{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SZN8","uniProtkbId":"A0ABY4SZN8_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57282.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57282.1"}],"value":"IM816_11595"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059148"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":536,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":517,"modifier":"EXACT"},"end":{"value":517,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"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":380,"modifier":"EXACT"},"end":{"value":383,"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":403,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57282.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57282.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57282.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338192.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11595","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO: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":"MTPLIFVTGGVVSSLGKGIAAASLASILEARGLSVTMMKLDPYINVDPGTMSPFQHGEVYVTDDGAETDLDLGHYERFVRTRLTGKNSITAGKIYESVIRKERRGDYLGATVQVIPHITDEIKHSIHEATRGFDVALVEIGGTVGDIESLPFLEAIRQLRIEHGPEKCMFVHLTLVPYIKAAGEIKTKPTQHSVKELRSIGIQPDVLLCRCEEPLPDGERHKIALFTNVPKNAVISTIDVDIIYKLPMWLHEQGLDELVIKRLGLDAGPADLSSWERTVEAVEHPRDEITVAIVGKYVEHKDAYKSLGEALRHGGIKQSTRVNLRWVDSEDVEARGARTVLGDADAILVPGGFGKRGFEGKILAAQFAREAGVPYFGICYGMHAAVVEFARNTAGLTQADSSENDRNTPDPVIALITEWTTASGETEIRTERSDLGGTMRLGAQECRLKAGTLARELYGEDVVRERHRHRYEFNNRYRQSFEDLGLVISGKSMDDLLVEIVELPRQVHPWFLGCQAHPEFTSTPREGHPLFIGFVRAAREYKAVRDGEKLAARSEESAA","length":559,"molWeight":61808,"crc64":"C2DDAC5FF260745D","md5":"2BB939FEC7BA59A1C63724D30ADD640F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":16},"uniParcId":"UPI002025CEDF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4T071","uniProtkbId":"A0ABY4T071_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58352.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"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":"URL58352.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58352.1"}],"value":"IM816_17455"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":110,"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":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"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":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI: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":383,"modifier":"EXACT"},"end":{"value":383,"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":389,"modifier":"EXACT"},"end":{"value":390,"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":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":426,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":443,"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":"UP001056681"}],"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-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58352.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58352.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL58352.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250339071.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_17455","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"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":"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":"MTATPLHVLILAAGEGKRMKSASAKVLMPLAGRPLLAHVIEAARSLEPAGIHVVYGHNGAQVREAFAADASLGWIEQRERLGTGHAVRTALESLQASRQLEGRVLVLYGDVPLIRPETLAMLATSSDALSMLATRLTDPSGYGRVVLDAAGRVRHIVEEKDASAAERAIDLVNTGIVAADAAKLLTWTRRLGNDNAQGEYYLTDVFEMAAAEGVPAACVDCDAVEASGANDPWQLATLEALFRERCARALALAGVRLADPRRLDVRGTVSAGRDVEVDVDVIFEGNVVLGDDVRIGPFTRVRHANLAAGTVVLAHCDLDGVVTHGPCTIGPFARLRPGTDLAAGVHIGNFVETKNAVIAEGSKANHLSYLGDTVIGSKVNIGAGTITCNYDGVNKSRTTIEDGVFVGSNSSLVAPVTLHAGATIGAGSVITKNAPADTLTIARGRQTAVEGWHRPTKKT","length":459,"molWeight":48166,"crc64":"1A86B7ECBD265D67","md5":"FC7C4459A3EC2C5369AAA0040059C074"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":20},"uniParcId":"UPI002025E538"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4T194","uniProtkbId":"A0ABY4T194_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58724.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"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":"URL58724.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58724.1"}],"value":"IM816_00875"}]}],"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":3,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":393,"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":189,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"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":288,"modifier":"EXACT"},"end":{"value":288,"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":305,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":323,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58724.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58724.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL58724.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_072323233.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_00875","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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":"MSLRQRRILIGVTGGIAAYKTCELVRRLRDLDAEVRVVMTEGATHFVTPTTFQALSGQPVRVSLWDEHGEAAMGHIELARWAERVLIAPASADTIARLAHGLADDLLSTVVLATAAPVYVAPAMNQQMWANLAVQANVGTLRVRGIGVLGPADGDQACGDIGSGRMLEPHELRDILVASFGEQPLRGRTVVVSAGPTYEDIDPVRFIGNRSSGRMGFAVAAAARDAGADVTLIAGPVSLPTPPGIRRVDVRSARQMHDAVLAAAEHADIYVGAAAVGDYRPDVEAAHKLKKADGAPLRIELIENPDIIATLSTRPSRPFLVGFAAETRELAGYAQDKLRRKRIDMIAANEVGEGKGFEVANNALHLYWPDGDATLPEMPKTELARRLVACIAERFLSGTGRTS","length":403,"molWeight":43107,"crc64":"5BE320E577B6B0F6","md5":"616E5AACA56152F5C536DB6CA3F2CFA8"},"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":"UPI0009086C32"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4T1D2","uniProtkbId":"A0ABY4T1D2_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57075.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"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":"URL57075.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57075.1"}],"value":"IM816_10430"}]}],"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":1075,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5050817537"},{"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":679,"modifier":"EXACT"},"end":{"value":871,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":938,"modifier":"EXACT"},"end":{"value":1075,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":555,"modifier":"EXACT"},"end":{"value":937,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":938,"modifier":"EXACT"},"end":{"value":1075,"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":715,"modifier":"EXACT"},"end":{"value":715,"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":754,"modifier":"EXACT"},"end":{"value":754,"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":756,"modifier":"EXACT"},"end":{"value":756,"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":761,"modifier":"EXACT"},"end":{"value":761,"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":787,"modifier":"EXACT"},"end":{"value":787,"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":788,"modifier":"EXACT"},"end":{"value":788,"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":789,"modifier":"EXACT"},"end":{"value":789,"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":790,"modifier":"EXACT"},"end":{"value":790,"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":830,"modifier":"EXACT"},"end":{"value":830,"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":830,"modifier":"EXACT"},"end":{"value":830,"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":830,"modifier":"EXACT"},"end":{"value":830,"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":842,"modifier":"EXACT"},"end":{"value":842,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":842,"modifier":"EXACT"},"end":{"value":842,"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":842,"modifier":"EXACT"},"end":{"value":842,"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":842,"modifier":"EXACT"},"end":{"value":842,"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":842,"modifier":"EXACT"},"end":{"value":842,"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":844,"modifier":"EXACT"},"end":{"value":844,"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":844,"modifier":"EXACT"},"end":{"value":844,"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":"UP001056681"}],"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-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57075.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57075.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57075.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338032.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_10430","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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":"3.30.1490.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"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":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"PRK05294.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRSDIKTILVIGAGPIVIGQACEFDYSGAQACKALKEEGYRVVLVNSNPATIMTDPETAHAVYIEPINWQTVERIIAKERPDAVLPTMGGQTGLNCALDLADNGVLEKYGVELIGATRDAIRMAEDRDLFRKAMAEIGLECPKAEVARSMEQALEIQTTVGFPTIIRPSFTLGGSGGGIAYNKEEFVEIVGRGLELSPVHEVLVEESVLGWKEFEMEVVRDKADNCIIVCSIENFDPMGVHTGDSITVAPAQTLTDKEYQRLRNASIAVLRKIGVDTGGSNVQFGINAEDGRVVVIEMNPRVSRSSALASKATGFPIAKVAAKLAVGYTLDELKNDITGGLTPASFEPSIDYVVTKIPRFAFEKFPAADARLTTQMKSVGEVMAMGRTFHESMQKALRGLEIGKTGLNPTGLDIGSEEGFLTLKRELREPRPDRVFHVADAFRAGLSLEEVHDLTHIDPWFLAAFEDIVMTEGEVQRQGLTALDEPRMRELKRMGFSDARLAELVGTDEGAVRHLRRTLGVRPVYKRVDSCAAEFATTTAYMYSTYEEECEANPTNRDKIVVLGGGPNRIGQGIEFDYCCVHAALALREDGFETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVDLEKPKGVIVQYGGQTPLKLARALEAAGVPVIGTSADSIDLAEDRERFQKMIQKLELKQPPNRTARNADEALALAREIGYPLVVRPSYVLGGRAMEIVYADADLSRYIREAVQVSNESPVLLDRFLDHAVEVDVDIVADAEGNVLVGGIMEHIEEAGVHSGDSSCSLPPYSLSAEVQDEMRRQVKLMAQELKVIGLMNTQFAIQGDEVFILEVNPRASRTVPFVCKATGMSLAKIAARAMAGRTLVEQNATKEIIPSYYSVKEAIFPFLKFQNVDPILGPEMRSTGEVMGVGRSFGAAFARGHEAAGIKAPPKGKVFMSVRDADKDRLLSIAQDVASRGYGIVATSGTAKFLQDNGVACERINKVLEGRPHIVDLIKNGEVVYIVNTTEGKQAISDSFSIRREALQQRVTYSTTVAGARALVHSLDFHADGEVNSLQDLHKELNA","length":1075,"molWeight":117428,"crc64":"9E5A27033AFEC069","md5":"3C3E43D37D989B3CE7A9522755BD131D"},"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":"UPI0020276A06"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4T2X3","uniProtkbId":"A0ABY4T2X3_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59283.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional NAD(P)H-hydrate repair enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Nicotinamide nucleotide repair protein"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"NAD(P)H-hydrate epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"5.1.99.6"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59283.1"}],"value":"IM816_03995"}]}],"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":16,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":68,"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":65,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":160,"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":163,"modifier":"EXACT"},"end":{"value":163,"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":255,"modifier":"EXACT"},"end":{"value":255,"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":316,"modifier":"EXACT"},"end":{"value":316,"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":363,"modifier":"EXACT"},"end":{"value":363,"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":400,"modifier":"EXACT"},"end":{"value":404,"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":429,"modifier":"EXACT"},"end":{"value":429,"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":430,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59283.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59283.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL59283.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250339862.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_03995","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAHDLAVDLFTSAQSRAIDQRAMRELGIPGFELMTRAASAAYAMLRRRWPASRRVRVVCGGGNNGGDGYLVARDALADGLAVDLIALDPPKGDDARRARQAFEALGGVAKPLSAWGGLAPADMMVDAIYGTGLNRAPEGEAREAIEAINAARAPVLALDVPSGLSADTGACPGVVVRATATATFIVRKRGLYTHQAEVAGDVELHTLDLPASVLEAPDARLLVAESLPPRALDSHKGSNGHVLAIGGDHGTGGAIRMAAEAALRTGAGLVSVATRDQNVLAMNAARPELMPHGVDGPQTLQPMLDKASVLALGPGLGQAAWGHALWTTALDADKPTVLDADGLNLLHSEPRALPTKTVLTPHPGEAARLLGMSTADVQADRFAAARALAARFHATVVLKGNGSLIASAEGEVSVCPWGNPGMASGGMGDTLTGIIAGLLAQGCEPYHAACLGVGLHARAADVAAQDGQRGLLAGDLLIPLRHLVNGVDA","length":490,"molWeight":50219,"crc64":"EF558AFEE3D64CB1","md5":"CAC7DB3FFED6572E90DEB5BA0332B75C"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI00202728C4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4T3I7","uniProtkbId":"A0ABY4T3I7_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59459.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"RecBCD enzyme subunit RecB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"3.1.11.5"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"DNA 3'-5' helicase subunit RecB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Exonuclease V subunit RecB"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"ExoV subunit RecB"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Helicase/nuclease RecBCD subunit RecB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59459.1"}],"value":"recB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59459.1"}],"value":"IM816_04970"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.","ecNumber":"3.1.11.