4D72363689CFC8EB27AFF6E603F88E9"},"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":"UPI000F6F9594"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9K9T2","uniProtkbId":"A0A3G9K9T2_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50040.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"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"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50040.1"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50040.1"}],"value":"Pcatena_06270"}]}],"comments":[{"texts":[{"evidences":[{"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":267,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":531,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":512,"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":514,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"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":141,"modifier":"EXACT"},"end":{"value":141,"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":148,"modifier":"EXACT"},"end":{"value":150,"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":188,"modifier":"EXACT"},"end":{"value":193,"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":188,"modifier":"EXACT"},"end":{"value":193,"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":224,"modifier":"EXACT"},"end":{"value":224,"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":224,"modifier":"EXACT"},"end":{"value":224,"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":357,"modifier":"EXACT"},"end":{"value":357,"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":385,"modifier":"EXACT"},"end":{"value":388,"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":408,"modifier":"EXACT"},"end":{"value":408,"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":465,"modifier":"EXACT"},"end":{"value":465,"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":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH50040.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126421549.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9K9T2","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848757","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_06270","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801107at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000273154","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":"MTKHIFVTGGVVSSLGKGITAASLGRLLKSRGYKVMMQKADPYLNVDPGTMSPFQHGEVFVTEDGYESDLDLGHYERFIDENLTRNSNFTTGAIYQSLIARERRGDFLGGTVQVIPHVTNAIKERFRRVEEQTGADVVITELGGTIGDIEGQAFVEAIRQFRKEKGTADCCLIHVSLVPYIAAAHEVKTKPTQHSVRELRSMGIQPDFIMCRSDHEVDESIRAKIASFCDVEPDHVFENSDCASIYDVPEHLARQGFDLKVCERLGLDPRKSDMSEWYGFTSRMHEANDKADVTKIAVVGKYTQLPDAYLSVIEALHHSGVYYGRHVDINLIDGENLTEDDVEQVLGDADGILVPGGFGIRGLEGKILATHRARTTGTPFLGICLGLQVAVCEYARNVAGMPGASSTEFVPDCEYPVIDLMPDQEDVTSKGGTMRLGAYPCKVAEGTLAREAYGEELVYERHRHRFEVNNAYREKLHQAGLTFSGVSPDDRLVEMVELPEDVHPWFVAAQFHPEFKSRPTRPQPLFREFVRAAIARHEGVDRHEVNAGE","length":549,"molWeight":61059,"crc64":"BE11021AC6A6AE65","md5":"6414CC3962A8CC74DCCDC2EF79560197"},"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":15},"uniParcId":"UPI000F6CC089"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9K9Y2","uniProtkbId":"A0A3G9K9Y2_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50210.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50210.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH50210.1"}],"value":"Pcatena_07970"}]}],"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":10,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":399,"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":194,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":283,"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":293,"modifier":"EXACT"},"end":{"value":293,"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":310,"modifier":"EXACT"},"end":{"value":313,"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":328,"modifier":"EXACT"},"end":{"value":328,"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":342,"modifier":"EXACT"},"end":{"value":342,"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":346,"modifier":"EXACT"},"end":{"value":346,"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":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH50210.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126421839.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9K9Y2","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848924","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_07970","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802554at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000273154","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":"MAETLVDGHAARVALFVTGGIAAYKACEVLRGLQKQGCEVRVAMSAHACELVGPKTFEALSGHHVTLGLFDDASSPIPHIELAEWADLALVCPATANVIAKMAHGIADDAVSTTLLACPCPVVVAPAMNVHMWQNLATVANVETLKNRNYLFVGPESGRLACGETGAGKLASIEQIVSAALYRIRARGDLAGRRIVITAGPTHEPVDPVRYLSNASSGKMGYAIAAAAAAHGAHVTLVSGPVSLPEPAGVGVIHVTTAAQMLEATQDAFATADAAILAAAVSDYRPEQAADHKLKKAAEPIDNIALAENPDILATLSQSRGSRVVIGFAAETDNVLENARKKLATKGCDLIVANDVSRDDSTFGSDTNRVTLVGPHDETELDCMPKEQVAEKIIERLHDLLEPDEPLQQASAADQTLLMPRTGADC","length":426,"molWeight":44616,"crc64":"ADC562EF442F34B5","md5":"756D3E3FFA4CC37C8E2DEEA7B677A952"},"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":"UPI000F6CAC02"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9KAH5","uniProtkbId":"A0A3G9KAH5_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":29,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49975.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49975.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49975.1"}],"value":"Pcatena_05620"}]}],"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":1068,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5048910363"},{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":676,"modifier":"EXACT"},"end":{"value":867,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":935,"modifier":"EXACT"},"end":{"value":1068,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":552,"modifier":"EXACT"},"end":{"value":934,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":935,"modifier":"EXACT"},"end":{"value":1068,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":712,"modifier":"EXACT"},"end":{"value":712,"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":751,"modifier":"EXACT"},"end":{"value":751,"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":753,"modifier":"EXACT"},"end":{"value":753,"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":758,"modifier":"EXACT"},"end":{"value":758,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":783,"modifier":"EXACT"},"end":{"value":783,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":784,"modifier":"EXACT"},"end":{"value":784,"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":785,"modifier":"EXACT"},"end":{"value":785,"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":786,"modifier":"EXACT"},"end":{"value":786,"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":826,"modifier":"EXACT"},"end":{"value":826,"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":826,"modifier":"EXACT"},"end":{"value":826,"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":826,"modifier":"EXACT"},"end":{"value":826,"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":838,"modifier":"EXACT"},"end":{"value":838,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":838,"modifier":"EXACT"},"end":{"value":838,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":838,"modifier":"EXACT"},"end":{"value":838,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI: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":838,"modifier":"EXACT"},"end":{"value":838,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"3"}},{"type":"Binding site","location":{"start":{"value":838,"modifier":"EXACT"},"end":{"value":838,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Binding site","location":{"start":{"value":840,"modifier":"EXACT"},"end":{"value":840,"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":840,"modifier":"EXACT"},"end":{"value":840,"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":"UP000273154"}],"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-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49975.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126421444.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9KAH5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848696","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_05620","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":"UP000273154","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:000026","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"1"}]},{"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":"MPKRTDIKKILVIGSGPIVIGQACEFDYSGTQACESLKALGYEVVLVNSNPATIMTDPGIADRTYVEPITADSVAKVIERERPDALLPNMGGQTGLNCAIELDEAGVLSKYGVEVIGCNTESIRIGEDRKLFAEAMEDIGLHICRSGFAYSVADAERIVGELGFPVIIRPSFTLGGAGGGIAYDMDDLRRIVAQGIDLSPEGEVLVEESIQDWKEIEMEVMRDCAGNGIVICSIENLDPMGVHTGDSITVAPAQTLSDTELQRLRDYSLAILEKVGVATGGSNVQFAVNPEDGRIIVVEMNPRVSRSSALASKATGFPIAKVAARLAVGLTLDEVTNDITQATPACFEPSIDYCVVKVPRFAFEKFKGTDETLSTRMKAVGEVMAIGRTFEESFNKAMRSLEVGENMLGADDPALYDVPDFRQRVSVPTAQRIYYVIEALRRGWSIEDIHELTGIDPWYLSHLKNLTDTEGWLAERRLTDISERDMRSVKQMGFSDEQIAHFTGSTELEVRAWRKAKGVTPAIKTVDTCGGEFPARTSYHYKTYEWGPSERRDTDKPRAMILSAGPNRIGQGIEFDYCCCHAAYALHDKGYETVMVNCNPETVSTDYDTSDRLYFEPLTFEDVMDIVDVEQPEGVICTLGGQTPINLAARLKAAGVPIMGTQPDALDLAEDRERFSALLDELDIAYPVSGVAETYEEAVEVAHRIGFPLLVRPSYVLGGRGMVIAYDERHLKSYMEAATRVSKDHPIYLDSFLDSAVELDVDALADGEQCYVGSVLEQIEEAGIHSGDSACCMPPYSLADSMIAEIRETTHKLALACHVVGALNVQYAVHNGRLYVIELNPRASRTVPFSSKSTGVPLARMAAKIMAGEKICDLGLPPEDRTFDYFACKETVLPFDRFPGADMTLGPEMKSTGEVMGVAPTFPAAYAKTQLAISYGLPTKGRVFISVRDRDKRAIIGVARDLVGMGFELVGTTGTAKALRAAGIDCKSVRRASEMRPNIATMLSGGDIQLIINTPGGHDTRGDFYTLRQLAVRYRVTNVTTLAGAQAMTEAIRTARAGSLDVVALQDL","length":1068,"molWeight":116340,"crc64":"4CA5AD5E44BEE833","md5":"3E2A9FF1C194BD54656D3A552C55E2DB"},"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":3,"Binding site":38,"Lipidation":2},"uniParcId":"UPI000F6D8803"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVD8","uniProtkbId":"A0A3G9JVD8_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49431.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00665"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"Replicative DNA helicase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00665"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"5.6.2.3"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49431.1"}],"value":"dnaB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49431.1"}],"value":"Pcatena_00180"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating dsDNA into templates for DNA synthesis. A processive ATP-dependent 5'-3' DNA helicase it has DNA-dependent ATPase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048954"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093875"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008428"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"Belongs to the helicase family. DnaB subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"SF4 helicase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51199"}]},{"type":"Region","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022705"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022515"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0639","category":"Cellular component","name":"Primosome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49431.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_232619854.