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Belongs to the helicase family. UvrD subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"UvrD-like helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51198"}]},{"type":"Domain","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":766,"modifier":"EXACT"}},"description":"UvrD-like helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51217"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":880,"modifier":"EXACT"}},"description":"DNA-binding and helicase activity, interacts with RecC","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":928,"modifier":"EXACT"},"end":{"value":1215,"modifier":"EXACT"}},"description":"Nuclease activity, interacts with RecD and RecA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Active site","location":{"start":{"value":1119,"modifier":"EXACT"},"end":{"value":1119,"modifier":"EXACT"}},"description":"For nuclease activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Binding site","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00560"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":985,"modifier":"EXACT"},"end":{"value":985,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1106,"modifier":"EXACT"},"end":{"value":1106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1119,"modifier":"EXACT"},"end":{"value":1119,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59459.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL59459.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL59459.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250340010.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_04970","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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:0009338","properties":[{"key":"GoTerm","value":"C:exodeoxyribonuclease V complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008854","properties":[{"key":"GoTerm","value":"F:exodeoxyribonuclease V activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd22352","properties":[{"key":"EntryName","value":"RecB_C-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.320.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.486.10","properties":[{"key":"EntryName","value":"PCRA, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.3170.10","properties":[{"key":"EntryName","value":"Recbcd, chain B, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01485","properties":[{"key":"EntryName","value":"RecB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011604","properties":[{"key":"EntryName","value":"PDDEXK-like_dom_sf"}]},{"database":"InterPro","id":"IPR038726","properties":[{"key":"EntryName","value":"PDDEXK_AddAB-type"}]},{"database":"InterPro","id":"IPR004586","properties":[{"key":"EntryName","value":"RecB"}]},{"database":"InterPro","id":"IPR011335","properties":[{"key":"EntryName","value":"Restrct_endonuc-II-like"}]},{"database":"InterPro","id":"IPR000212","properties":[{"key":"EntryName","value":"UvrD-like"}]},{"database":"InterPro","id":"IPR014016","properties":[{"key":"EntryName","value":"UvrD-like_ATP-bd"}]},{"database":"InterPro","id":"IPR014017","properties":[{"key":"EntryName","value":"UvrD-like_C"}]},{"database":"NCBIfam","id":"TIGR00609","properties":[{"key":"EntryName","value":"recB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070:SF23","properties":[{"key":"EntryName","value":"RECBCD ENZYME SUBUNIT RECB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070","properties":[{"key":"EntryName","value":"UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12705","properties":[{"key":"EntryName","value":"PDDEXK_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00580","properties":[{"key":"EntryName","value":"UvrD-helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13361","properties":[{"key":"EntryName","value":"UvrD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52980","properties":[{"key":"EntryName","value":"Restriction endonuclease-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51198","properties":[{"key":"EntryName","value":"UVRD_HELICASE_ATP_BIND"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51217","properties":[{"key":"EntryName","value":"UVRD_HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTPMQPLQPVTMPLHGVRLIEASAGTGKTWTIAALYVRAVLGHDMPQPLLPPQLLVVTFTEAATQELRERIRARLVEAARAFRASASDEPFLAELIATYPVDAHASCARRLELAAQWMDEAAIFTIHGWSQRMLTQHAFGSGHAFALTLEPDESELLADCVRDYWRQTFYPLPPRQAEMVLEEWRSPDDLLRALKPLFYGGEVTLRVAGEVLAAATDPRALMASREAWQAEHDRLLAEAAEAWRSDVDRIEALLTEASATKVLNNTRYRPDRMPGYLAPVRRWAFGGEAIEEALQRFTATRLADAAGKGKQRPEHPAFAALDAWQAWHEHKVDIRHALLVDALARVRERFAAQKRRRAQIGFDDLLHRLDAALRSDAGDALAETIRRQFPLALIDEFQDTDPVQYRIFSRIYAGVPDVGLLLIGDPKQAIYAFRGADIHTYLSARAQALAPHYSLDTNYRSSHAMIEAVNAVFLHGERHPRGAFHFPDRGLPFAAVSAKGRAERFVVAKESQPALRLWLLDDERPVGVRHYREQMADACASEIVRLLEGATRGDTGFAEADGHIVPLRPADVAVLVRSRSEAAQVRASLAARQVRSVFLSDRDSVWESTEAEDVLAWLRAAAAPASDTAMRAALATRTLDLGYTELEQLNVDEAHWERRGEEFLALRQVWQHAGVLAMLHALLHRFDLPARLLPRAGGERALTNVLHLAELLQHAASTLDGEQALIRHVAERIADTASHHGDDQLVRLESDDDVVKVITIHKSKGLEYPIVFLPFVCASGGPHPGQTAYRYHDGTGSQLELVSKSKGGAASEQAKDAADLAAMQEDLRLLYVAMTRARHACYVGVAPVCHGTSRTPQVHRSAFGHLLSGGEEIGNGRIAGLLHELAQATPSIRVEYMPPPDERRFVAPDRPEAARPAREAMARRADPWRIASYSGLRYADEVSAPETATDDVIVEYATEPVVAAPAVAGIHAFERGAEAGTFLHDLLEWIAEEGFAIVASDSARLRDTVARRCERRGWSAFIDLLTDWLSMLLRTPLALPDGGQLALASLDDPSRYRAELEFLFASRGVDTLALDRIVREHTLDGEARPTLAADIINGMLKGFIDLIVEHEGRWYVIDYKSNWLGVDAQAYTTAAMRRSILEARYELQYALYLLALHRQLRARLGDAYDYDTHIGGAVYLYLRGVDGHGHGVHVERPPRAMIEAMDRLFEGASA","length":1215,"molWeight":134768,"crc64":"1C9C0FB2CFC7CF74","md5":"63390725B4841B960C1D44B8EA788070"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"MISCELLANEOUS":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":4},"uniParcId":"UPI00202726F2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4T586","uniProtkbId":"A0ABY4T586_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate dehydrogenase [ubiquinone]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"1.2.5.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate oxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"POX"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Pyruvate:ubiquinone-8 oxidoreductase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"}],"value":"poxB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"}],"value":"IM816_15775"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"A peripheral cell membrane enzyme that catalyzes the oxidative decarboxylation of pyruvate to form acetate and CO(2). It channels electrons from the cytoplasm to the respiratory chain at the cell membrane via ubiquinone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ubiquinone + pyruvate + H2O = a ubiquinol + acetate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27405"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:30089"}],"ecNumber":"1.2.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 FAD per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Binds 1 thiamine pyrophosphate per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"The C-terminus inhibits activity; it has to move for the enzyme to be active. Activated by lipid-binding, which occurs via the C-terminus"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Has 4 domains; the Pyr domain which binds the pyrimidine moiety of the thiamine pyrophosphate cofactor, the FAD-binding domain, the PP-binding domain which binds the pyrophosphate portion of thiamine pyrophosphate and the C-terminal membrane binding region. The C-terminus is held closely against the rest of the protein and covers the active site; during activation it unfolds from the rest of the protein and forms an amphipathic helix upon membrane binding, exposing the active site"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362132"}],"value":"Belongs to the TPP enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme N-terminal TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02776"}]},{"type":"Domain","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00205"}]},{"type":"Domain","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":530,"modifier":"EXACT"}},"description":"Thiamine pyrophosphate enzyme TPP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02775"}]},{"type":"Region","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"FAD-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Region","location":{"start":{"value":536,"modifier":"EXACT"},"end":{"value":577,"modifier":"EXACT"}},"description":"Membrane-binding domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]},{"type":"Binding site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":413,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":440,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":465,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Site","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":470,"modifier":"EXACT"}},"description":"Moves into active site upon enzyme activation, plays a role in electron transfer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0446","category":"Ligand","name":"Lipid-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00850"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL58044.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL58044.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338823.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_15775","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008289","properties":[{"key":"GoTerm","value":"F:lipid binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052737","properties":[{"key":"GoTerm","value":"F:pyruvate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048039","properties":[{"key":"GoTerm","value":"F:ubiquinone binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042867","properties":[{"key":"GoTerm","value":"P:pyruvate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02014","properties":[{"key":"EntryName","value":"TPP_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd07039","properties":[{"key":"EntryName","value":"TPP_PYR_POX"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1220:FF:000013","properties":[{"key":"EntryName","value":"Pyruvate dehydrogenase [ubiquinone]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.1220","properties":[{"key":"EntryName","value":"TPP-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00850","properties":[{"key":"EntryName","value":"POX"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR047211","properties":[{"key":"EntryName","value":"POXB-like"}]},{"database":"InterPro","id":"IPR044261","properties":[{"key":"EntryName","value":"Pyruvate_dehydrogenase"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR012000","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_cen_dom"}]},{"database":"InterPro","id":"IPR012001","properties":[{"key":"EntryName","value":"Thiamin_PyroP_enz_TPP-bd_dom"}]},{"database":"InterPro","id":"IPR000399","properties":[{"key":"EntryName","value":"TPP-bd_CS"}]},{"database":"InterPro","id":"IPR011766","properties":[{"key":"EntryName","value":"TPP_enzyme_TPP-bd"}]},{"database":"InterPro","id":"IPR047212","properties":[{"key":"EntryName","value":"TPP_POXB-like"}]},{"database":"InterPro","id":"IPR047210","properties":[{"key":"EntryName","value":"TPP_PYR_POXB-like"}]},{"database":"NCBIfam","id":"NF006591","properties":[{"key":"EntryName","value":"PRK09124.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42981:SF2","properties":[{"key":"EntryName","value":"PYRUVATE DEHYDROGENASE [UBIQUINONE]"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02775","properties":[{"key":"EntryName","value":"TPP_enzyme_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00205","properties":[{"key":"EntryName","value":"TPP_enzyme_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02776","properties":[{"key":"EntryName","value":"TPP_enzyme_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00187","properties":[{"key":"EntryName","value":"TPP_ENZYMES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSIANVADLIAETLEEAGVRRIYGVVGDSLNAITESLRQRQRIDWVHVRHEEVAAFAAGGESQLTGELAVCAGSCGPGNLHLINGLFDCHRSRTPVLAIAAHIPSAEIGNGYFQETHPTELFRECSVYCEMVSDAAQMPRVIDAAIRAAVGQRGVAVVVIPGDVAMRKSPVKAATPAASLLPAAPRVVPAERQLDALAALLNEGKRVTLLCGRGTAGAHDELIALADALKAPIVHALGGKEFVEYDNPFDVGMTGLIGFSSGYHAMEDCDTLLMLGTDFPYRQFYPEDAKIAQVDIRPGNIGRRCRVDLGIVGDVGETLRALLPRIEPKRVRGHLDRCLAHYERARHDLDELARIEPGHDLIHPQQVTRLVSELAEEDAVFTCDVGTPTIWAARYLRMNGKRRLLGSWVHGSMACAMPQAIGAQAAYPERQVISLSGDGGFTMLMGDFITLAQQKLPVKVIVLNNGTLGFVELEMKAAGLLETGVELRNPDFAAMANAMGIHGRRVARASDLPSAIAEVLAHEGPALLDVVSNRLELSIPPKISGEQVKGLSLYALKAVMSGRGDSIVDLALSNLSR","length":577,"molWeight":61956,"crc64":"A9E59E3EC1D16050","md5":"18201DC6414B5C013F83A868BB1718E8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"ACTIVITY REGULATION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":9,"Site":1},"uniParcId":"UPI0020275764"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4T6B2","uniProtkbId":"A0ABY4T6B2_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60422.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-tripeptide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramyl-tripeptide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60422.1"}],"value":"IM816_15280"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60422.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60422.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60422.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL60422.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250340781.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_15280","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRLADLLDGFADASGAGELDVSGLAIDSREIEPGNAFVALRGTKDHGIAFAAKAVERGAVVVLAEPPYDAPELGVPVVAVEKLREKTGAIAARFFGEPSAALKVIGVTGTNGKTSTVQLLAQALAFLGRKPATVGTLGAGLHGAIAEGERTTPDAIRIQALLGSFREAGATHVAMEVSSHALEQGRVNAIAFDVAVFTNLTRDHLDYHGTMEAYGAAKAKLFAFDGLRAAVINIDDPFGAKLAKGLPEGIAKLRTSMATDSTDKDAEIRADIIVTSAKGLSFNLVTPWGARTVRSALLGRFNVANLLAVAAVLGALDEPFERIHAALEALQPVNGRMSRLGGDGRKPLVVVDYSHTPDSLKQALLALRSHTKGRLLCVFGAGGDRDQGKRPIMAGIAERLADVVIVTDDNPRTEDGDAIVAQIVAGFAHPDTVIVERDRAQAIALALADAKADDVVLIAGKGHETYQEGPEGKRPFDDLAVAREAMESSKKGVRA","length":495,"molWeight":51813,"crc64":"2ADE45A4E459B93E","md5":"EF55B769E8BA30D548F06BD004851777"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI0020267238"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4TCB0","uniProtkbId":"A0ABY4TCB0_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60346.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60346.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60346.1"}],"value":"IM816_09630"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"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":124,"modifier":"EXACT"},"end":{"value":124,"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":127,"modifier":"EXACT"},"end":{"value":127,"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":173,"modifier":"EXACT"},"end":{"value":174,"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":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":229,"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":306,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"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-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60346.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL60346.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL60346.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250340733.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_09630","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.530:FF:000003","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000008","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSHAVNTPAEKVNLLDFDRQGLRDFFAQLGEKTYRAEQVMKWIYHRLESDFEKMTDVGKALREKLTASCYVGPPKTVFEKGAVDGTHKWLLGMDGGNAIETVYIPEPTRGTLCVSSQVGCALNCQFCSTATQGFSRNLSTAEIIGQVWVAAKHLGNVPHQQRRITNVVMMGMGEPLLNFDNVVKAMSLMRDDLGFGLASKRVTLSTAGLVPMIDRLSAESDVSLAVSLHAANDELRTELVPLNKRYPLAELMGACERYIQRAPRTSITFEYTLMKGVNDQPEHARQLIKFMRRLPGANKVNLIPFNPFPGARFERSGQDEIRAFQTQLLNAGVLTMLRRTRGDDIDAACGQLKGQVVDRTRRQAEFRKKLAEGVVNAA","length":378,"molWeight":42063,"crc64":"26C342FB45EE924A","md5":"58BF0E50A6E5BAE9E8EB5135633009C0"},"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":"UPI002026CE79"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SW38","uniProtkbId":"A0ABY4SW38_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56921.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}],"value":"Inosine-5'-monophosphate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"IMP dehydrogenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"IMPD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"IMPDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}],"value":"1.1.1.205"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56921.1"}],"value":"guaB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56921.1"}],"value":"IM816_09585"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + NAD(+) + H2O = XMP + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11708"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58053"}],"ecNumber":"1.1.1.205","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048028"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}],"value":"Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005502"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003927"}],"value":"Belongs to the IMPDH/GMPR family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"CBS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51371"}]},{"type":"Domain","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"CBS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51371"}]},{"type":"Active site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Thioimidate intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-1"}]},{"type":"Active site","location":{"start":{"value":398,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-1"}]},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-4"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-4"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-4"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":337,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":358,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":412,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":466,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":468,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023122"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00703"}],"id":"KW-0129","category":"Domain","name":"CBS domain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0332","category":"Biological process","name":"GMP biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56921.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56921.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL56921.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_072321041.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_09585","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0003938","properties":[{"key":"GoTerm","value":"F:IMP dehydrogenase activity"},{"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:0000166","properties":[{"key":"GoTerm","value":"F:nucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006177","properties":[{"key":"GoTerm","value":"P:GMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006183","properties":[{"key":"GoTerm","value":"P:GTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04601","properties":[{"key":"EntryName","value":"CBS_pair_IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00381","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000003","properties":[{"key":"EntryName","value":"GMP reductase"},{"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_01964","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR000644","properties":[{"key":"EntryName","value":"CBS_dom"}]},{"database":"InterPro","id":"IPR046342","properties":[{"key":"EntryName","value":"CBS_dom_sf"}]},{"database":"InterPro","id":"IPR005990","properties":[{"key":"EntryName","value":"IMP_DH"}]},{"database":"InterPro","id":"IPR015875","properties":[{"key":"EntryName","value":"IMP_DH/GMP_Rdtase_CS"}]},{"database":"InterPro","id":"IPR001093","properties":[{"key":"EntryName","value":"IMP_DH_GMPRt"}]},{"database":"NCBIfam","id":"TIGR01302","properties":[{"key":"EntryName","value":"IMP_dehydrog"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11911:SF111","properties":[{"key":"EntryName","value":"INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11911","properties":[{"key":"EntryName","value":"INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00571","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00478","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000130","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00116","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM01240","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54631","properties":[{"key":"EntryName","value":"CBS-domain pair"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51412","properties":[{"key":"EntryName","value":"Inosine monophosphate dehydrogenase (IMPDH)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51371","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00487","properties":[{"key":"EntryName","value":"IMP_DH_GMP_RED"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRILAEALTYDDVFLVPGHSTVMPRDVDTSTRFTRGLRLNIPIVSAAMDTVTEARLAITMAQNGGIGIIHKNMTFEQQAAEVRLVKKFEAGVIRNPITVRPDTSIGEVLQLTRAHNISGVPVVDGEKLVGIVTSRDLRFERKHDDPVRNIMTREDRLITVKEGATHDEVLQLLHKNRIEKVLVVNDGFQLRGLITVKDIQKARDNPNAAKDSHERLVVGAAVGVAGDTEQRVEALVEAGVDVIVVDTAHGHSQSVIDRAAWVKKRFPQVQVIAGNIVTGEAARALLDAGVDAVKVGVGPGSICTTRIVTGIGVPQITSIDLVATALKGEIPLIADGGIRYSGDIPKALAAGASSVMLGSMFAGTEEAPGEVELFQGRSYKSYRGMGSIGAMQLGSKDRYFQDEADADKLVPEGIEGRVPYRGQLRNIIHQLIGGLRASMGYMGAATVEEIHAKAQFVKVTGAGVLEAHPHDIQITKEAPNYRLD","length":484,"molWeight":52107,"crc64":"9BA800DA54E85DFE","md5":"CB13A99FB842AECDA2A57553C1B83AE3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":13},"uniParcId":"UPI000908D5FB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SW39","uniProtkbId":"A0ABY4SW39_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56924.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00073635"}],"value":"Molybdopterin-synthase adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00066884"}],"value":"2.7.7.80"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00078531"}],"value":"MoaD protein adenylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075110"}],"value":"Molybdopterin-converting factor subunit 1 adenylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075328"}],"value":"Sulfur carrier protein MoaD adenylyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56924.1"}],"value":"moeB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56924.1"}],"value":"IM816_09600"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055169"}],"value":"Catalyzes the adenylation by ATP of the carboxyl group of the C-terminal glycine of sulfur carrier protein MoaD"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43616"},{"database":"Rhea","id":"RHEA-COMP:12159"},{"database":"Rhea","id":"RHEA-COMP:12202"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:90618"},{"database":"ChEBI","id":"CHEBI:90778"}],"ecNumber":"2.7.7.80","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052218"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005046"}],"value":"Cofactor biosynthesis; molybdopterin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00063809"}],"value":"Homodimer. Forms a stable heterotetrameric complex of 2 MoeB and 2 MoaD during adenylation of MoaD"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009919"}],"value":"Belongs to the HesA/MoeB/ThiF family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"Rhodanese","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50206"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56924.1"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56924.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56924.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL56924.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250337892.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_09600","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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:0061605","properties":[{"key":"GoTerm","value":"F:molybdopterin-synthase adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008146","properties":[{"key":"GoTerm","value":"F:sulfotransferase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004792","properties":[{"key":"GoTerm","value":"F:thiosulfate-cyanide sulfurtransferase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008641","properties":[{"key":"GoTerm","value":"F:ubiquitin-like modifier activating enzyme activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00158","properties":[{"key":"EntryName","value":"RHOD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00757","properties":[{"key":"EntryName","value":"ThiF_MoeB_HesA_family"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000033","properties":[{"key":"EntryName","value":"Adenylyltransferase and sulfurtransferase MOCS3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.250.10","properties":[{"key":"EntryName","value":"Rhodanese-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001763","properties":[{"key":"EntryName","value":"Rhodanese-like_dom"}]},{"database":"InterPro","id":"IPR036873","properties":[{"key":"EntryName","value":"Rhodanese-like_dom_sf"}]},{"database":"InterPro","id":"IPR045886","properties":[{"key":"EntryName","value":"ThiF/MoeB/HesA"}]},{"database":"InterPro","id":"IPR000594","properties":[{"key":"EntryName","value":"ThiF_NAD_FAD-bd"}]},{"database":"InterPro","id":"IPR035985","properties":[{"key":"EntryName","value":"Ubiquitin-activating_enz"}]},{"database":"NCBIfam","id":"NF004281","properties":[{"key":"EntryName","value":"PRK05690.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006444","properties":[{"key":"EntryName","value":"PRK08762.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10953:SF102","properties":[{"key":"EntryName","value":"ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10953","properties":[{"key":"EntryName","value":"UBIQUITIN-ACTIVATING ENZYME E1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00581","properties":[{"key":"EntryName","value":"Rhodanese"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00899","properties":[{"key":"EntryName","value":"ThiF"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00450","properties":[{"key":"EntryName","value":"RHOD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69572","properties":[{"key":"EntryName","value":"Activating enzymes of the ubiquitin-like proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52821","properties":[{"key":"EntryName","value":"Rhodanese/Cell cycle control phosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50206","properties":[{"key":"EntryName","value":"RHODANESE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDDLNRDRWLADLRSRVPEISATEALVRQQGGALLVDVREEAERATGTPLGALGLSRGFLELRIEEAEPDRERDILVLCGSGQRSLLGAEALQRMGYRTVSSVAGGMAAWKAAGLPVSTGALDADAAERYARQMLLPQIGAAGQAKLAAAKVLVVGAGGLGAPALLYLAAAGVGHVSIVDDDQVERSNLHRQVIHADARVGMAKAESARMTLTALNPRIHVRPVVERLRAENVEALLAGHDVVIDGADNFATRYLLAAATRRLRLPMVYAAIERFTGQVSVFDPRRDDSPCYRCLFPQPPAAADAPNCSEAGVLGVLPGLIGLVQATEAMKLILGVGQPLVGRLLTYDALAMQFRELRLRRDPACPGCGPDATFDGYVDIERMCSSAG","length":389,"molWeight":41420,"crc64":"B649225EAEEB5A44","md5":"CF2A0E497952289279C5A5E00D558166"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI00202730AD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SW71","uniProtkbId":"A0ABY4SW71_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56951.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"Enolase-phosphatase E1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"3.1.3.77"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"2,3-diketo-5-methylthio-1-phosphopentane phosphatase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56951.1"}],"value":"mtnC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56951.1"}],"value":"IM816_09740"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"Bifunctional enzyme that catalyzes the enolization of 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P) into the intermediate 2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate (HK-MTPenyl-1-P), which is then dephosphorylated to form the acireductone 1,2-dihydroxy-3-keto-5-methylthiopentene (DHK-MTPene)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-methylsulfanyl-2,3-dioxopentyl phosphate + H2O = 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:49252"},{"database":"ChEBI","id":"CHEBI:58828"}],"ecNumber":"3.1.3.77","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 3/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via salvage pathway; L-methionine from S-methyl-5-thio-alpha-D-ribose 1-phosphate: step 4/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"value":"Belongs to the HAD-like hydrolase superfamily. MasA/MtnC family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Region","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01681"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56951.