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVD8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848160","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_00180","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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:1990077","properties":[{"key":"GoTerm","value":"C:primosome complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006269","properties":[{"key":"GoTerm","value":"P:DNA replication, synthesis of primer"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00984","properties":[{"key":"EntryName","value":"DnaB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.860.10","properties":[{"key":"EntryName","value":"DNAb Helicase, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR036185","properties":[{"key":"EntryName","value":"DNA_heli_DnaB-like_N_sf"}]},{"database":"InterPro","id":"IPR007692","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB"}]},{"database":"InterPro","id":"IPR007694","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB-like_C"}]},{"database":"InterPro","id":"IPR007693","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB-like_N"}]},{"database":"InterPro","id":"IPR016136","properties":[{"key":"EntryName","value":"DNA_helicase_N/primase_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR00665","properties":[{"key":"EntryName","value":"DnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30153:SF2","properties":[{"key":"EntryName","value":"REPLICATIVE DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30153","properties":[{"key":"EntryName","value":"REPLICATIVE DNA HELICASE DNAB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00772","properties":[{"key":"EntryName","value":"DnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03796","properties":[{"key":"EntryName","value":"DnaB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48024","properties":[{"key":"EntryName","value":"N-terminal domain of DnaB helicase"},{"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":"PS51199","properties":[{"key":"EntryName","value":"SF4_HELICASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDEIVYDAAPSPMALASIKSMPSHPDAERSVLSAMMLSPEVLESALVELSEVDFFVDANRIVFAAMRTMFERGIALDPISLADYLTSNEQLERAGGIQSLARLGEDSFAIASWKHHADMLHRDATLRLMIDASAKIANLAANAPEDTKEVVETAEKMLLDVTNRDIKTSYVRLEDAMVTLYDELGRLAQQDGETVGIQTGFPAMDRMFLGLRAGQMIVVGARPGVGKTSFALNLAVQMAQSGATVCFFSLEMSVEEVAQRLLSTYSMVPLQTIRSGKIAPESWDQILSATQDLSNLDILIDDTPGTTVTEIRAKARRMLRNKEKGVVILDYLQLVSPPPSKRADSRATEVSEMSRGIKIMAKDLGIPVIALSQLSRKNEERTGQRGKRPQLSDLRESGSIEQDADIVILLDRSMTEEEGSREDRPDYGITEFVVAKNRSGPLGIIDMAFFAEKTKFMEVDMHHDDV","length":466,"molWeight":51363,"crc64":"430C7A8EB535F322","md5":"E028A51B5008FE1BAA33763E4FBAFA73"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Region":1,"Binding site":1},"uniParcId":"UPI000F711833"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVF7","uniProtkbId":"A0A3G9JVF7_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2019-02-13","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49453.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Deoxyribose-phosphate aldolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"DERA"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"4.1.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"2-deoxy-D-ribose 5-phosphate aldolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Phosphodeoxyriboaldolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Deoxyriboaldolase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49453.1"}],"value":"deoC_1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"deoC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49453.1"}],"value":"Pcatena_00400"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056337"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12821"},{"database":"ChEBI","id":"CHEBI:15343"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:62877"}],"ecNumber":"4.1.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048791"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010936"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]},{"type":"Active site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Schiff-base intermediate with acetaldehyde","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]},{"type":"Active site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49453.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420567.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVF7","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848182","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_00400","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6579831at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00002","properties":[{"key":"RectionId","value":"UER00468"}]},{"database":"Proteomes","id":"UP000273154","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:0004139","properties":[{"key":"GoTerm","value":"F:deoxyribose-phosphate aldolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006018","properties":[{"key":"GoTerm","value":"P:2-deoxyribose 1-phosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016052","properties":[{"key":"GoTerm","value":"P:carbohydrate catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009264","properties":[{"key":"GoTerm","value":"P:deoxyribonucleotide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00959","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000044","properties":[{"key":"EntryName","value":"Deoxyribose-phosphate aldolase"},{"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_00114","properties":[{"key":"EntryName","value":"DeoC_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR011343","properties":[{"key":"EntryName","value":"DeoC"}]},{"database":"InterPro","id":"IPR002915","properties":[{"key":"EntryName","value":"DeoC/FbaB/LacD_aldolase"}]},{"database":"InterPro","id":"IPR028581","properties":[{"key":"EntryName","value":"DeoC_typeI"}]},{"database":"NCBIfam","id":"TIGR00126","properties":[{"key":"EntryName","value":"deoC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10889","properties":[{"key":"EntryName","value":"DEOXYRIBOSE-PHOSPHATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10889:SF1","properties":[{"key":"EntryName","value":"DEOXYRIBOSE-PHOSPHATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01791","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001357","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01133","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSRWTLDDLARLVDHTNLHADATEADMAKLCDEAKAYHFKMVAINQVQSKFCSEYLAGTDIHTGAAIAFPLGQTSIAAKVNETKDAIANGANEIDYVVNLTQVKAGNWDYIKNEMTQIVEVCREASKGRDEEIPSKVIFENCLLTDDEKVKLAEIAREVEPTFIKTSTGFSTGGATVEDVKLMKAHCGDKVQVKAAGGIRDADTFLDMVRAGATRIGCSAGMPIIDELKRRFEEQGIDSIEL","length":242,"molWeight":26492,"crc64":"24507ECD5A875D4A","md5":"705C3B82153D1941250B8E9F55F4235A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI000F6C883F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVG7","uniProtkbId":"A0A3G9JVG7_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2019-02-13","entryVersion":26,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49461.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Deoxyribose-phosphate aldolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"DERA"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"4.1.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"2-deoxy-D-ribose 5-phosphate aldolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Phosphodeoxyriboaldolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Deoxyriboaldolase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49461.1"}],"value":"deoC_2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"deoC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49461.1"}],"value":"Pcatena_00480"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056337"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Catalyzes a reversible aldol reaction between acetaldehyde and D-glyceraldehyde 3-phosphate to generate 2-deoxy-D-ribose 5-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-deoxy-D-ribose 5-phosphate = D-glyceraldehyde 3-phosphate + acetaldehyde","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12821"},{"database":"ChEBI","id":"CHEBI:15343"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:62877"}],"ecNumber":"4.1.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048791"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Carbohydrate degradation; 2-deoxy-D-ribose 1-phosphate degradation; D-glyceraldehyde 3-phosphate and acetaldehyde from 2-deoxy-alpha-D-ribose 1-phosphate: step 2/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010936"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"value":"Belongs to the DeoC/FbaB aldolase family. DeoC type 1 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":95,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]},{"type":"Active site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Schiff-base intermediate with acetaldehyde","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]},{"type":"Active site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00114"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49461.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420580.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVG7","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848190","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_00480","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"6579831at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00002","properties":[{"key":"RectionId","value":"UER00468"}]},{"database":"Proteomes","id":"UP000273154","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:0004139","properties":[{"key":"GoTerm","value":"F:deoxyribose-phosphate aldolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006018","properties":[{"key":"GoTerm","value":"P:2-deoxyribose 1-phosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016052","properties":[{"key":"GoTerm","value":"P:carbohydrate catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009264","properties":[{"key":"GoTerm","value":"P:deoxyribonucleotide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00959","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000044","properties":[{"key":"EntryName","value":"Deoxyribose-phosphate aldolase"},{"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_00114","properties":[{"key":"EntryName","value":"DeoC_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR011343","properties":[{"key":"EntryName","value":"DeoC"}]},{"database":"InterPro","id":"IPR002915","properties":[{"key":"EntryName","value":"DeoC/FbaB/LacD_aldolase"}]},{"database":"InterPro","id":"IPR028581","properties":[{"key":"EntryName","value":"DeoC_typeI"}]},{"database":"NCBIfam","id":"TIGR00126","properties":[{"key":"EntryName","value":"deoC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10889","properties":[{"key":"EntryName","value":"DEOXYRIBOSE-PHOSPHATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10889:SF1","properties":[{"key":"EntryName","value":"DEOXYRIBOSE-PHOSPHATE ALDOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01791","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001357","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01133","properties":[{"key":"EntryName","value":"DeoC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MARWTLDELSRLIDHTNIHADATEEDLAKLCDEAKEYHFKMVAINQVPVKFCSERLAGTDIDTGAAISFPLGQTSIASKVFETKDALANGANEIDYVVNLTQVKAGNWDYVEDEMTQIVAACQEAREATGLPIPCKVILETCLLTDEEKVKICEIATRVKPTFVKTSTGCSTGGATVEDVKLMKATVGDAVQVKASGGIRDADTFLDMVRAGATRIGCSAGIPIINEIRRRFEEQGVDSIEL","length":242,"molWeight":26274,"crc64":"CA58B30D833B1DD8","md5":"C4B29D1055E255BEA1476F1FCDEFFB25"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI000F6BB067"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVH5","uniProtkbId":"A0A3G9JVH5_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":28,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49418.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"DNA gyrase subunit B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"5.6.2.2"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49418.1"}],"value":"gyrB_1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"gyrB"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49418.1"}],"value":"Pcatena_00050"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"A type II topoisomerase that negatively supercoils closed circular double-stranded (ds) DNA in an ATP-dependent manner to modulate DNA topology and maintain chromosomes in an underwound state. Negative supercoiling favors strand separation, and DNA replication, transcription, recombination and repair, all of which involve strand separation. Also able to catalyze the interconversion of other topological isomers of dsDNA rings, including catenanes and knotted rings. Type II topoisomerases break and join 2 DNA strands simultaneously in an ATP-dependent manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP-dependent breakage, passage and rejoining of double-stranded DNA.","ecNumber":"5.6.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000185"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Binds two Mg(2+) per subunit. The magnesium ions form salt bridges with both the protein and the DNA. Can also accept other divalent metal cations, such as Mn(2+) or Ca(2+)."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Heterotetramer, composed of two GyrA and two GyrB chains. In the heterotetramer, GyrA contains the active site tyrosine that forms a transient covalent intermediate with DNA, while GyrB binds cofactors and catalyzes ATP hydrolysis"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Few gyrases are as efficient as E.coli at forming negative supercoils. Not all organisms have 2 type II topoisomerases; in organisms with a single type II topoisomerase this enzyme also has to decatenate newly replicated chromosomes"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010708"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"value":"Belongs to the type II topoisomerase GyrB family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":432,"modifier":"EXACT"},"end":{"value":552,"modifier":"EXACT"}},"description":"Toprim","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50880"}]},{"type":"Binding site","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":517,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":517,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Site","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]},{"type":"Site","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023029"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01898"}],"id":"KW-0799","category":"Molecular function","name":"Topoisomerase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49418.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420502.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVH5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848143","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_00050","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802808at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005694","properties":[{"key":"GoTerm","value":"C:chromosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0034335","properties":[{"key":"GoTerm","value":"F:DNA negative supercoiling activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006265","properties":[{"key":"GoTerm","value":"P:DNA topological change"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006261","properties":[{"key":"GoTerm","value":"P:DNA-templated DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd16928","properties":[{"key":"EntryName","value":"HATPase_GyrB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00822","properties":[{"key":"EntryName","value":"TopoII_Trans_DNA_gyrase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000005","properties":[{"key":"EntryName","value":"DNA gyrase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.565.10:FF:000002","properties":[{"key":"EntryName","value":"DNA gyrase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.670","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.565.10","properties":[{"key":"EntryName","value":"Histidine kinase-like ATPase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01898","properties":[{"key":"EntryName","value":"GyrB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002288","properties":[{"key":"EntryName","value":"DNA_gyrase_B_C"}]},{"database":"InterPro","id":"IPR011557","properties":[{"key":"EntryName","value":"GyrB"}]},{"database":"InterPro","id":"IPR036890","properties":[{"key":"EntryName","value":"HATPase_C_sf"}]},{"database":"InterPro","id":"IPR003594","properties":[{"key":"EntryName","value":"HATPase_dom"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"InterPro","id":"IPR001241","properties":[{"key":"EntryName","value":"Topo_IIA"}]},{"database":"InterPro","id":"IPR013760","properties":[{"key":"EntryName","value":"Topo_IIA-like_dom_sf"}]},{"database":"InterPro","id":"IPR000565","properties":[{"key":"EntryName","value":"Topo_IIA_B"}]},{"database":"InterPro","id":"IPR013759","properties":[{"key":"EntryName","value":"Topo_IIA_B_C"}]},{"database":"InterPro","id":"IPR013506","properties":[{"key":"EntryName","value":"Topo_IIA_bsu_dom2"}]},{"database":"InterPro","id":"IPR018522","properties":[{"key":"EntryName","value":"TopoIIA_CS"}]},{"database":"InterPro","id":"IPR006171","properties":[{"key":"EntryName","value":"TOPRIM_dom"}]},{"database":"NCBIfam","id":"TIGR01059","properties":[{"key":"EntryName","value":"gyrB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004189","properties":[{"key":"EntryName","value":"PRK05644.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011501","properties":[{"key":"EntryName","value":"PRK14939.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866:SF1","properties":[{"key":"EntryName","value":"DNA GYRASE SUBUNIT B, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866","properties":[{"key":"EntryName","value":"DNA GYRASE/TOPOISOMERASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00204","properties":[{"key":"EntryName","value":"DNA_gyraseB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00986","properties":[{"key":"EntryName","value":"DNA_gyraseB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02518","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01751","properties":[{"key":"EntryName","value":"Toprim"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01159","properties":[{"key":"EntryName","value":"DNAGYRASEB"}]},{"database":"PRINTS","id":"PR00418","properties":[{"key":"EntryName","value":"TPI2FAMILY"}]},{"database":"SMART","id":"SM00387","properties":[{"key":"EntryName","value":"HATPase_c"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00433","properties":[{"key":"EntryName","value":"TOP2c"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55874","properties":[{"key":"EntryName","value":"ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56719","properties":[{"key":"EntryName","value":"Type II DNA topoisomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00177","properties":[{"key":"EntryName","value":"TOPOISOMERASE_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50880","properties":[{"key":"EntryName","value":"TOPRIM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAETPKNSEYDGGEIKILEGLEAVRKRPGMYIGSTSASGLHHLVWEIVDNSVDEAMAGFCTEISVTVHADNSITVVDNGRGIPVDLHPVKKIPTLEVVMTILHAGGKFDNSAYKVSGGLHGVGISVVNALSKKVVVQVKRDGNVYEMQFARGKTTEKMKVVGQSEQTGTTVTFWPDDEIFETCVYDFDTLHNRLQETAFLNKNLKISLTDEREATPRVEEFCYAGGIIDFVRFLNDGKDVPEGLKDPIYIEGKTGPETPLDKMGEVEVALQWNSGYGENVMSFANDIYTPEGGMHLEGFRTALTRVVNDYARKQGLLKEKEANLTGDDVREGLSAVISVKLPDPQFEGQTKAKLGSSYMRTLTNKVVSDGLAEYLEEHPKQARTIVSKAQQACKARTAARKAREATRRKSLLESASLPGKLADCSVRDAELTELFIVEGDSAGGSAKDGRRRDIQAILPLRGKILNVERVGDHRAFSSDTIQSLITAIGTGVTTAAGDGGDFDITKARYHKIIIMTDADVDGAHIRILLMTFFYKYMRPLIDAGYIYVACPPIFGVKVRKKIHYVYPNGRQTEEEILRDTIRSLGFSPDDDGDTKDDSGKLKKKKRGYDVQRYKGLGEMDPKQLASTTMDPKTRILQRVTIEDAAAADRAVRELMGSEVGYRRDYIERHAHDARFLDA","length":678,"molWeight":74948,"crc64":"7C1ED6B5B1EFB566","md5":"3C16B95C415025BAEB8357EB9277E816"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":4,"Site":2},"uniParcId":"UPI000F6D79A2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVJ8","uniProtkbId":"A0A3G9JVJ8_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49493.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"Homoserine O-acetyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"HAT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"2.3.1.31"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"Homoserine transacetylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"HTA"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49493.1"}],"value":"metA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"metAA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49493.1"}],"value":"Pcatena_00800"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-homoserine + acetyl-CoA = O-acetyl-L-homoserine + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13701"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57476"},{"database":"ChEBI","id":"CHEBI:57716"}],"ecNumber":"2.3.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"Belongs to the MetA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000450-1"}]},{"type":"Active site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}]},{"type":"Active site","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}]},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":110,"modifier":"EXACT"}},"description":"Important for acyl-CoA specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}]},{"type":"Site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"Important for substrate specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00295"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"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_00295"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49493.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420638.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVJ8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848222","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_00800","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9772423at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00051","properties":[{"key":"RectionId","value":"UER00074"}]},{"database":"Proteomes","id":"UP000273154","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:0004414","properties":[{"key":"GoTerm","value":"F:homoserine O-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008899","properties":[{"key":"GoTerm","value":"F:homoserine O-succinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03131","properties":[{"key":"EntryName","value":"GATase1_HTS"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00295","properties":[{"key":"EntryName","value":"MetA_acyltransf"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR033752","properties":[{"key":"EntryName","value":"MetA_family"}]},{"database":"PANTHER","id":"PTHR20919","properties":[{"key":"EntryName","value":"HOMOSERINE O-SUCCINYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20919:SF0","properties":[{"key":"EntryName","value":"HOMOSERINE O-SUCCINYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04204","properties":[{"key":"EntryName","value":"HTS"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000450","properties":[{"key":"EntryName","value":"H_ser_succinyltr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPINIPDGLPAKRILQQERIFALEEDVARKQQIRPLHVALLNLMPTKIETETQILRLISKSPIQVSVDFMRVSSHEATHAADHLVKFYDTFDDLKHNNYDGLIITGAPVEQMPFEEVDYWDELCQIMDWAQEHVLSTMFLCWGAFAGLYHLHGIHKRLLGSKLFGVFPQRLCDEYNFLTNGFDEVHNMPHSRHAAPDEKEIDADPALQVLSRGETSGPALIATRDFHEIYALGHFEYGRDTLADEYWRDFHAGLPIQLPLNYFPDDDPEKQPLFTWRSHANLLYRNWLNYVYQTTPYELERVPEVVAELREHTEQLLAKGGVPSKF","length":326,"molWeight":37750,"crc64":"92CC3F5112395F23","md5":"0C0407058BDEAF432DC61531EC57AC41"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":3,"Binding site":3,"Site":2},"uniParcId":"UPI000F706CF8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVL2","uniProtkbId":"A0A3G9JVL2_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49501.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"4-hydroxy-tetrahydrodipicolinate reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"HTPA reductase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"1.17.1.8"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49501.1"}],"value":"dapB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49501.1"}],"value":"Pcatena_00880"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Catalyzes the conversion of 4-hydroxy-tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate + NAD(+) + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:35323"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16845"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:67139"}],"ecNumber":"1.17.