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56951.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL56951.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250337916.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_09740","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0043715","properties":[{"key":"GoTerm","value":"F:2,3-diketo-5-methylthiopentyl-1-phosphate enolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043716","properties":[{"key":"GoTerm","value":"F:2-hydroxy-3-keto-5-methylthiopentenyl-1-phosphate phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043874","properties":[{"key":"GoTerm","value":"F:acireductone synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01629","properties":[{"key":"EntryName","value":"HAD_EP"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.720.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1000","properties":[{"key":"EntryName","value":"HAD superfamily/HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01681","properties":[{"key":"EntryName","value":"Salvage_MtnC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023943","properties":[{"key":"EntryName","value":"Enolase-ppase_E1"}]},{"database":"InterPro","id":"IPR036412","properties":[{"key":"EntryName","value":"HAD-like_sf"}]},{"database":"InterPro","id":"IPR006439","properties":[{"key":"EntryName","value":"HAD-SF_hydro_IA"}]},{"database":"InterPro","id":"IPR023214","properties":[{"key":"EntryName","value":"HAD_sf"}]},{"database":"NCBIfam","id":"TIGR01691","properties":[{"key":"EntryName","value":"enolase-ppase"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01549","properties":[{"key":"EntryName","value":"HAD-SF-IA-v1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20371","properties":[{"key":"EntryName","value":"ENOLASE-PHOSPHATASE E1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20371:SF1","properties":[{"key":"EntryName","value":"ENOLASE-PHOSPHATASE E1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00702","properties":[{"key":"EntryName","value":"Hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00413","properties":[{"key":"EntryName","value":"HADHALOGNASE"}]},{"database":"SFLD","id":"SFLDG01133","properties":[{"key":"EntryName","value":"C1.5.4:_Enolase-phosphatase_Li"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01129","properties":[{"key":"EntryName","value":"C1.5:_HAD__Beta-PGM__Phosphata"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00044","properties":[{"key":"EntryName","value":"enolase-phosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00003","properties":[{"key":"EntryName","value":"Haloacid_Dehalogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56784","properties":[{"key":"EntryName","value":"HAD-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDIRAILTDIEGTTSSIDFVKDVLFPYARTHLPAYVETHADTPEVQHWLHEAAKEAGFVEASRTEIIDLLVRWIDEDRKSTALKALQGMIWREGYESGAYVSHMYPEVAARLRAWHEQGLALYVYSSGSVPAQKLLFGYSENGDLTPLFSGYFDTQTGHKREVDSYRRIAEAIGLPPAQVLFLSDIREELDAARTAGMRTTQLVRPPQPLSENGHPAVADFDAIAP","length":227,"molWeight":25363,"crc64":"3B3BEDE43E4E8ED8","md5":"1EBC080F6160668A8AE2916429363C5D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Region":1},"uniParcId":"UPI002025B8BC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SWT3","uniProtkbId":"A0ABY4SWT3_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57176.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"Polyphosphate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"2.7.4.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"value":"ATP-polyphosphate phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"value":"Polyphosphoric acid kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57176.1"}],"value":"ppk1"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"value":"ppk"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57176.1"}],"value":"IM816_10980"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[phosphate](n) + ATP = [phosphate](n+1) + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19573"},{"database":"Rhea","id":"RHEA-COMP:9859"},{"database":"Rhea","id":"RHEA-COMP:14280"},{"database":"ChEBI","id":"CHEBI:16838"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"Belongs to the polyphosphate kinase 1 (PPK1) family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Polyphosphate kinase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13089"}]},{"type":"Domain","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":311,"modifier":"EXACT"}},"description":"Polyphosphate kinase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02503"}]},{"type":"Domain","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":506,"modifier":"EXACT"}},"description":"Polyphosphate kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF17941"}]},{"type":"Domain","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":689,"modifier":"EXACT"}},"description":"Polyphosphate kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13090"}]},{"type":"Active site","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}]},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":481,"modifier":"EXACT"},"end":{"value":481,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":577,"modifier":"EXACT"},"end":{"value":577,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":605,"modifier":"EXACT"},"end":{"value":605,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"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_00347"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57176.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57176.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57176.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338111.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_10980","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0009358","properties":[{"key":"GoTerm","value":"C:polyphosphate kinase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008976","properties":[{"key":"GoTerm","value":"F:polyphosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006799","properties":[{"key":"GoTerm","value":"P:polyphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd09168","properties":[{"key":"EntryName","value":"PLDc_PaPPK1_C2_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.870.10","properties":[{"key":"EntryName","value":"Endonuclease Chain A"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1840.10","properties":[{"key":"EntryName","value":"Polyphosphate kinase middle domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.310","properties":[{"key":"EntryName","value":"Polyphosphate kinase N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00347","properties":[{"key":"EntryName","value":"Polyphosphate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003414","properties":[{"key":"EntryName","value":"PP_kinase"}]},{"database":"InterPro","id":"IPR041108","properties":[{"key":"EntryName","value":"PP_kinase_C_1"}]},{"database":"InterPro","id":"IPR024953","properties":[{"key":"EntryName","value":"PP_kinase_middle"}]},{"database":"InterPro","id":"IPR036830","properties":[{"key":"EntryName","value":"PP_kinase_middle_dom_sf"}]},{"database":"InterPro","id":"IPR025200","properties":[{"key":"EntryName","value":"PPK_C_dom2"}]},{"database":"InterPro","id":"IPR025198","properties":[{"key":"EntryName","value":"PPK_N_dom"}]},{"database":"InterPro","id":"IPR036832","properties":[{"key":"EntryName","value":"PPK_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR03705","properties":[{"key":"EntryName","value":"poly_P_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003917","properties":[{"key":"EntryName","value":"PRK05443.1-1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003918","properties":[{"key":"EntryName","value":"PRK05443.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003921","properties":[{"key":"EntryName","value":"PRK05443.2-2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30218","properties":[{"key":"EntryName","value":"POLYPHOSPHATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30218:SF0","properties":[{"key":"EntryName","value":"POLYPHOSPHATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02503","properties":[{"key":"EntryName","value":"PP_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13090","properties":[{"key":"EntryName","value":"PP_kinase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17941","properties":[{"key":"EntryName","value":"PP_kinase_C_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13089","properties":[{"key":"EntryName","value":"PP_kinase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF015589","properties":[{"key":"EntryName","value":"PP_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56024","properties":[{"key":"EntryName","value":"Phospholipase D/nuclease"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF143724","properties":[{"key":"EntryName","value":"PHP14-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140356","properties":[{"key":"EntryName","value":"PPK N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNGPPERMIQPIDLGAPELYINRELAALEFNFRVLAQARDPDVPVLERLRYLTIVSNNLDEYFEVRVAVLKHKHALGAAIPGADGLSSTEILTCIRERALELFSELFAIWRNELLPALAEEDIRFLTRDDWSDKQRRWLQGYFQNEIMPVLSPLGLDPAHPFPRILNKTLNLAVVLKGRDAFGREGHMALVRAPRSLPRIIHLPAEVSGGEGDFVFLAEVLQAFADEIFPGFQVCAAYQFRVTRNSELTVEEADVENLARALSEELAGRGYARPVRLEVGEDCPRAITEMLIANFQLEETDVYRCEGPVNIIRAGVIYDQLDRPELKFPRFTPRLPPVFEKGTNEFDVLGTRDVLLHHPYESFVSVVELLRRASQDPGVLAIKQTLYRAGKDSPLVDILVEAARNGKDVTVVVELRARFDEEANIGLANRLQEAGVQVVYGVVGYKTHAKMLLIVRRENGGLRRYVHLSTGNYHQGNSRGYTDIGLMTADPEIGEDIHKVFQQLSGLGPMIQLKRLLHSPFTLYSSVMGKIERETEHARNGRPGRIVAKLNALNEAHVVEALYRASMAGVQIDLIIRGACTLRPGIPGISENIRVRSIVGRFLEHSRVYWFGNDGEPELYCASADWMERNLMRRIEIGVPILDPALAKRVYDETLDNYLRDNTQAWLLGSDGRYTRSHPAKGEAPHNAQQALLVAYSG","length":698,"molWeight":78473,"crc64":"37F9B15C9AE19537","md5":"0D544081139E5451FACC2AA785920D4C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PTM":1,"SIMILARITY":1},"countByFeatureType":{"Domain":4,"Active site":1,"Binding site":6},"uniParcId":"UPI002026BA3D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SWT5","uniProtkbId":"A0ABY4SWT5_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57183.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"value":"Amidophosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"value":"ATase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"value":"2.4.2.14"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"value":"Glutamine phosphoribosylpyrophosphate amidotransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"value":"GPATase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57183.1"}],"value":"purF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57183.1"}],"value":"IM816_11015"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"value":"Catalyzes the formation of phosphoribosylamine from phosphoribosylpyrophosphate (PRPP) and glutamine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-phospho-beta-D-ribosylamine + L-glutamate + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + L-glutamine + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14905"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:58681"}],"ecNumber":"2.4.2.14","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000485"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-2"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000485"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010138"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000485"}],"value":"In the C-terminal section; belongs to the purine/pyrimidine phosphoribosyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"Glutamine amidotransferase type-2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51278"}]},{"type":"Active site","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":2,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-1"}]},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-2"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":366,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-2"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-2"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-2"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000485-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01931"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"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_01931"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57183.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57183.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57183.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338116.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11015","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0004044","properties":[{"key":"GoTerm","value":"F:amidophosphoribosyltransferase 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:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009113","properties":[{"key":"GoTerm","value":"P:purine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00715","properties":[{"key":"EntryName","value":"GPATase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.20.10","properties":[{"key":"EntryName","value":"Glutamine Phosphoribosylpyrophosphate, subunit 1, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01931","properties":[{"key":"EntryName","value":"PurF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017932","properties":[{"key":"EntryName","value":"GATase_2_dom"}]},{"database":"InterPro","id":"IPR029055","properties":[{"key":"EntryName","value":"Ntn_hydrolases_N"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR005854","properties":[{"key":"EntryName","value":"PurF"}]},{"database":"InterPro","id":"IPR035584","properties":[{"key":"EntryName","value":"PurF_N"}]},{"database":"NCBIfam","id":"TIGR01134","properties":[{"key":"EntryName","value":"purF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11907","properties":[{"key":"EntryName","value":"AMIDOPHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13537","properties":[{"key":"EntryName","value":"GATase_7"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000485","properties":[{"key":"EntryName","value":"Amd_phspho_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56235","properties":[{"key":"EntryName","value":"N-terminal nucleophile aminohydrolases (Ntn hydrolases)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51278","properties":[{"key":"EntryName","value":"GATASE_TYPE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MCGIIGIVGTTEVASALYDGLTVLQHRGQDAAGIATVDGARLRLHKGNGLVRDVFNSAGVSKLRGRIGIGHCRYPTAGSEGTEEAQPFYVNSPYGIAFAHNGNLVNTEALRKAMFEDDRRHIDTDSDSEVLLNVLAHELQVDDRGDLTPEHVFKAISRVHGRARGGYACIALVLGYGLIAFRDPNGIRPLVLGERVTPEGREYAVASESVALDVLGFKRVRDIEPGEAVIITDGGELHAQRCAEGAVHAPCIFEYVYLARPDSMIEDVSVYKARLRMGEKLAEKILRERGPDHGIDAVIPIPDTSRTAASSLAQALGVPMREGLVKNRYIGRTFIMPGQGERVKSVRRKLNAIDLEFRKKNVLLVDDSIVRGTTSKQIIQMARDAGAKNVYFASAAPPVRFPNIYGIDMPAASELIAAGRTVEEVEKALGADWLIYQDLDDLIWAVADGNEDLTKFDTSCFSGEYVTGVEAAFLEQQEAMRSDAAKNERRSA","length":492,"molWeight":53577,"crc64":"5941DF9A957C11BF","md5":"FA74A414D03E5E11C038C625DD48FD75"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":3},"uniParcId":"UPI00202723AF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SWU6","uniProtkbId":"A0ABY4SWU6_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57194.