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate + NADP(+) + H2O = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:35331"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16845"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:67139"}],"ecNumber":"1.17.1.8","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006642"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Belongs to the DapB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"value":"Was originally thought to be a dihydrodipicolinate reductase (DHDPR), catalyzing the conversion of dihydrodipicolinate to tetrahydrodipicolinate. However, it was shown in E.coli that the substrate of the enzymatic reaction is not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by the DapA-catalyzed reaction"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Dihydrodipicolinate reductase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01113"}]},{"type":"Domain","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"Dihydrodipicolinate reductase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF05173"}]},{"type":"Active site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]},{"type":"Active site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}]},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":89,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16845"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate","id":"ChEBI:CHEBI:16845"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16845"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"ligand":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate","id":"ChEBI:CHEBI:16845"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"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_00102"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022915"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0220","category":"Biological process","name":"Diaminopimelate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00102"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49501.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_232619855.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVL2","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848229","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_00880","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00034","properties":[{"key":"RectionId","value":"UER00018"}]},{"database":"Proteomes","id":"UP000273154","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:0008839","properties":[{"key":"GoTerm","value":"F:4-hydroxy-tetrahydrodipicolinate reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009085","properties":[{"key":"GoTerm","value":"P:L-lysine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00102","properties":[{"key":"EntryName","value":"DapB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022663","properties":[{"key":"EntryName","value":"DapB_C"}]},{"database":"InterPro","id":"IPR000846","properties":[{"key":"EntryName","value":"DapB_N"}]},{"database":"InterPro","id":"IPR022664","properties":[{"key":"EntryName","value":"DapB_N_CS"}]},{"database":"InterPro","id":"IPR023940","properties":[{"key":"EntryName","value":"DHDPR_bac"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00036","properties":[{"key":"EntryName","value":"dapB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20836:SF7","properties":[{"key":"EntryName","value":"4-HYDROXY-TETRAHYDRODIPICOLINATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20836","properties":[{"key":"EntryName","value":"DIHYDRODIPICOLINATE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05173","properties":[{"key":"EntryName","value":"DapB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01113","properties":[{"key":"EntryName","value":"DapB_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000161","properties":[{"key":"EntryName","value":"DHPR"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01298","properties":[{"key":"EntryName","value":"DAPB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSENAAPIRVAIMGEGRMGSLIRSTAEAARTEEGSAAFEVVAQIGFDLSAADAAPAADVLIDFSNVVTLPAVASYVRRTGAALVSGTTGYTDEQMAELRSLAKTSAVLQSGNYSLGIAALRHAATLAARELAGFDVEIVETHHNQKVDAPSGTAKLLLDAVVATEAEEGRGEYHPVYGREGMVGKRDPREVGMHSLRGGTVAGVHTVSFFGTDEEVSLTHRATSRQIFVNGALAAARKMAGREPGFYGFDEVMFN","length":256,"molWeight":26932,"crc64":"DA07167F95FD4FDE","md5":"E17CD7FCC3A4A5757AA8F4D045638F26"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":5},"uniParcId":"UPI000F6F7EC7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVN8","uniProtkbId":"A0A3G9JVN8_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49533.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"Glucose-6-phosphate isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"GPI"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"5.3.1.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"Phosphoglucose isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"PGI"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"Phosphohexose isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"PHI"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49533.1"}],"value":"pgi_1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"pgi"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49533.1"}],"value":"Pcatena_01200"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"Catalyzes the reversible isomerization of glucose-6-phosphate to fructose-6-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029321"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004926"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006604"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Belongs to the GPI family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":529,"modifier":"EXACT"},"end":{"value":529,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00473"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49533.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420701.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVN8","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848262","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_01200","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"140919at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00181"}]},{"database":"UniPathway","id":"UPA00138","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004347","properties":[{"key":"GoTerm","value":"F:glucose-6-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051156","properties":[{"key":"GoTerm","value":"P:glucose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05015","properties":[{"key":"EntryName","value":"SIS_PGI_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd05016","properties":[{"key":"EntryName","value":"SIS_PGI_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1390.10:FF:000001","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000003","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10490:FF:000018","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1390.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10490","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase like protein, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00473","properties":[{"key":"EntryName","value":"G6P_isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001672","properties":[{"key":"EntryName","value":"G6P_Isomerase"}]},{"database":"InterPro","id":"IPR023096","properties":[{"key":"EntryName","value":"G6P_Isomerase_C"}]},{"database":"InterPro","id":"IPR018189","properties":[{"key":"EntryName","value":"Phosphoglucose_isomerase_CS"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"InterPro","id":"IPR035476","properties":[{"key":"EntryName","value":"SIS_PGI_1"}]},{"database":"InterPro","id":"IPR035482","properties":[{"key":"EntryName","value":"SIS_PGI_2"}]},{"database":"NCBIfam","id":"NF001211","properties":[{"key":"EntryName","value":"pgi"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11469","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11469:SF1","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00342","properties":[{"key":"EntryName","value":"PGI"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00662","properties":[{"key":"EntryName","value":"G6PISOMERASE"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00765","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00174","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51463","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNIPAPVDATKTPEWEALKAHHDKLVADHFNLKDAFAADDKRVEKLSFDMSDLHFDLSKDLVTDETVKLLCDLARAVKVEERRDAMFSGEHINTTEDRAVLHTALRRPKDQIGKFVVDGQDTVADVHEVLDRMYAFAERVRSGEWKGVSGKRIEHVMSIGIGGSDLGPVMAYEALKPYADAGIDCRFVSNIDPNDMAEKTRGLDPETTLVIIVSKTFTTLETITNAREARTWMLDALKAQGAIDGSDAQNADAIKKHFVAVSTNLELVEQFGIDPENAFGFWSWVGGRYSVDSAVGLSLIIAFGPERFAEFLAGFHDVDNYFKNTPLERNVVALMGLMNVWYVNFCGMGSHAVLPYNQYLHRFPAYLQQLTMESNGKSTRWDGTPATSATGEVFWGEAGTNGQHAFYQLIHQGTKPIPADFIAFVNTPNPTKDGDQDVHELFLGNFLAQTKALAFGKTADEVRAEGTAEWMVPARCFEGNRPTTSIFGEALTPHALGELIALYEHITFVEGTVWGLDSYDQWGVELGKQLAKQITPAFHDDEALARQDASTQALIAYYRAHRK","length":564,"molWeight":62588,"crc64":"279CB19B2E20528E","md5":"612A03E5D16ECFFE30C8FFCD916A45B2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI000F70E55D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVS6","uniProtkbId":"A0A3G9JVS6_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49563.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"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:0000313","source":"EMBL","id":"BBH49563.1"}],"value":"glgC_1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00624"}],"value":"glgC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49563.1"}],"value":"Pcatena_01500"}]}],"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":8,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Domain","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":368,"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":100,"modifier":"EXACT"},"end":{"value":100,"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":165,"modifier":"EXACT"},"end":{"value":165,"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":180,"modifier":"EXACT"},"end":{"value":181,"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":191,"modifier":"EXACT"},"end":{"value":191,"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":60,"modifier":"EXACT"},"end":{"value":60,"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":99,"modifier":"EXACT"},"end":{"value":99,"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":"UP000273154"}],"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-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49563.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420754.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVS6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848293","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_01500","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801810at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00164","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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":"NF003670","properties":[{"key":"EntryName","value":"PRK05293.1"},{"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":"PS00808","properties":[{"key":"EntryName","value":"ADP_GLC_PYROPHOSPH_1"},{"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":"MSKKESIAMLLAGGQGSRLLALTRNIAKPAVSFGGKYRIIDFALSNCANSGIDTVGVLTQYRPYLLHSYIGTGEAWNLDSRDGGVSILPPYATEAGGNWYAGTADAIYQNIGYIESYDPKYVVILSGDHLYRMDYSKMVESHIANNADLTISVMPVAWAEASRFGIITKNDDDSVAKFTEKPNKPDSNLASMGIYVFSTDILIRALKEDALDATSEHDFGKNIIPKLLEEQARIFCYEFHGFWRDVGTISSYHETSMDLLGPNPEFDLFGKEFPFMTNAPVRPPHYVGPDAVVEDAIIANGCKVNGTVRHSILSTDAVVESRAVVEDSVLFPGAVVKEGAHVARAILGEHAVVEAGVELGSVDVTKDTAVIGDDVVVGKGEE","length":382,"molWeight":41377,"crc64":"1C91D8DECE403373","md5":"820D116555B6F23009994017E1471138"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Binding site":4,"Site":2},"uniParcId":"UPI000F6EB8E1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JVS7","uniProtkbId":"A0A3G9JVS7_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49561.