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"L-threonine 3-dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"TDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"1.1.1.103"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57194.1"}],"value":"tdh"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57194.1"}],"value":"IM816_11075"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"Catalyzes the NAD(+)-dependent oxidation of L-threonine to 2-amino-3-ketobutyrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonine + NAD(+) = (2S)-2-amino-3-oxobutanoate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13161"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57926"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:78948"}],"ecNumber":"1.1.1.103","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"Amino-acid degradation; L-threonine degradation via oxydo-reductase pathway; glycine from L-threonine: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"value":"Belongs to the zinc-containing alcohol dehydrogenase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"Enoyl reductase (ER)","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00829"}]},{"type":"Active site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}]},{"type":"Active site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}]},{"type":"Binding site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"Important for catalytic activity for the proton relay mechanism but does not participate directly in the coordination of zinc atom","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00627"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57194.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57194.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57194.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_177257376.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11075","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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:0008743","properties":[{"key":"GoTerm","value":"F:L-threonine 3-dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006567","properties":[{"key":"GoTerm","value":"P:L-threonine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.90.180.10","properties":[{"key":"EntryName","value":"Medium-chain alcohol dehydrogenases, catalytic domain"},{"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_00627","properties":[{"key":"EntryName","value":"Thr_dehydrog"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013149","properties":[{"key":"EntryName","value":"ADH-like_C"}]},{"database":"InterPro","id":"IPR013154","properties":[{"key":"EntryName","value":"ADH-like_N"}]},{"database":"InterPro","id":"IPR002328","properties":[{"key":"EntryName","value":"ADH_Zn_CS"}]},{"database":"InterPro","id":"IPR020843","properties":[{"key":"EntryName","value":"ER"}]},{"database":"InterPro","id":"IPR011032","properties":[{"key":"EntryName","value":"GroES-like_sf"}]},{"database":"InterPro","id":"IPR004627","properties":[{"key":"EntryName","value":"L-Threonine_3-DHase"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR050129","properties":[{"key":"EntryName","value":"Zn_alcohol_dh"}]},{"database":"NCBIfam","id":"NF003808","properties":[{"key":"EntryName","value":"PRK05396.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00692","properties":[{"key":"EntryName","value":"tdh"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43401","properties":[{"key":"EntryName","value":"L-THREONINE 3-DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43401:SF2","properties":[{"key":"EntryName","value":"L-THREONINE 3-DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08240","properties":[{"key":"EntryName","value":"ADH_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00107","properties":[{"key":"EntryName","value":"ADH_zinc_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00829","properties":[{"key":"EntryName","value":"PKS_ER"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50129","properties":[{"key":"EntryName","value":"GroES-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00059","properties":[{"key":"EntryName","value":"ADH_ZINC"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQQTMKALVKRKPEQGIWMEEVPVPQVGPNEVLIKVEKTAICGTDLHIYKWDEWSQRTIKPGLTIGHEFVGRVADIGPGVTGYKIGDRVSAEGHIVCGHCRNCRAGRQHLCPNTIGIGVNRNGAFAEYMTMPASNLWPIPDQIPSELAAFFDPYGNAAHCALEFDLIGEDVLITGAGPIGIIAAGIAKHVGARNVVVTDVNDYRLKLAADMGATRVVNVANQSLKDVVKDLHIEGFDVGLEMSGNPRAFGDMLECMYHGGKIAMLGIMPRGAGIDWDKVIFKGLTLQGIYGRRMYETWYKMTQMVLTGFPLQKVLTHQIAIDDFQRGFDLMDAGQCGKVVCSWT","length":344,"molWeight":37745,"crc64":"C3A988DFB2CBCCFE","md5":"197BF48C16D0349C688CD6D93F71DD73"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":12,"Site":1},"uniParcId":"UPI000908BBD3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SWW7","uniProtkbId":"A0ABY4SWW7_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57203.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NADH-quinone oxidoreductase subunit H"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NADH dehydrogenase I subunit H"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH-1 subunit H"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57203.1"}],"value":"nuoH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57203.1"}],"value":"IM816_11125"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient. This subunit may bind ubiquinone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"value":"NDH-1 is composed of 14 different subunits. Subunits NuoA, H, J, K, L, M, N constitute the membrane sector of the complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"value":"Belongs to the complex I subunit 1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Transmembrane","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]},{"type":"Transmembrane","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000471"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57203.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01350"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57203.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57203.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57203.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338129.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11125","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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:0003954","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016655","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"HAMAP","id":"MF_01350","properties":[{"key":"EntryName","value":"NDH1_NuoH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001694","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_su1/FPO"}]},{"database":"InterPro","id":"IPR018086","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase_su1_CS"}]},{"database":"NCBIfam","id":"NF004741","properties":[{"key":"EntryName","value":"PRK06076.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11432","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE SUBUNIT 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11432:SF3","properties":[{"key":"EntryName","value":"NADH-UBIQUINONE OXIDOREDUCTASE CHAIN 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00146","properties":[{"key":"EntryName","value":"NADHdh"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00668","properties":[{"key":"EntryName","value":"COMPLEX1_ND1_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGQQLWDHLLMPVLFIVAIVLPLIIAVAMFVYWERKVIGWMHVRMGPNKIGPLGLLQAFADVVKLLLKEVILPTNANKFLYYLAPMLALVPALAAWAVVPFGPETVLANLNAGVLYLLAMTSMGVYGIILAGWSSNSRYAMLGAMRAAAQVISYELAMGMSIVCVLVLTGSLNLTAIVNAQSGNFFDWFWLPLLPVFVIYFVSGVAETNRAPFDVAEGESEIVAGFHVEYSGSAFAIFFLAEYANMILVSFLTSILFMGGWLSPFPESWGLIGHGGFHWLFIKAFLFAFLFLWFRASFPRYRYDQIMRLGWKVFIPITIVWVLVAGCMKYFGWVHIGTGA","length":340,"molWeight":37853,"crc64":"23CD089C39A6C619","md5":"6CEC1D785938379E95C28B264481A356"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Transmembrane":8},"uniParcId":"UPI002026DCC0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SWW8","uniProtkbId":"A0ABY4SWW8_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57209.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NADH-quinone oxidoreductase subunit B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"7.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NADH dehydrogenase I subunit B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH-1 subunit B"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"nuoB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57209.1"}],"value":"IM816_11155"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH-1 shuttles electrons from NADH, via FMN and iron-sulfur (Fe-S) centers, to quinones in the respiratory chain. The immediate electron acceptor for the enzyme in this species is believed to be ubiquinone. Couples the redox reaction to proton translocation (for every two electrons transferred, four hydrogen ions are translocated across the cytoplasmic membrane), and thus conserves the redox energy in a proton gradient"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + NADH + 5 H(+)(in) = a quinol + NAD(+) + 4 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57888"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Binds 1 [4Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"NDH-1 is composed of 14 different subunits. Subunits NuoB, C, D, E, F, and G constitute the peripheral sector of the complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009173"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004464"}],"value":"Belongs to the complex I 20 kDa subunit family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"NADH:ubiquinone oxidoreductase-like 20kDa subunit","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01058"}]},{"type":"Binding site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"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_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004464"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004464"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004464"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004464"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022719"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0874","category":"PTM","name":"Quinone"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0813","category":"Biological process","name":"Transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023075"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01356"}],"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57209.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57209.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57209.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_072321341.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11155","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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:0045271","properties":[{"key":"GoTerm","value":"C:respiratory chain complex I"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"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:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050136","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (quinone) (non-electrogenic) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008137","properties":[{"key":"GoTerm","value":"F:NADH dehydrogenase (ubiquinone) activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0048038","properties":[{"key":"GoTerm","value":"F:quinone binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009060","properties":[{"key":"GoTerm","value":"P:aerobic respiration"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0015990","properties":[{"key":"GoTerm","value":"P:electron transport coupled proton transport"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.40.50.12280:FF:000001","properties":[{"key":"EntryName","value":"NADH-quinone oxidoreductase subunit B 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12280","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01356","properties":[{"key":"EntryName","value":"NDH1_NuoB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006137","properties":[{"key":"EntryName","value":"NADH_UbQ_OxRdtase-like_20kDa"}]},{"database":"InterPro","id":"IPR006138","properties":[{"key":"EntryName","value":"NADH_UQ_OxRdtase_20Kd_su"}]},{"database":"NCBIfam","id":"TIGR01957","properties":[{"key":"EntryName","value":"nuoB_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF005012","properties":[{"key":"EntryName","value":"PRK06411.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11995","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11995:SF14","properties":[{"key":"EntryName","value":"NADH DEHYDROGENASE [UBIQUINONE] IRON-SULFUR PROTEIN 7, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01058","properties":[{"key":"EntryName","value":"Oxidored_q6"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56770","properties":[{"key":"EntryName","value":"HydA/Nqo6-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01150","properties":[{"key":"EntryName","value":"COMPLEX1_20K"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGVMTSIDRVMHNPEPLNLVDDILRPNGDAPVVNRGFGVTSIDALMNWARTGSMWPMTFGLACCAVEMMHAGAARLDLDRYGVIFRPSPRQSDVMIVAGTLVNKMAPALRKVYDQMPDPKWVISMGSCANGGGYYHYSYSVVRGCDRIVPVDIYVPGCPPTAEALIHGILQLQKKIRRTHTIAR","length":184,"molWeight":20275,"crc64":"08072BEBC44CA140","md5":"4A0E3B89B57493F4E6398537D51FCE4D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":4},"uniParcId":"UPI000908F734"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SX22","uniProtkbId":"A0ABY4SX22_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57258.