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"1,4-alpha-glucan branching enzyme GlgB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"2.4.1.18"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"1,4-alpha-D-glucan:1,4-alpha-D-glucan 6-glucosyl-transferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"Alpha-(1->4)-glucan branching enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"Glycogen branching enzyme"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"BE"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49561.1"}],"value":"glgB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49561.1"}],"value":"Pcatena_01480"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"Catalyzes the formation of the alpha-1,6-glucosidic linkages in glycogen by scission of a 1,4-alpha-linked oligosaccharide from growing alpha-1,4-glucan chains and the subsequent attachment of the oligosaccharide to the alpha-1,6 position"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Transfers a segment of a (1->4)-alpha-D-glucan chain to a primary hydroxy group in a similar glucan chain.","ecNumber":"2.4.1.18","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000826"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004964"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"Glycan biosynthesis; glycogen biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009000"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"value":"Belongs to the glycosyl hydrolase 13 family. GlgB subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Glycosyl hydrolase family 13 catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00642"}]},{"type":"Region","location":{"start":{"value":623,"modifier":"EXACT"},"end":{"value":642,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":669,"modifier":"EXACT"},"end":{"value":725,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":686,"modifier":"EXACT"},"end":{"value":697,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":712,"modifier":"EXACT"},"end":{"value":725,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":338,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000463-1"}]},{"type":"Active site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000463-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"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_00685"}],"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_00685"}],"id":"KW-0321","category":"Biological process","name":"Glycogen metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00685"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"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_00685"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49561.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420753.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JVS7","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848291","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_01480","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9800174at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00164","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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:0003844","properties":[{"key":"GoTerm","value":"F:1,4-alpha-glucan branching enzyme activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043169","properties":[{"key":"GoTerm","value":"F:cation binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004553","properties":[{"key":"GoTerm","value":"F:hydrolase activity, hydrolyzing O-glycosyl compounds"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005978","properties":[{"key":"GoTerm","value":"P:glycogen biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd11322","properties":[{"key":"EntryName","value":"AmyAc_Glg_BE"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02855","properties":[{"key":"EntryName","value":"E_set_GBE_prok_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.1180:FF:000002","properties":[{"key":"EntryName","value":"1,4-alpha-glucan branching enzyme GlgB"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.1180","properties":[{"key":"EntryName","value":"Golgi alpha-mannosidase II"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00685","properties":[{"key":"EntryName","value":"GlgB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006048","properties":[{"key":"EntryName","value":"A-amylase/branching_C"}]},{"database":"InterPro","id":"IPR037439","properties":[{"key":"EntryName","value":"Branching_enzy"}]},{"database":"InterPro","id":"IPR006047","properties":[{"key":"EntryName","value":"GH13_cat_dom"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR006407","properties":[{"key":"EntryName","value":"GlgB"}]},{"database":"InterPro","id":"IPR044143","properties":[{"key":"EntryName","value":"GlgB_N_E_set_prok"}]},{"database":"InterPro","id":"IPR004193","properties":[{"key":"EntryName","value":"Glyco_hydro_13_N"}]},{"database":"InterPro","id":"IPR013780","properties":[{"key":"EntryName","value":"Glyco_hydro_b"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"InterPro","id":"IPR014756","properties":[{"key":"EntryName","value":"Ig_E-set"}]},{"database":"NCBIfam","id":"TIGR01515","properties":[{"key":"EntryName","value":"branching_enzym"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003811","properties":[{"key":"EntryName","value":"glgB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008967","properties":[{"key":"EntryName","value":"glgB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43651","properties":[{"key":"EntryName","value":"1,4-ALPHA-GLUCAN-BRANCHING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43651:SF3","properties":[{"key":"EntryName","value":"1,4-ALPHA-GLUCAN-BRANCHING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00128","properties":[{"key":"EntryName","value":"Alpha-amylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02806","properties":[{"key":"EntryName","value":"Alpha-amylase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02922","properties":[{"key":"EntryName","value":"CBM_48"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000463","properties":[{"key":"EntryName","value":"GlgB"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00642","properties":[{"key":"EntryName","value":"Aamy"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81296","properties":[{"key":"EntryName","value":"E set domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51011","properties":[{"key":"EntryName","value":"Glycosyl hydrolase domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGNTRPAGATSAGALDITNDDLYLMGAGTWYRSYEKMGAHPCERDGRAGYRFAVWAPDVRSVHVVGDFNGWDAQADPLEPLLTSGVWCGFVAGVRPGELYKYVIETDSGELLYKADPYAFTSELAPGTASVTAAEPAYAWHDDAWLAARAETDHMHAPLNIYEVHLGSWRRHGDEPQGKPREDGTWPGPMDEFPAQRGRYYSYDDLAAELVPYAKRMGYTHIEMLPVMEHPFDGSWGYQVTGYFAPTSRFGEPEGLMRLIDACHEAGLGVILDWVPGGFCADAQGLAMFNGHMLYEREIHPNWGTHKFDFARGEVRSFLVSNALYWLDRFHADGIRMDGVSSMLYLNFGIDNPAEKRLNEKGTEEDLDASAFIRQVNTAVAEYCPGVVMMAEESTAWPLVTYPPEDGGLGFHYKWDMGWMNDTLHYLQTDFPWRPGNHGMLTFSMMYAFNENFILPLSHDEVVHGKCSLITRQPGDQWRQFAGLRTLAFYQMTHPGGKLNFMGNEIGQYIEWRYYESIQWFLAERFEPHAKHQHYIEALNNLYLAEPALWRESYDWSGFEWLSADDSEHSIVSFVRRGDGPDEELVIVINFDVNFRPSWRVPVPREGDYVEIFNSDAEEFGGSGQRNAGVLSSRPEDCDGRENSLIMNVPPLGGAILRRTGPTSYVAPAPAEKAALPRPTAQPSSRKPRATRAKKVTAKPLVAGEGGPLPKKGSKKKRKRAKGRA","length":725,"molWeight":81431,"crc64":"BAEC614322056E2E","md5":"2D37C58054993EF1A31B2F9F85D1FEE0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":2,"Active site":2},"uniParcId":"UPI000F715392"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JW02","uniProtkbId":"A0A3G9JW02_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49641.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015972"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"DNA-directed RNA polymerase subunit alpha"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"RNAP subunit alpha"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012418"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"RNA polymerase subunit alpha"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032524"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Transcriptase subunit alpha"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49641.1"}],"value":"rpoA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49641.1"}],"value":"Pcatena_02280"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007123"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Belongs to the RNA polymerase alpha chain family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"DNA-directed RNA polymerase RpoA/D/Rpb3-type","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00662"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"Alpha N-terminal domain (alpha-NTD)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}]},{"type":"Region","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"Alpha C-terminal domain (alpha-CTD)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022478"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49641.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420890.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JW02","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848377","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_02280","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9805706at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046983","properties":[{"key":"GoTerm","value":"F:protein dimerization activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06928","properties":[{"key":"EntryName","value":"RNAP_alpha_NTD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.170.120.12:FF:000001","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.20","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.120.12","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase, insert domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1360.10","properties":[{"key":"EntryName","value":"RNA polymerase, RBP11-like subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00059","properties":[{"key":"EntryName","value":"RNApol_bact_RpoA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011262","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_insert"}]},{"database":"InterPro","id":"IPR011263","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_RpoA/D/Rpb3"}]},{"database":"InterPro","id":"IPR011773","properties":[{"key":"EntryName","value":"DNA-dir_RpoA"}]},{"database":"InterPro","id":"IPR036603","properties":[{"key":"EntryName","value":"RBP11-like"}]},{"database":"InterPro","id":"IPR011260","properties":[{"key":"EntryName","value":"RNAP_asu_C"}]},{"database":"InterPro","id":"IPR036643","properties":[{"key":"EntryName","value":"RNApol_insert_sf"}]},{"database":"NCBIfam","id":"NF003513","properties":[{"key":"EntryName","value":"PRK05182.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003519","properties":[{"key":"EntryName","value":"PRK05182.2-5"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02027","properties":[{"key":"EntryName","value":"rpoA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01000","properties":[{"key":"EntryName","value":"RNA_pol_A_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03118","properties":[{"key":"EntryName","value":"RNA_pol_A_CTD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01193","properties":[{"key":"EntryName","value":"RNA_pol_L"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00662","properties":[{"key":"EntryName","value":"RPOLD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47789","properties":[{"key":"EntryName","value":"C-terminal domain of RNA polymerase alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56553","properties":[{"key":"EntryName","value":"Insert subdomain of RNA polymerase alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55257","properties":[{"key":"EntryName","value":"RBP11-like subunits of RNA polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDFIRPNVTVEEVSENVARVIAEPLEHGYGDTLGNSLRRVLLSSLEGAAVEAIQIDGVQHEFTTVEGVYEDVTDIVLNVKGLAFKSLGVGDEATATISIDGPATVTGGDFDIPSEFNLVNPEHVICTLAEGAHLTMSMRIGIGRGYVSGEDNEHDDDPIGLIHVDSLFSPVRRCAKAVEPCRVGQHTDYDKLVLEVETNGGVSPREAVVEAANIINQHMTAFMSLADEGEQAEEPSIFAAGQTDDNTELDKQIEDLDLSVRSYNCLKRAGIHSVRQLVEFSENDLLNIRNFGVKSIEEVKDKLESMGLSFKA","length":313,"molWeight":33986,"crc64":"34ACA0CFB5092208","md5":"76DF012F08890754EEB2387B290C3D3B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Region":2},"uniParcId":"UPI000F6E6CB9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JW19","uniProtkbId":"A0A3G9JW19_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49647.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Arginine biosynthesis bifunctional protein ArgJ"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Glutamate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"2.3.1.35"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Ornithine acetyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"OATase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Ornithine transacetylase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Amino-acid acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"2.3.