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"2: Evidence at transcript level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001174"}],"value":"Lon protease"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001174"}],"value":"3.4.21.53"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"value":"ATP-dependent protease La"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57258.1"}],"value":"lon"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57258.1"}],"value":"IM816_11445"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"value":"ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short-lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins in presence of ATP.","ecNumber":"3.4.21.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001174"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001174"}],"value":"Homohexamer. Organized in a ring with a central cavity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001174"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"value":"By heat shock"}],"commentType":"INDUCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001174"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000591"}],"value":"Belongs to the peptidase S16 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Lon N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51787"}]},{"type":"Domain","location":{"start":{"value":618,"modifier":"EXACT"},"end":{"value":799,"modifier":"EXACT"}},"description":"Lon proteolytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51786"}]},{"type":"Region","location":{"start":{"value":806,"modifier":"EXACT"},"end":{"value":832,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":705,"modifier":"EXACT"},"end":{"value":705,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001174-1"}]},{"type":"Active site","location":{"start":{"value":748,"modifier":"EXACT"},"end":{"value":748,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001174-1"}]},{"type":"Binding site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001174-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023016"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01973"}],"id":"KW-0346","category":"Biological process","name":"Stress response"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57258.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57258.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57258.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338175.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11445","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO: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:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0034605","properties":[{"key":"GoTerm","value":"P:cellular response to heat"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19500","properties":[{"key":"EntryName","value":"RecA-like_Lon"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000010","properties":[{"key":"EntryName","value":"Lon protease"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.5270:FF:000002","properties":[{"key":"EntryName","value":"Lon protease homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000021","properties":[{"key":"EntryName","value":"Lon protease homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.5270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.1480","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.130.40","properties":[{"key":"EntryName","value":"LON domain-like"},{"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_01973","properties":[{"key":"EntryName","value":"lon_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR027543","properties":[{"key":"EntryName","value":"Lon_bac"}]},{"database":"InterPro","id":"IPR004815","properties":[{"key":"EntryName","value":"Lon_bac/euk-typ"}]},{"database":"InterPro","id":"IPR054594","properties":[{"key":"EntryName","value":"Lon_lid"}]},{"database":"InterPro","id":"IPR008269","properties":[{"key":"EntryName","value":"Lon_proteolytic"}]},{"database":"InterPro","id":"IPR027065","properties":[{"key":"EntryName","value":"Lon_Prtase"}]},{"database":"InterPro","id":"IPR003111","properties":[{"key":"EntryName","value":"Lon_prtase_N"}]},{"database":"InterPro","id":"IPR046336","properties":[{"key":"EntryName","value":"Lon_prtase_N_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008268","properties":[{"key":"EntryName","value":"Peptidase_S16_AS"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"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":"NCBIfam","id":"TIGR00763","properties":[{"key":"EntryName","value":"lon"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008053","properties":[{"key":"EntryName","value":"PRK10787.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10046","properties":[{"key":"EntryName","value":"ATP DEPENDENT LON PROTEASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05362","properties":[{"key":"EntryName","value":"Lon_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22667","properties":[{"key":"EntryName","value":"Lon_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02190","properties":[{"key":"EntryName","value":"LON_substr_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001174","properties":[{"key":"EntryName","value":"Lon_proteas"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00830","properties":[{"key":"EntryName","value":"ENDOLAPTASE"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00464","properties":[{"key":"EntryName","value":"LON"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51787","properties":[{"key":"EntryName","value":"LON_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51786","properties":[{"key":"EntryName","value":"LON_PROTEOLYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01046","properties":[{"key":"EntryName","value":"LON_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAKNRSQTPIGSELDLLPVLPLRDVVVYPHMVIPLFVGRDKSMRALERAMEGERQILLVAQKSPDIDDPTIADLHNVGTLAGVLQLLKLPDGTVKVLVEGQSRVQVDAFEDEAGMMSGRARVIEPIYSNNERELDVVSRSLVSLFEQLVKQSRKLPPEILATLSGIDDPSRLADSIAAHLSVRMADKQRVLETADVGQRLELLIGLVDGEMDLQQVEKRIRGRVKSQMEKSQREYYLNEQMKAIQKELGEGEEGANEIEELQKKIDAAGMPKAVLAKARQEFNKLKQMSPMSAEATVVRNYLDWVVGVPWKKRSKVRKDLALAQETLDADHFGLEKVKERILEYLAVQQRVNTMKGPILCLVGPPGVGKTSLGQSIAKATNRKFVRMSLGGVRDEAEIRGHRRTYIGSMPGRIVQNLNKVGTKNPLFVLDEIDKMSMDFRGDPSSALLEVLDPEQNNAFNDHYLEVDLDLSEVMWIATANSLNIPGPLLDRMEVIRIPGYTEDEKLNIAQKYLLPKQLKANGLKAEELAIAEDALRDIVRYYTRESGVRNLEREISKICRKVVKEIALGTVPAHAKAKVAKTARKGKALAPDHVRVDGSNLDHYLGVRRFDFGRAEQQNEVGLVTGLAWTQVGGDLLSIEASVVPGKGRLVHTGQLGDVMKESIQAALSVVRARAAGLGIEPDFHEKLDIHIHVPEGATPKDGPSAGIAMCTALVSALTKVPVRSEVAMTGEITLRGRVLPIGGLKEKLLAAHRGGITTVIIPEENRKDLVDLPENITSSLDIHAVKWIDEVLDLALERPLGPKAATDGGNVVEVPKGQGKRKGKASPSLTH","length":832,"molWeight":91470,"crc64":"F1D52D1B1C1C3636","md5":"74DC14501B3FF927915D0891012DD59B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"INDUCTION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Region":1,"Active site":2,"Binding site":1},"uniParcId":"UPI002025E3E6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SX44","uniProtkbId":"A0ABY4SX44_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57284.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"value":"DNA topoisomerase 4 subunit B"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"value":"5.6.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"value":"Topoisomerase IV subunit B"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57284.1"}],"value":"parE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57284.1"}],"value":"IM816_11605"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"value":"Topoisomerase IV is essential for chromosome segregation. It relaxes supercoiled DNA. Performs the decatenation events required during the replication of a circular DNA molecule"}],"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_00938"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"value":"Heterotetramer composed of ParC and ParE"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"value":"Belongs to the type II topoisomerase family. ParE type 1 subfamily"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":523,"modifier":"EXACT"}},"description":"Toprim","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50880"}]},{"type":"Binding site","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":5,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":332,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":441,"modifier":"EXACT"},"end":{"value":441,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]},{"type":"Site","location":{"start":{"value":444,"modifier":"EXACT"},"end":{"value":444,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00995"}]},{"type":"Site","location":{"start":{"value":495,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}]},{"type":"Site","location":{"start":{"value":613,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Interaction with DNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00938"}],"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_00938"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"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_00938"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"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_00938"}],"id":"KW-0799","category":"Molecular function","name":"Topoisomerase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57284.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57284.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57284.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_072321412.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11605","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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: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:0003918","properties":[{"key":"GoTerm","value":"F:DNA topoisomerase type II (double strand cut, ATP-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007059","properties":[{"key":"GoTerm","value":"P:chromosome segregation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006265","properties":[{"key":"GoTerm","value":"P:DNA topological change"},{"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":"3.30.565.10:FF:000002","properties":[{"key":"EntryName","value":"DNA gyrase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.670:FF:000003","properties":[{"key":"EntryName","value":"DNA topoisomerase 4 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_00938","properties":[{"key":"EntryName","value":"ParE_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002288","properties":[{"key":"EntryName","value":"DNA_gyrase_B_C"}]},{"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":"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":"IPR005737","properties":[{"key":"EntryName","value":"TopoIV_B_Gneg"}]},{"database":"InterPro","id":"IPR006171","properties":[{"key":"EntryName","value":"TOPRIM_dom"}]},{"database":"NCBIfam","id":"TIGR01055","properties":[{"key":"EntryName","value":"parE_Gneg"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866","properties":[{"key":"EntryName","value":"DNA GYRASE/TOPOISOMERASE SUBUNIT B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45866:SF4","properties":[{"key":"EntryName","value":"DNA TOPOISOMERASE 4 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":"PR01098","properties":[{"key":"EntryName","value":"TOPISMRASE4B"}]},{"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":"MNTRYNASDIEVLSGLDPVKRRPGMYTDTSRPNHLAQEVIDNSVDEALAGHAKTIEVTVFNDGSVEVSDDGRGMPVDIHPEEKVPGVELILTRLHAGGKFSNKNYAFSGGLHGVGVSVVNALSTRVDVTIRRDGQEYRMAFAHGDRASDLEVIGSVPKKKTGTTLRFWPDPKYFDTPKILVSKLKHLLRAKAVLCAGLTVRLTEEGGETSEWYYEDGLSDYLRGELQGAEALPSDLFVKHFARDTDALDVALAWLPEGELVQESYVNLIPTAQGGTHVNGLRSGLTNAIREFCDLRNLLPRGVKLAPEDVWERLAFVLSVKLQDAQFAGQTKERLSSRQAAGIVEGVVHDAFSLWLNQHVDLGEKIAQLAIERASARLKAAKQVVRKKITQGPALPGKLADCAATDLTRTELFLVEGDSAGGSAKQARDKDFQAILPLRGKILNTWEVESGAVLASQEVHDLAVAIGCDPGKDDLSGLRYGKVVILADADSDGLHIATLLSALFLRHFPSLVREGHVFVAMPPLFRVDVGKQVFYCLDEEEKRLMLEKVEREKMKGAVSVTRFKGLGEMNPAQLRESTIHPDTRRLVQLTVDTDDGTQKLMDMLLAKKRAGDRKQWLEDKGDLATLEV","length":628,"molWeight":68994,"crc64":"340DBC115B47CD53","md5":"F0E1BE02EED1B2AC31574D982AEEDE92"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Binding site":5,"Site":4},"uniParcId":"UPI000908EAB2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SX53","uniProtkbId":"A0ABY4SX53_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57288.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"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:0000256","source":"HAMAP-Rule","id":"MF_00473"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00796"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57288.1"}],"value":"pgi"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57288.1"}],"value":"IM816_11625"}]}],"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":"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":349,"modifier":"EXACT"},"end":{"value":349,"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":381,"modifier":"EXACT"},"end":{"value":381,"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":507,"modifier":"EXACT"},"end":{"value":507,"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":"HAMAP-Rule","id":"MF_00473"},{"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":"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":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57288.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57288.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57288.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338197.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11625","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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":"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":"PRK00179.1"},{"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":"MESKHVPLPSFEEHASRLAKTHLRDLVQDEARGERLRRRMGPILLDVSRQKLDVPALDAVGEYIESTGWKAARDAMFEGKHINTSEDRAVLHTALRGGASRHPAAPADVRKDVADALDKMEALVNAVHKGEGHSVGLIDGVTDVVNIGIGGSDLGPRLAVHALEQFHVKGITSHFLTNVDGQAATDLMKKLDPAHTLVILVSKSFNTQETLLNGGVFRNWILKANDGDEKKTARHFIAVSSNVEAVRKWGASQVLPMWDYVGGRFSLWSAVGASIAFSIGMQGFRELLAGAAEADDHFRTAAWQDNLPVLLAIAEVWNRNILGRNSRAVVPYVDSLADLPSYLQQLEMESLGKHVHPDDGSEVQQPTVPVVWGSIGTNAQHAYFQALHQGTDTVPLEFIGLVKPAHPLRENHDVLLSNLLAQAAALSLGKTFDEALAEAKTGTEAERRTLAAQRTFKGDRPSTVFMLDALTPHSLGALIALYEHKVFMLGHLWGINAFDQWGVELGKVIAKQIYPSLANDKSAGDLGQFDGATRGLIEAIRGRR","length":544,"molWeight":59272,"crc64":"624D6FF636AB2D95","md5":"C6D4E9C8AD48847841E6EA54BFCD41EB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI002026EC16"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SX86","uniProtkbId":"A0ABY4SX86_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57326.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00021726"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Phospholipase A1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013179"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"3.1.1.32"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013278"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"3.1.1.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Phosphatidylcholine 1-acylhydrolase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57326.1"}],"value":"IM816_11835"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Hydrolysis of phosphatidylcholine with phospholipase A2 (EC 3.1.1.4) and phospholipase A1 (EC 3.1.1.32) activities"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 1-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15801"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28868"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:58168"}],"ecNumber":"3.1.1.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001604"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphocholine + H2O = a 2-acyl-sn-glycero-3-phosphocholine + a fatty acid + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18689"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28868"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:57875"}],"ecNumber":"3.1.1.32","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000111"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Binds 1 Ca(2+) ion per monomer. In the dimeric form the Ca(2+) is bound by different amino acids with binding of each Ca(2+) shared with ligands coming from each monomer. The Ca(2+) ion may have a role in catalysis."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011702"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Homodimer; dimerization is reversible, and the dimeric form is the active one"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"One of the very few enzymes located there"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Cell outer membrane","id":"SL-0040"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010525"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"value":"Belongs to the phospholipase A1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}]},{"type":"Chain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"Phospholipase A1","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"featureId":"PRO_5044977751"},{"type":"Active site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-1"}]},{"type":"Active site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-1"}]},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"in dimeric form","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023237"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0998","category":"Cellular component","name":"Cell outer membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022963"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0442","category":"Biological process","name":"Lipid degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603187-2"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU366027"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022452"}],"id":"KW-1134","category":"Domain","name":"Transmembrane beta strand"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57326.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57326.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57326.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338231.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11835","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0009279","properties":[{"key":"GoTerm","value":"C:cell outer membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004623","properties":[{"key":"GoTerm","value":"F:A2-type glycerophospholipase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008970","properties":[{"key":"GoTerm","value":"F:glycerophospholipid phospholipase A1 activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0006629","properties":[{"key":"GoTerm","value":"P:lipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00541","properties":[{"key":"EntryName","value":"OMPLA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.230.10","properties":[{"key":"EntryName","value":"Phospholipase A1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003187","properties":[{"key":"EntryName","value":"PLipase_A1"}]},{"database":"InterPro","id":"IPR036541","properties":[{"key":"EntryName","value":"PLipase_A1_sf"}]},{"database":"PANTHER","id":"PTHR40457","properties":[{"key":"EntryName","value":"PHOSPHOLIPASE A1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR40457:SF1","properties":[{"key":"EntryName","value":"PHOSPHOLIPASE A1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02253","properties":[{"key":"EntryName","value":"PLA1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01486","properties":[{"key":"EntryName","value":"PHPHLIPASEA1"}]},{"database":"SUPFAM","id":"SSF56931","properties":[{"key":"EntryName","value":"Outer membrane phospholipase A (OMPLA)"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKSYRAPSVVALACLQAGAVYAQNPSPLDIRACAGIETDSQRLLCYDKAVGRDRLPQASKKQDPDANSVSVDLATRDSRDVARPLSLLDSRWELSPESKLGTFNLRGYKPTYALPVFATTKQNTTPHSPAPDHTVTTPQELDNVEAKFQISLKTKVAENLFGDNGDVWVGYTQSSRWQVYNKENSRPFRETNYEPEAMLVFNTHYEILGWTGRLAGIGINHQSNGRADPLSRSWNRVIADVGLEREGWTIMLRPWWRIPEGARDDDNPDIKDYMGRGEIQIVHEVGRQEFALTARHSFRGGDRSHGSLRGTWSFPLAGNLRGYLEVFNGYGESLIDYNHRASYLGLGVSLLDWY","length":354,"molWeight":39808,"crc64":"D58889CEF2FB6518","md5":"1AA63D57F5A9F7B45B517B83D609A48C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Active site":2,"Binding site":4},"uniParcId":"UPI0020273855"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SXA7","uniProtkbId":"A0ABY4SXA7_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57348.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"N-acetylornithine carbamoyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"2.1.3.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"N-acetyl-L-ornithine transcarbamylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"AOTCase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"Acetylornithine transcarbamylase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"argF'"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57348.1"}],"value":"IM816_11950"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"Catalyzes the transfer of the carbamoyl group from carbamoyl phosphate to the delta-amino group of N(2)-acetyl-L-ornithine to produce N(2)-acetyl-L-citrulline. This is a step in an alternative arginine biosynthesis pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-acetyl-L-ornithine + carbamoyl phosphate = N(2)-acetyl-L-citrulline + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18609"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57805"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58765"}],"ecNumber":"2.1.3.9","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"value":"Belongs to the aspartate/ornithine carbamoyltransferase superfamily. AOTCase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"Aspartate/ornithine carbamoyltransferase carbamoyl-P binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02729"}]},{"type":"Domain","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Aspartate/ornithine carbamoyltransferase Asp/Orn-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00185"}]},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57805"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"N(2)-acetyl-L-ornithine","id":"ChEBI:CHEBI:57805"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57805"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"N(2)-acetyl-L-ornithine","id":"ChEBI:CHEBI:57805"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57805"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"N(2)-acetyl-L-ornithine","id":"ChEBI:CHEBI:57805"}},{"type":"Binding site","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228","note":"ligand shared between two neighboring subunits"}},{"type":"Site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Key residue in conferring substrate specificity for N-acetyl-L-ornithine versus N-succinyl-L-ornithine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}]},{"type":"Modified residue","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":300,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02234"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"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_02234"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57348.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57348.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57348.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338253.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_11950","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","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:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043857","properties":[{"key":"GoTerm","value":"F:N-acetylornithine carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004585","properties":[{"key":"GoTerm","value":"F:ornithine carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_02234","properties":[{"key":"EntryName","value":"AOTCase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043695","properties":[{"key":"EntryName","value":"ArgF"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"NCBIfam","id":"NF003384","properties":[{"key":"EntryName","value":"PRK04523.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753:SF3","properties":[{"key":"EntryName","value":"ORNITHINE TRANSCARBAMYLASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00101","properties":[{"key":"EntryName","value":"ATCASE"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVRHFLSTQDYSRAEIDALLDQAAEFKRSPQGQQLAGKSIALLFFNSSMRTRTSFELGAFQLGGHAVVLSPGKDAWPIEFEVGAVMDGETEEHIAEVARVLSRYVDMIGVRAFPKFVDWSVDRQDKVLAAFAQYATVPVINLETITHPCQELAHALALKEHLGDLQNRKYVLTWTYHPKPLNTAVANSALLIATKMGMDVTLLCPTPEYVLDQRYMDFAEANARENGGSLRVSHDIESAYRDAHVVYAKSWGAIPYFGRWDEEKAIRDAHRHFIVDEAKMALTDHGLFSHCLPLRRNIKATDAVMDSPACIAIDEAENRLHVQKAVMASLISQSSGAPSGLGF","length":344,"molWeight":38231,"crc64":"30DE39F2D8CEBC91","md5":"8D9AED2981A1B0ED6CAF2735FB8DECC7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":2,"Binding site":9,"Site":1,"Modified residue":1},"uniParcId":"UPI002026F0B1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SXD3","uniProtkbId":"A0ABY4SXD3_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56930.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017632"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Nucleoside diphosphate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"NDK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"NDP kinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012966"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"2.7.4.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Nucleoside-2-P kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56930.1"}],"value":"ndk"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56930.1"}],"value":"IM816_09635"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Major role in the synthesis of nucleoside triphosphates other than ATP. The ATP gamma phosphate is transferred to the NDP beta phosphate via a ping-pong mechanism, using a phosphorylated active-site intermediate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-deoxyribonucleoside 5'-triphosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44640"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:61560"},{"database":"ChEBI","id":"CHEBI:73316"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.6","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-triphosphate + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18113"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57930"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.6","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008142"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004011"}],"value":"Belongs to the NDK family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"Nucleoside diphosphate kinase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00562"}]},{"type":"Active site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"Pros-phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00706"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00451"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"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_00451"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56930.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL56930.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL56930.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_072321050.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_09635","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004550","properties":[{"key":"GoTerm","value":"F:nucleoside diphosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006241","properties":[{"key":"GoTerm","value":"P:CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006183","properties":[{"key":"GoTerm","value":"P:GTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04413","properties":[{"key":"EntryName","value":"NDPk_I"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.141:FF:000001","properties":[{"key":"EntryName","value":"Nucleoside diphosphate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.141","properties":[{"key":"EntryName","value":"Nucleoside diphosphate kinase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00451","properties":[{"key":"EntryName","value":"NDP_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR034907","properties":[{"key":"EntryName","value":"NDK-like_dom"}]},{"database":"InterPro","id":"IPR036850","properties":[{"key":"EntryName","value":"NDK-like_dom_sf"}]},{"database":"InterPro","id":"IPR001564","properties":[{"key":"EntryName","value":"Nucleoside_diP_kinase"}]},{"database":"NCBIfam","id":"NF001908","properties":[{"key":"EntryName","value":"PRK00668.