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"N-acetylglutamate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"AGSase"}]}]}],"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Arginine biosynthesis bifunctional protein ArgJ alpha chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Arginine biosynthesis bifunctional protein ArgJ beta chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49647.1"}],"value":"argJ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49647.1"}],"value":"Pcatena_02340"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054976"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Catalyzes two activities which are involved in the cyclic version of arginine biosynthesis: the synthesis of N-acetylglutamate from glutamate and acetyl-CoA as the acetyl donor, and of ornithine by transacetylation between N(2)-acetylornithine and glutamate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamate + acetyl-CoA = N-acetyl-L-glutamate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24292"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"}],"ecNumber":"2.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-acetyl-L-ornithine + L-glutamate = N-acetyl-L-glutamate + L-ornithine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15349"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:46911"},{"database":"ChEBI","id":"CHEBI:57805"}],"ecNumber":"2.3.1.35","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049439"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; L-ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)-acetyl-L-ornithine (cyclic): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Heterotetramer of two alpha and two beta chains"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006774"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"value":"Belongs to the ArgJ family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"Arginine biosynthesis bifunctional protein ArgJ alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"featureId":"PRO_5023397427"},{"type":"Chain","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"Arginine biosynthesis bifunctional protein ArgJ beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"featureId":"PRO_5023397428"},{"type":"Active site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]},{"type":"Binding site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":423,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]},{"type":"Site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Involved in the stabilization of negative charge on the oxyanion by the formation of the oxyanion hole","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]},{"type":"Site","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"Cleavage; by autolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"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_01106"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022813"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0068","category":"PTM","name":"Autocatalytic cleavage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01106"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"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_01106"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49647.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420902.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JW19","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848383","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_02340","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804242at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00106"}]},{"database":"Proteomes","id":"UP000273154","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:0004042","properties":[{"key":"GoTerm","value":"F:L-glutamate N-acetyltransferase activity, acting on acetyl-CoA as donor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004358","properties":[{"key":"GoTerm","value":"F:L-glutamate N-acetyltransferase activity, acting on acetyl-L-ornithine as donor"},{"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:0006592","properties":[{"key":"GoTerm","value":"P:L-ornithine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd02152","properties":[{"key":"EntryName","value":"OAT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.20.340:FF:000001","properties":[{"key":"EntryName","value":"Arginine biosynthesis bifunctional protein ArgJ, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.70.12:FF:000001","properties":[{"key":"EntryName","value":"Arginine biosynthesis bifunctional protein ArgJ, chloroplastic"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.340","properties":[{"key":"EntryName","value":"ArgJ beta chain, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.70.12","properties":[{"key":"EntryName","value":"L-amino peptidase D-ALA esterase/amidase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01106","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002813","properties":[{"key":"EntryName","value":"Arg_biosynth_ArgJ"}]},{"database":"InterPro","id":"IPR016117","properties":[{"key":"EntryName","value":"ArgJ-like_dom_sf"}]},{"database":"InterPro","id":"IPR042195","properties":[{"key":"EntryName","value":"ArgJ_beta_C"}]},{"database":"NCBIfam","id":"NF003802","properties":[{"key":"EntryName","value":"argJ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00120","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23100","properties":[{"key":"EntryName","value":"ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23100:SF0","properties":[{"key":"EntryName","value":"ARGININE BIOSYNTHESIS BIFUNCTIONAL PROTEIN ARGJ, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01960","properties":[{"key":"EntryName","value":"ArgJ"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56266","properties":[{"key":"EntryName","value":"DmpA/ArgJ-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEQTIAPKLSVIADGGVASPAGIHAGGIHAGFRRDPQRFDLALVEVDECAVAAGAFTTNKFCAAPVTVSRAHLGKGGSAPVRAVCINSGNANAATGEEGLECAETTCALVAKTIGCEPEQVLVASTGVIGQLLDVAPFETGVPALHDKICAQATDESLRLSGGHDAARAIMTTDTHPKEYAVSYEAGGSLAGSTVTVGGMCKGSGMIMPNMATMIAIISTNAPVSAAALHEVLLGVVKKTFNKVTVDSDTSTNDTCIAIATGKAAADAAPIEPGTPEAAELACAVNAVCQHLAREIAADGEGASKLVTVTVAGAATDEDADTAARAIANSPLVKTAIYGHDCNWGRIAMALGKCGVAFDQRDVDIDIMGMPVCRDGLTVAFDEDEALRRFEEPEITIWADLGAGACETTVWTCDLTHEYVKINGEYRT","length":428,"molWeight":43948,"crc64":"4D901458696AE94F","md5":"1A17D18031766FFA45452CE007591B3F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":2,"Active site":1,"Binding site":6,"Site":3},"uniParcId":"UPI000F70D825"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JW40","uniProtkbId":"A0A3G9JW40_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49648.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Acetylglutamate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"2.7.2.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"N-acetyl-L-glutamate 5-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"NAG kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"NAGK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49648.1"}],"value":"argB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49648.1"}],"value":"Pcatena_02350"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Catalyzes the ATP-dependent phosphorylation of N-acetyl-L-glutamate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-L-glutamate + ATP = N-acetyl-L-glutamyl 5-phosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14629"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:44337"},{"database":"ChEBI","id":"CHEBI:57936"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004828"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; N(2)-acetyl-L-ornithine from L-glutamate: step 2/4"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"value":"Belongs to the acetylglutamate kinase family. ArgB subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Aspartate/glutamate/uridylate kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00696"}]},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}]},{"type":"Site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00082"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49648.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420904.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JW40","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848384","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_02350","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9803155at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00107"}]},{"database":"Proteomes","id":"UP000273154","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:0003991","properties":[{"key":"GoTerm","value":"F:acetylglutamate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd04250","properties":[{"key":"EntryName","value":"AAK_NAGK-C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1160.10:FF:000004","properties":[{"key":"EntryName","value":"Acetylglutamate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1160.10","properties":[{"key":"EntryName","value":"Acetylglutamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00082","properties":[{"key":"EntryName","value":"ArgB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036393","properties":[{"key":"EntryName","value":"AceGlu_kinase-like_sf"}]},{"database":"InterPro","id":"IPR004662","properties":[{"key":"EntryName","value":"AcgluKinase_fam"}]},{"database":"InterPro","id":"IPR037528","properties":[{"key":"EntryName","value":"ArgB"}]},{"database":"InterPro","id":"IPR001048","properties":[{"key":"EntryName","value":"Asp/Glu/Uridylate_kinase"}]},{"database":"InterPro","id":"IPR001057","properties":[{"key":"EntryName","value":"Glu/AcGlu_kinase"}]},{"database":"InterPro","id":"IPR041727","properties":[{"key":"EntryName","value":"NAGK-C"}]},{"database":"NCBIfam","id":"TIGR00761","properties":[{"key":"EntryName","value":"argB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23342","properties":[{"key":"EntryName","value":"N-ACETYLGLUTAMATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23342:SF0","properties":[{"key":"EntryName","value":"N-ACETYLGLUTAMATE SYNTHASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00696","properties":[{"key":"EntryName","value":"AA_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000728","properties":[{"key":"EntryName","value":"NAGK"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00474","properties":[{"key":"EntryName","value":"GLU5KINASE"}]},{"database":"SUPFAM","id":"SSF53633","properties":[{"key":"EntryName","value":"Carbamate kinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKYAVDTSKRAKDTDERTGQVLFEALPWIKNITGKTVVVKYGGAAMVDEKLRADVMSDIVLLKILGVNVVIVHGGGKAINRAFDALNFPVEFKDGQRVTTPAAMDVVRQVLVGEVNQDLVTAINRHGNLAVGVAGSDAGTIVCSTLNPELGRVGKIEHVDTTYLETLIKSDYIPVVATVGIGEDGGYYNINADVAAGHVAAAIGAQKIVYLTDVDGVYMDFSDKNSLISNMSLREMEDMLASGTVDKGMIPKLESCCYALHAGVFRSHVINGKTPHSLLIELLTDKGIGTTMHSTEEALKYDEHPLGTLASRLAVNN","length":317,"molWeight":33973,"crc64":"9E21669BDF788949","md5":"6F1C1CEE4B128A241893208BB63E42B6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":2},"uniParcId":"UPI000F700A6D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JW48","uniProtkbId":"A0A3G9JW48_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-02-13","entryVersion":29,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49687.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"3-isopropylmalate dehydratase large subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"4.2.1.33"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"Alpha-IPM isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"IPMI"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"Isopropylmalate isomerase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49687.1"}],"value":"leuC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49687.1"}],"value":"Pcatena_02740"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32287"},{"database":"ChEBI","id":"CHEBI:1178"},{"database":"ChEBI","id":"CHEBI:35121"}],"ecNumber":"4.2.1.33","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"Binds 1 [4Fe-4S] cluster per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"Heterodimer of LeuC and LeuD"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"value":"Belongs to the aconitase/IPM isomerase family. LeuC type 2 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":288,"modifier":"EXACT"}},"description":"Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00330"}]},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0100","category":"Biological process","name":"Branched-chain amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0432","category":"Biological process","name":"Leucine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01027"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49687.