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46161","properties":[{"key":"EntryName","value":"NUCLEOSIDE DIPHOSPHATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46161:SF3","properties":[{"key":"EntryName","value":"NUCLEOSIDE DIPHOSPHATE KINASE DDB_G0292928-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00334","properties":[{"key":"EntryName","value":"NDK"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01243","properties":[{"key":"EntryName","value":"NUCDPKINASE"}]},{"database":"SMART","id":"SM00562","properties":[{"key":"EntryName","value":"NDK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54919","properties":[{"key":"EntryName","value":"Nucleoside diphosphate kinase, NDK"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51374","properties":[{"key":"EntryName","value":"NDPK_LIKE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALERTLSIIKPDAVKKNVIGQILARFEGAGLKVVAARMAQLSRAEAEGFYAVHKERPFFNALVEFMISGPVMIQVLEGEGAILKNRELMGATNPKEAAPGTIRADFAESIDANAVHGSDAAETAAVEIAYFFRTTEVVSH","length":141,"molWeight":15189,"crc64":"198A20A81DD806A6","md5":"B25D9E8472E7DDAD6C4988934C2A2264"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":6},"uniParcId":"UPI000908A2F2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SXH0","uniProtkbId":"A0ABY4SXH0_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57419.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Fused isobutyryl-CoA mutase"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Isobutyryl-CoA mutase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"ICM"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"5.4.99.13"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"P-loop GTPase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"3.6.5.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"G-protein chaperone"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"icmF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57419.1"}],"value":"IM816_12320"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Catalyzes the reversible interconversion of isobutyryl-CoA and n-butyryl-CoA, using radical chemistry. Also exhibits GTPase activity, associated with its G-protein domain (MeaI) that functions as a chaperone that assists cofactor delivery and proper holo-enzyme assembly"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylpropanoyl-CoA = butanoyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13141"},{"database":"ChEBI","id":"CHEBI:57338"},{"database":"ChEBI","id":"CHEBI:57371"}],"ecNumber":"5.4.99.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"adenosylcob(III)alamin","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001922"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18408"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Is composed of four functional domains: the N-terminal 5'-deoxyadenosylcobalamin binding region that is homologous to the small subunit of ICM (IcmB), a middle P-loop GTPase domain (MeaI) that likely acts as a chaperone for ICM, a structured linker region involved in dimer formation, and a C-terminal part that is homologous to the large substrate-binding subunit of ICM (IcmA)"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Belongs to the IcmF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"B12-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51332"}]},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18408"},{"database":"ChEBI","id":"CHEBI:27638"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"adenosylcob(III)alamin","id":"ChEBI:CHEBI:18408"},"ligandPart":{"name":"Co","id":"ChEBI:CHEBI:27638"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":259,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":635,"modifier":"EXACT"},"end":{"value":635,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":784,"modifier":"EXACT"},"end":{"value":784,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":828,"modifier":"EXACT"},"end":{"value":828,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":877,"modifier":"EXACT"},"end":{"value":877,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":912,"modifier":"EXACT"},"end":{"value":912,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":917,"modifier":"EXACT"},"end":{"value":917,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":1149,"modifier":"EXACT"},"end":{"value":1149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023186"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0143","category":"Molecular function","name":"Chaperone"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0846","category":"Ligand","name":"Cobalamin"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023285"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0170","category":"Ligand","name":"Cobalt"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02050"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57419.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57419.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57419.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338306.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_12320","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0031419","properties":[{"key":"GoTerm","value":"F:cobalamin binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0047727","properties":[{"key":"GoTerm","value":"F:isobutyryl-CoA mutase 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:0034784","properties":[{"key":"GoTerm","value":"F:pivalyl-CoA mutase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006637","properties":[{"key":"GoTerm","value":"P:acyl-CoA metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02071","properties":[{"key":"EntryName","value":"MM_CoA_mut_B12_BD"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.280","properties":[{"key":"EntryName","value":"Cobalamin-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.240","properties":[{"key":"EntryName","value":"Methylmalonyl-CoA mutase"},{"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_02050","properties":[{"key":"EntryName","value":"IcmF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016176","properties":[{"key":"EntryName","value":"Cbl-dep_enz_cat"}]},{"database":"InterPro","id":"IPR006158","properties":[{"key":"EntryName","value":"Cobalamin-bd"}]},{"database":"InterPro","id":"IPR036724","properties":[{"key":"EntryName","value":"Cobalamin-bd_sf"}]},{"database":"InterPro","id":"IPR052040","properties":[{"key":"EntryName","value":"GTPase/Isobutyryl-CoA_mutase"}]},{"database":"InterPro","id":"IPR033669","properties":[{"key":"EntryName","value":"IcmF"}]},{"database":"InterPro","id":"IPR006099","properties":[{"key":"EntryName","value":"MeMalonylCoA_mutase_a/b_cat"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"PANTHER","id":"PTHR43087:SF1","properties":[{"key":"EntryName","value":"LAO_AO TRANSPORT SYSTEM ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43087","properties":[{"key":"EntryName","value":"LYSINE/ARGININE/ORNITHINE TRANSPORT SYSTEM KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02310","properties":[{"key":"EntryName","value":"B12-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03308","properties":[{"key":"EntryName","value":"MeaB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01642","properties":[{"key":"EntryName","value":"MM_CoA_mutase"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52242","properties":[{"key":"EntryName","value":"Cobalamin (vitamin B12)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51703","properties":[{"key":"EntryName","value":"Cobalamin (vitamin B12)-dependent enzymes"},{"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":"PS51332","properties":[{"key":"EntryName","value":"B12_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSQPKHIPASSTDAEATPLRFVTAASLFDGHDAAINIMRRIIQSQGAEVIHLGHNRSVEDVVRAALQEDADAIALSSYQGGHVEYFKYMVDMLRERGASHVRVFGGGGGTITPEEIKELQAYGVERIYHPNDGMKLGLTEMIEDVMARTREAAGRRVTVAPPTASVEDEISIGAMLSAIEEDRLGDEELARLRKAWKLAGGKTPVLGLTGTGGAGKSSVVDELLLRFLQAFPQMRIAVLAVDPTRRRSGGALLGDRIRMNSLRSPRVYMRSMATRRQHAATSVVLHDCIDFLKSQAYDLVIVETAGIGQSDSEIVDLVDFPVYVMTSEYGAASQLEKIDMLDFAELVVLNKFDKRGAEDALRDVRKQWKRNRVAFQLADDAVPVYPTIASQFNDPGVTWMFANLCRLLRDKLALPESAWTPDVDTTLREPRATVLIPGQRVRYLAEIAEQGRGVNGAIAKQAEAASKAQHYYESLKDIGDEALPRALDLYDHGLLTVSGDRSLATLRQRYNEAVRELSSEAIGLLREWPARFESVTAEFNEYQVRDKVIRVENYRESLSHQKIPKVSPPKTKDWGDLLSFLMRENLPGHYPYTGGVFPYRRAGEDPTRMFAGEGTPERTNRRFHYLSLGGGAARLSTAFDSVTLYGEDPAPRPDIYGKIGNSGVSIATLDDMKKLYSGFDLSAPTTSVSMTINGPAPIILAMFMNTAIDQNVEKYLNEDASRWEAANKRIAELYPDGNRPRYHGELPKGNDGLGLGLLGVSGAEVVDAETYARIKAYTLATVRGTVQADILKEDQAQNTCIFSTEFALRMMGDIQQYFVDHKVRNFYSVSISGYHIAEAGANPISQLAFTLSNGFTIVEYYLARGMKIDDFAPNLSFFFSNGMDPEYTVIGRVARRIWARAMRERYGASARSQMLKYHIQTSGRSLHAQEIQFNDIRTTLQALYALFDNCNSLHTNAYDEAITTPTEESVRRAVAIQLIINRELGLNFNENPWQGSFVVDELTDLVEEAVYKEFEAISERGGVLGAMDTMYQRGKIQEESMYYEHLKHDGTLPLIGVNTFLPKDHGGEIATEIELIRSTEEEKGQQIDNVRLFGKARNSLAPESLKVLQKTARDRRNVFEQLMEAVQNNSLGQISHALYDVGGEYRRNM","length":1150,"molWeight":128101,"crc64":"7E523FEDA019D142","md5":"D07C05A01575574B2679E9353D50BB0A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":19},"uniParcId":"UPI002027332A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABY4SXL6","uniProtkbId":"A0ABY4SXL6_9GAMM","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Luteibacter flocculans","taxonId":2780091,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57468.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Gammaproteobacteria","Lysobacterales","Rhodanobacteraceae","Luteibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"NAD kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"2.7.1.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"ATP-dependent NAD kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"nadK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57468.1"}],"value":"IM816_12600"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"Involved in the regulation of the intracellular balance of NAD and NADP, and is a key enzyme in the biosynthesis of NADP. Catalyzes specifically the phosphorylation on 2'-hydroxyl of the adenosine moiety of NAD to yield NADP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NAD(+) + ATP = ADP + NADP(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18629"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047925"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}]},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"Belongs to the NAD kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}]},{"type":"Binding site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00361"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001056681"}],"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_00361"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-47LDKTRJ15RV8","citationType":"submission","authors":["Friedrich I.","Hertel R.","Daniel R."],"title":"Whole-genome sequence of Luteibacter sp. EIF3.","publicationDate":"OCT-2020","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57468.1"}],"value":"EIF3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"URL57468.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"CP063231","properties":[{"key":"ProteinId","value":"URL57468.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_250338350.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP063231.1"}]},{"database":"KEGG","id":"lfl:IM816_12600","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001056681","properties":[{"key":"Component","value":"Chromosome"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051287","properties":[{"key":"GoTerm","value":"F:NAD binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003951","properties":[{"key":"GoTerm","value":"F:NAD+ kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019674","properties":[{"key":"GoTerm","value":"P:NAD+ metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006741","properties":[{"key":"GoTerm","value":"P:NADP+ biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.10330","properties":[{"key":"EntryName","value":"Probable inorganic polyphosphate/atp-NAD kinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.200.30","properties":[{"key":"EntryName","value":"Probable inorganic polyphosphate/atp-NAD kinase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00361","properties":[{"key":"EntryName","value":"NAD_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017438","properties":[{"key":"EntryName","value":"ATP-NAD_kinase_N"}]},{"database":"InterPro","id":"IPR017437","properties":[{"key":"EntryName","value":"ATP-NAD_kinase_PpnK-typ_C"}]},{"database":"InterPro","id":"IPR016064","properties":[{"key":"EntryName","value":"NAD/diacylglycerol_kinase_sf"}]},{"database":"InterPro","id":"IPR002504","properties":[{"key":"EntryName","value":"NADK"}]},{"database":"NCBIfam","id":"NF003406","properties":[{"key":"EntryName","value":"PRK04761.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20275","properties":[{"key":"EntryName","value":"NAD KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20275:SF0","properties":[{"key":"EntryName","value":"NAD KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01513","properties":[{"key":"EntryName","value":"NAD_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20143","properties":[{"key":"EntryName","value":"NAD_kinase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF111331","properties":[{"key":"EntryName","value":"NAD kinase/diacylglycerol kinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRLAFVASETDVAQRARATLVKRYRGVGPGDADIIVSLGGDGFMLRTLHAHRTLGVPFYGMKLGRLGFLMNHHDVDHLPERIEKAHPAVLHPLEMHTTCCDGVEHRALAFNEVALLRQSNQAAHLRVSLNGEVKLDELVCDGILVSTPAGSTAYNLSAHGPILPLDANVLALTPISPFRPRRWRGAILPHATRVGFDTKDPNKRPISATADFHEVRDVRSVEVKQSRRHAVRLLFDPEHNLQQRILDEQFAP","length":252,"molWeight":28001,"crc64":"6637108DDE6F2753","md5":"538D1413107C9172C4AD21A4F5EE00DB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":1,"Binding site":6},"uniParcId":"UPI002026C5D2"}}]}