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_172596336.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JW48","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848422","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_02740","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00048","properties":[{"key":"RectionId","value":"UER00071"}]},{"database":"UniPathway","id":"UPA00946","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000273154","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0003861","properties":[{"key":"GoTerm","value":"F:3-isopropylmalate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009098","properties":[{"key":"GoTerm","value":"P:L-leucine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01583","properties":[{"key":"EntryName","value":"IPMI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.499.10","properties":[{"key":"EntryName","value":"Aconitase, domain 3"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01027","properties":[{"key":"EntryName","value":"LeuC_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015931","properties":[{"key":"EntryName","value":"Acnase/IPM_dHydase_lsu_aba_1/3"}]},{"database":"InterPro","id":"IPR001030","properties":[{"key":"EntryName","value":"Acoase/IPM_deHydtase_lsu_aba"}]},{"database":"InterPro","id":"IPR018136","properties":[{"key":"EntryName","value":"Aconitase_4Fe-4S_BS"}]},{"database":"InterPro","id":"IPR036008","properties":[{"key":"EntryName","value":"Aconitase_4Fe-4S_dom"}]},{"database":"InterPro","id":"IPR011826","properties":[{"key":"EntryName","value":"HAcnase/IPMdehydase_lsu_prok"}]},{"database":"InterPro","id":"IPR006251","properties":[{"key":"EntryName","value":"Homoacnase/IPMdehydase_lsu"}]},{"database":"InterPro","id":"IPR050067","properties":[{"key":"EntryName","value":"IPM_dehydratase_rel_enz"}]},{"database":"InterPro","id":"IPR033941","properties":[{"key":"EntryName","value":"IPMI_cat"}]},{"database":"InterPro","id":"IPR011823","properties":[{"key":"EntryName","value":"IsopropMal_deHydtase_lsu_bac"}]},{"database":"NCBIfam","id":"TIGR01343","properties":[{"key":"EntryName","value":"hacA_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02086","properties":[{"key":"EntryName","value":"IPMI_arch"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02083","properties":[{"key":"EntryName","value":"LEU2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001614","properties":[{"key":"EntryName","value":"PRK00402.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43822:SF16","properties":[{"key":"EntryName","value":"3-ISOPROPYLMALATE DEHYDRATASE LARGE SUBUNIT 2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43822","properties":[{"key":"EntryName","value":"HOMOACONITASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00330","properties":[{"key":"EntryName","value":"Aconitase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00415","properties":[{"key":"EntryName","value":"ACONITASE"}]},{"database":"SUPFAM","id":"SSF53732","properties":[{"key":"EntryName","value":"Aconitase iron-sulfur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00450","properties":[{"key":"EntryName","value":"ACONITASE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTRPMTMAEKILAAHAGLPEVVPGQLVECDLDLVLANDITAPIAIKTVNEIGAGVFDRDRICLVPDHYSPNKDIKSAEQTKVTRDFAHEHKITNYFEQGCMGIEHALLPEQGVVVPGDLMIGADSHTCTYGGIGAFSTGVGSTDAGVGMATGRAWFKVPETIRFVIDGELPAGATAKDVILHIIGMIGVDGALYCAMEFGGSTIESLSVEGRLTIANMAIEAGGKAGLFEVDDKCREWVAKRARREPREFHPDADATYKQVIHIDAADIVPCVSWPHLPSNTHPVTESRHIEIDQAVIGSCTNGRIEDMRAAADVLRGRAVAEGVRCIVIPATQKVWLQCVHEGLMDVFVNAHCVVSTPTCGPCLGGYMGILAAGERCVSSTNRNFVGRMGDPTSEVYLASPAVCAASAVAGHIALPADLD","length":421,"molWeight":44766,"crc64":"C95E7238A0941DB2","md5":"6BBC41D68603C7F8E1927137E45EB673"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":3},"uniParcId":"UPI000F6BB696"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JW54","uniProtkbId":"A0A3G9JW54_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49613.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011952"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Glucose-6-phosphate isomerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011952"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"5.3.1.9"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49613.1"}],"value":"pgi_2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"pgi"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49613.1"}],"value":"Pcatena_02000"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucose 6-phosphate = beta-D-fructose 6-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11816"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:58225"}],"ecNumber":"5.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 2/4"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000612"}],"value":"Belongs to the GPI family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]},{"type":"Active site","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49613.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420844.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JW54","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848349","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_02000","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"140919at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00181"}]},{"database":"Proteomes","id":"UP000273154","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:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004347","properties":[{"key":"GoTerm","value":"F:glucose-6-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051156","properties":[{"key":"GoTerm","value":"P:glucose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05016","properties":[{"key":"EntryName","value":"SIS_PGI_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10490","properties":[{"key":"EntryName","value":"Glucose-6-phosphate isomerase like protein, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR001672","properties":[{"key":"EntryName","value":"G6P_Isomerase"}]},{"database":"InterPro","id":"IPR018189","properties":[{"key":"EntryName","value":"Phosphoglucose_isomerase_CS"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"InterPro","id":"IPR035482","properties":[{"key":"EntryName","value":"SIS_PGI_2"}]},{"database":"PANTHER","id":"PTHR11469","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11469:SF1","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00342","properties":[{"key":"EntryName","value":"PGI"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00662","properties":[{"key":"EntryName","value":"G6PISOMERASE"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00174","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51463","properties":[{"key":"EntryName","value":"P_GLUCOSE_ISOMERASE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLRLNEASLGARVTSDDVTRASRASGELLAQVQKGEVCYRSSLGWLHVDEWASVEQLVRIAELASRLRAETDTFVLIGVGGSNNAARAVLRALGQPDSTHQVVWAGNTLSPRALNEMLASLEGHEAVIDCVAKNFETLEPGSSFRLLRQWMSAHMDASQIARHIVCCGTPKSQLEKLCTDEGYAFTTFPPNVGGRFTAFTPVHLLALAYAGIDIHALVQGARDEERRLRQTSARPEDNAALRYAQIRHLAWEEGMRVELLSSFEPCLSGVSLWWQQLFGESEGKGDRGLLPASAQYSEDLHSLGQYVQEGTPLLMETLLDVLEARESDRLVLGGTDVADGFDYLDGMDFWDINKASFHATRAAHARRLPCPTIELERLDEHTLGELLYFFMFSCYLSARLLEVNPFNQPGVEAYKQLMFRTLRGA","length":425,"molWeight":47203,"crc64":"483661497215C3DB","md5":"155D9C2010119E6C0CE96106D94F7B1E"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI000F7003F3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JW86","uniProtkbId":"A0A3G9JW86_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49643.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridine synthase A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"5.4.99.12"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridine(38-40) synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA pseudouridylate synthase I"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"tRNA-uridine isomerase I"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49643.1"}],"value":"truA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49643.1"}],"value":"Pcatena_02300"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine(38/39/40) in tRNA = pseudouridine(38/39/40) in tRNA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22376"},{"database":"Rhea","id":"RHEA-COMP:10085"},{"database":"Rhea","id":"RHEA-COMP:10087"},{"database":"ChEBI","id":"CHEBI:65314"},{"database":"ChEBI","id":"CHEBI:65315"}],"ecNumber":"5.4.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003792"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009375"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003792"}],"value":"Belongs to the tRNA pseudouridine synthase TruA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"Pseudouridine synthase I TruA alpha/beta","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01416"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001430-1"}]},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001430-2"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00171"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49643.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126420894.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JW86","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848379","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_02300","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9811823at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0160147","properties":[{"key":"GoTerm","value":"F:tRNA pseudouridine(38-40) synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0031119","properties":[{"key":"GoTerm","value":"P:tRNA pseudouridine synthesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02570","properties":[{"key":"EntryName","value":"PseudoU_synth_EcTruA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.660","properties":[{"key":"EntryName","value":"Pseudouridine synthase I, catalytic domain, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.580","properties":[{"key":"EntryName","value":"Pseudouridine synthase I, catalytic domain, N-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00171","properties":[{"key":"EntryName","value":"TruA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR020103","properties":[{"key":"EntryName","value":"PsdUridine_synth_cat_dom_sf"}]},{"database":"InterPro","id":"IPR001406","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA"}]},{"database":"InterPro","id":"IPR020097","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA_a/b_dom"}]},{"database":"InterPro","id":"IPR020095","properties":[{"key":"EntryName","value":"PsdUridine_synth_TruA_C"}]},{"database":"InterPro","id":"IPR020094","properties":[{"key":"EntryName","value":"TruA/RsuA/RluB/E/F_N"}]},{"database":"NCBIfam","id":"TIGR00071","properties":[{"key":"EntryName","value":"hisT_truA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11142","properties":[{"key":"EntryName","value":"PSEUDOURIDYLATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11142:SF0","properties":[{"key":"EntryName","value":"TRNA PSEUDOURIDINE SYNTHASE-LIKE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01416","properties":[{"key":"EntryName","value":"PseudoU_synth_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001430","properties":[{"key":"EntryName","value":"tRNA_psdUrid_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55120","properties":[{"key":"EntryName","value":"Pseudouridine synthase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQHTIEHRPPERPSIEERATDPATLDATLVLKLGYRGADFCGFAAQPGRRTVAGEVTRSLETLLRREVGLACAGRTDAGVHAIAQYVSVPVTASELAMPARRLMHGLSALLPDDISPAALYRAPKGFSARFDARSRSYRYRIVAGEARPVLAWDHAWWLRGELDAAAMHDAAQLLVGEHDFKSFCKATSAEGKPTHRCVMRCDVSEEWECGERVVCIDVVGNAFLHSMVRTMAGTLVEVGRGHRGAAWVADALAACDRKAAGPCAPAKGLTFVGVDYPQELLVPWE","length":286,"molWeight":31102,"crc64":"CCA819B60A225344","md5":"2FD2E7C4AE0534BCEF89A0CDC700ADDB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":1},"uniParcId":"UPI000F7165E4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JWB2","uniProtkbId":"A0A3G9JWB2_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49761.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004512"}],"value":"2,3-bisphosphoglycerate-dependent phosphoglycerate mutase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"value":"BPG-dependent PGAM"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"value":"PGAM"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"value":"Phosphoglyceromutase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"value":"dPGM"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004512"}],"value":"5.4.2.11"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49761.1"}],"value":"gpmA_1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"value":"gpmA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49761.1"}],"value":"Pcatena_03480"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004512"}],"value":"Catalyzes the interconversion of 2-phosphoglycerate and 3-phosphoglycerate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-phosphoglycerate = (2R)-3-phosphoglycerate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15901"},{"database":"ChEBI","id":"CHEBI:58272"},{"database":"ChEBI","id":"CHEBI:58289"}],"ecNumber":"5.4.2.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000380"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004512"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004512"}],"value":"Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006717"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"value":"Belongs to the phosphoglycerate mutase family. BPG-dependent PGAM subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Active site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"Tele-phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-1"}]},{"type":"Active site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-1"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":119,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-2"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR613078-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01039"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49761.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_126421095.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_AP019367.1"}]},{"database":"AlphaFoldDB","id":"A0A3G9JWB2","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"88848492","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_03480","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9781415at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00186"}]},{"database":"Proteomes","id":"UP000273154","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0004619","properties":[{"key":"GoTerm","value":"F:phosphoglycerate mutase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07067","properties":[{"key":"EntryName","value":"HP_PGM_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1240:FF:000003","properties":[{"key":"EntryName","value":"2,3-bisphosphoglycerate-dependent phosphoglycerate mutase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1240","properties":[{"key":"EntryName","value":"Phosphoglycerate mutase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01039","properties":[{"key":"EntryName","value":"PGAM_GpmA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013078","properties":[{"key":"EntryName","value":"His_Pase_superF_clade-1"}]},{"database":"InterPro","id":"IPR029033","properties":[{"key":"EntryName","value":"His_PPase_superfam"}]},{"database":"InterPro","id":"IPR001345","properties":[{"key":"EntryName","value":"PG/BPGM_mutase_AS"}]},{"database":"InterPro","id":"IPR005952","properties":[{"key":"EntryName","value":"Phosphogly_mut1"}]},{"database":"NCBIfam","id":"NF010713","properties":[{"key":"EntryName","value":"gpmA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01258","properties":[{"key":"EntryName","value":"pgm_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11931","properties":[{"key":"EntryName","value":"PHOSPHOGLYCERATE MUTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00300","properties":[{"key":"EntryName","value":"His_Phos_1"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00855","properties":[{"key":"EntryName","value":"PGAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53254","properties":[{"key":"EntryName","value":"Phosphoglycerate mutase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00175","properties":[{"key":"EntryName","value":"PG_MUTASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDDTMQLVIIRHGQSEWNKLNLFTGWTDVDLTQEGRAEAAAGGRALAEAGFDFDVCYTSRLKRAIHTLDIVLAEMDREWLPVVKTWKLNERHYGALQGLNKADAAAEHGEEQVLVWRRSFDVRPPALEPGDERDPHAQDMYRDVPADELPYTECLKDCIARAWPYFEEVIRPQMLAGKRVLIAAHGNSLRSLVMKLEGLTPEQILKVNIPTGVPLVYTFDRDLNVLDKHYIGDADAIAAKIDAVADQGKARG","length":253,"molWeight":28405,"crc64":"985AF05E40D5DDB5","md5":"DD524E4DA34BAA74AD4FDE6590223110"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1},"countByFeatureType":{"Active site":2,"Binding site":7,"Site":1},"uniParcId":"UPI000F6D8D44"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A3G9JWC3","uniProtkbId":"A0A3G9JWC3_9ACTN","entryAudit":{"firstPublicDate":"2019-02-13","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-02-13","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Parolsenella catena","taxonId":2003188,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49757.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Coriobacteriia","Coriobacteriales","Atopobiaceae","Parolsenella"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Aspartate--tRNA(Asp/Asn) ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"6.1.1.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Aspartyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"AspRS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Non-discriminating aspartyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"ND-AspRS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49757.1"}],"value":"aspS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"BBH49757.1"}],"value":"Pcatena_03440"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Aspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Asx) + L-aspartate + ATP = L-aspartyl-tRNA(Asx) + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18349"},{"database":"Rhea","id":"RHEA-COMP:9710"},{"database":"Rhea","id":"RHEA-COMP:9711"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78516"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.23","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006303"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Belongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":584,"modifier":"EXACT"}},"description":"Aminoacyl-transfer RNA synthetases class-II family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50862"}]},{"type":"Region","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Aspartate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}]},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":477,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":511,"modifier":"EXACT"},"end":{"value":511,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":518,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":563,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Important for tRNA non-discrimination","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00044"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-CIBEQ7UAI0H70","citationType":"submission","authors":["Sakamoto M.","Ikeyama N.","Murakami T.","Mori H.","Yuki M.","Ohkuma M."],"title":"Comparative genomics of Parolsenella catena and Libanicoccus massiliensis: Reclassification of Libanicoccus massiliensis as Parolsenella massiliensis comb. nov.","publicationDate":"NOV-2018","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}],"value":"JCM 31932","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000273154"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AP019367","properties":[{"key":"ProteinId","value":"BBH49757.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A3G9JWC3","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"pcat:Pcatena_03440","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802326at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000273154","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:0004815","properties":[{"key":"GoTerm","value":"F:aspartate-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050560","properties":[{"key":"GoTerm","value":"F:aspartate-tRNA(Asn) ligase 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:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006422","properties":[{"key":"GoTerm","value":"P:aspartyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00777","properties":[{"key":"EntryName","value":"AspRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04317","properties":[{"key":"EntryName","value":"EcAspRS_like_N"},{"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":"Gene3D","id":"3.30.1360.30","properties":[{"key":"EntryName","value":"GAD-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00044","properties":[{"key":"EntryName","value":"Asp_tRNA_synth_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004364","properties":[{"key":"EntryName","value":"Aa-tRNA-synt_II"}]},{"database":"InterPro","id":"IPR006195","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR004524","properties":[{"key":"EntryName","value":"Asp-tRNA-ligase_1"}]},{"database":"InterPro","id":"IPR047089","properties":[{"key":"EntryName","value":"Asp-tRNA-ligase_1_N"}]},{"database":"InterPro","id":"IPR002312","properties":[{"key":"EntryName","value":"Asp/Asn-tRNA-synth_IIb"}]},{"database":"InterPro","id":"IPR047090","properties":[{"key":"EntryName","value":"AspRS_core"}]},{"database":"InterPro","id":"IPR004115","properties":[{"key":"EntryName","value":"GAD-like_sf"}]},{"database":"InterPro","id":"IPR029351","properties":[{"key":"EntryName","value":"GAD_dom"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR004365","properties":[{"key":"EntryName","value":"NA-bd_OB_tRNA"}]},{"database":"NCBIfam","id":"NF001750","properties":[{"key":"EntryName","value":"aspS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00459","properties":[{"key":"EntryName","value":"aspS_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22594:SF5","properties":[{"key":"EntryName","value":"ASPARTATE--TRNA LIGASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR22594","properties":[{"key":"EntryName","value":"ASPARTYL/LYSYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02938","properties":[{"key":"EntryName","value":"GAD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00152","properties":[{"key":"EntryName","value":"tRNA-synt_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01336","properties":[{"key":"EntryName","value":"tRNA_anti-codon"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01042","properties":[{"key":"EntryName","value":"TRNASYNTHASP"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55261","properties":[{"key":"EntryName","value":"GAD domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50249","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50862","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_II"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQDTSTTPAVEAQAASAFAAETEAMHEHSMHTRTAGELRRENIGEEVTLTGWVWRRRDHGGLIFVDLRDRSGMTQCTFDPEHSGGTAFHAAEVIRTEWPIRVHGVVRGRDEETINAKLPTGEVEVCVDTIEVLNRSKTPPFQIEDGIDTSEDTRLRYRYLDIRRPEMMANLKLRSDFTFAIREALHKRAFMEVETPFLFKSTPEGARDFLVPCRIQPGHFYALPQSPQLLKQLLMVGGVERYYQVAKCFRDEDLRADRQPEFTQVDIEMSFVDQDDVMDALEDVLRDAFAKMGVELPTPLRRMQYWDAMDTYGIDKPDTRYGMTLKDVTDIFVNSKFKVFSSAANTEGSVVKCINAKGAGTWPRAQIDKLEDVAKTFGAKGLAWIAFREDGSINSPIVKFFSDEEMAALRERAEVEPGDLVMFAAGPRLASDEILGGMRCHMADALNVPREGHDFLWVVNFPLFHWDEERKAYAAEHQPFTLPTESDVEKIKADPLAAGSYTYDFVMDGYEAGGGGMRIHDAAMQEAMLELLGFTPERAREQFGFVMEALEFGAPPMGGFALGLDRVCMLLTGSDSIREVMAFPKTSSGSDLMSDAPGEVSAKQLKEVSIRPL","length":613,"molWeight":68754,"crc64":"E0E62A400257B4A4","md5":"15C8B76952A354B78AFE1B3279FD8A5B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Binding site":8,"Site":1},"uniParcId":"UPI000F6BC6EB"}}]}