{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M0Q9","uniProtkbId":"A0A6I4M0Q9_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Lysine--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"6.1.1.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Lysyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"LysRS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"}],"value":"lysX"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"lysS"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"}],"value":"F8568_000270"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024681"}],"value":"Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-tRNA(Lys) + a 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10668"},{"database":"Rhea","id":"RHEA-COMP:9696"},{"database":"Rhea","id":"RHEA-COMP:9697"},{"database":"ChEBI","id":"CHEBI:64716"},{"database":"ChEBI","id":"CHEBI:75792"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78529"}],"ecNumber":"2.3.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047540"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Lys) + L-lysine + ATP = L-lysyl-tRNA(Lys) + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20792"},{"database":"Rhea","id":"RHEA-COMP:9696"},{"database":"Rhea","id":"RHEA-COMP:9697"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32551"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78529"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048573"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Binds 3 Mg(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Belongs to the class-II aminoacyl-tRNA synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009968"}],"value":"In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005270"}],"value":"In the N-terminal section; belongs to the LPG synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":764,"modifier":"EXACT"},"end":{"value":1081,"modifier":"EXACT"}},"description":"Aminoacyl-transfer RNA synthetases class-II family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50862"}]},{"type":"Binding site","location":{"start":{"value":994,"modifier":"EXACT"},"end":{"value":994,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":1001,"modifier":"EXACT"},"end":{"value":1001,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":1001,"modifier":"EXACT"},"end":{"value":1001,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023251"}],"id":"KW-0046","category":"Biological process","name":"Antibiotic resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98841.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000001","properties":[{"key":"ProteinId","value":"MVZ98841.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A6I4M0Q9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004824","properties":[{"key":"GoTerm","value":"F:lysine-tRNA ligase 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:0050071","properties":[{"key":"GoTerm","value":"F:phosphatidylglycerol lysyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006430","properties":[{"key":"GoTerm","value":"P:lysyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04322","properties":[{"key":"EntryName","value":"LysRS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00252","properties":[{"key":"EntryName","value":"Lys_tRNA_synth_class2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004364","properties":[{"key":"EntryName","value":"Aa-tRNA-synt_II"}]},{"database":"InterPro","id":"IPR006195","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR024320","properties":[{"key":"EntryName","value":"LPG_synthase_C"}]},{"database":"InterPro","id":"IPR002313","properties":[{"key":"EntryName","value":"Lys-tRNA-ligase_II"}]},{"database":"InterPro","id":"IPR044136","properties":[{"key":"EntryName","value":"Lys-tRNA-ligase_II_N"}]},{"database":"InterPro","id":"IPR018149","properties":[{"key":"EntryName","value":"Lys-tRNA-synth_II_C"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR004365","properties":[{"key":"EntryName","value":"NA-bd_OB_tRNA"}]},{"database":"InterPro","id":"IPR031553","properties":[{"key":"EntryName","value":"tRNA-synt_2_TM"}]},{"database":"NCBIfam","id":"TIGR00499","properties":[{"key":"EntryName","value":"lysS_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002821","properties":[{"key":"EntryName","value":"lysX"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001756","properties":[{"key":"EntryName","value":"PRK00484.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42918:SF15","properties":[{"key":"EntryName","value":"LYSINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42918","properties":[{"key":"EntryName","value":"LYSYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09924","properties":[{"key":"EntryName","value":"LPG_synthase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00152","properties":[{"key":"EntryName","value":"tRNA-synt_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16995","properties":[{"key":"EntryName","value":"tRNA-synt_2_TM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01336","properties":[{"key":"EntryName","value":"tRNA_anti-codon"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00982","properties":[{"key":"EntryName","value":"TRNASYNTHLYS"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50249","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50862","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_II"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLQAAPTIFFWYTRLSGILSLLAWVSYGLILEIADIWALRWIGYLGWFPSVPIGMLWILLSMGIRRRKKAAWRILVLIFCLPAAVGVSTVLTTLFDPSEPTSIGEFVTAGVYVAVLALLVSARGQFTTLPDRANRRLAAIVFTSLLVVTCGIGTFLVTLTDANAKGDFWTHPLYAISQTVLGPRVTGKPIDVSVPFWVDVILWVLGTGLMIATFWALFKPGRRDPVLSPPEELAARRLLAEYGEQDSLGYFALRRDKDVMVAPNGKAAIAYRVEGSVSLASGDPLGDPESWDQAIEAWLEECREHAWIPGAVSVGERGAHVYKRHGFDALELGDEAIVDLTEFNLDGREMRQVRQAVRRVERAGYTVRIRRHAQIPAWEMAKLIRSADAWRGEETERGFSMALGRLGDPTDGRCVMVEAFDAEGELRGLLSFVPWGRGGLSLDLMRRDRAAENGLNEYMVAKLAEKAAAVGAQHLSLNFAMLRSAFERGSQIGAGPVSRIYYRFLSFASKFWQLESLYLSNAKYLPHWRPRYICYTQGRHIIRLGLAYARAEGFLPNLNRPKLDRAAAIIPSPDLVEEIRRIEEAADAARAPHRRLSEQERVRHAKLDQIRAAGMEPYPLGFARGDFAADVRERFAGLAPDTRTGERVAIAGRVVLAREHGRLIFVTLRDETADLQVMLTSDALGAESLRQWKALVDLGDQVGVRGEVVTSRRGELSVLASCWQLTAKCLRPLPNKRTGLSDPEARVRQRYVDFIVNDEARRMLRMRGDAIAAVRDRLRAGGFLEVETPMLQPVHGGATARPFTTRINAYNMQLYLRIAPELYLKRLLVGGVGRVFELNRNFRNEGVSQKHNPEFTMLEAYEPYGDYDTMAELTRSIVVDAANAALGTTVVVRDGVEYDLAEPWHEITVYESLSKALGEEVTPDTPLPAVHAHAERIGLNFDPAWGQGKIVQELFEELVEEQLTAPTFVRDYPAETSPLTRPHRDDPRLAEKWDLIVFGLELGTAYSELIDPILQRQRLTEQSLQAAGGDPEAMELDEDFLRALEYAMPPAGGMGMGIDRLLITLTGRSIRETIPFPLVRPGY","length":1083,"molWeight":120869,"crc64":"66DB6A6982C19D39","md5":"23D5825507343E7BE2224E7369A5EA5B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Transmembrane":6,"Domain":1,"Binding site":3},"uniParcId":"UPI00124C50AF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M497","uniProtkbId":"A0A6I4M497_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99153.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00069359"}],"value":"Broad-specificity linear acyl-CoA dehydrogenase FadE5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012033"}],"value":"1.3.8.7"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"1.3.8.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077090"}],"value":"Long-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077336"}],"value":"Medium-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075470"}],"value":"Short-chain-acyl-CoA dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99153.1"}],"value":"F8568_001875"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054301"}],"value":"Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17721"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83721"},{"database":"ChEBI","id":"CHEBI:83727"}],"ecNumber":"1.3.8.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049247"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a medium-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14477"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83723"},{"database":"ChEBI","id":"CHEBI:83726"}],"ecNumber":"1.3.8.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047882"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050315"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050695"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"decanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48176"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:61406"},{"database":"ChEBI","id":"CHEBI:61430"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050703"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57330"},{"database":"ChEBI","id":"CHEBI:57375"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050336"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048375"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47240"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57394"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:71412"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050877"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43448"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57379"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:61526"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052387"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004872"}],"value":"Lipid metabolism; fatty acid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99153.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]},{"type":"Domain","location":{"start":{"value":473,"modifier":"EXACT"},"end":{"value":607,"modifier":"EXACT"}},"description":"Acetyl-CoA dehydrogenase-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12806"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99153.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99153.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000001","properties":[{"key":"ProteinId","value":"MVZ99153.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151590490.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000001.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M497","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004466","properties":[{"key":"GoTerm","value":"F:long-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070991","properties":[{"key":"GoTerm","value":"F:medium-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0016937","properties":[{"key":"GoTerm","value":"F:short-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"FunFam","id":"2.40.110.20:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase AidB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000016","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase FadE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR025878","properties":[{"key":"EntryName","value":"Acyl-CoA_dh-like_C_dom"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"InterPro","id":"IPR052166","properties":[{"key":"EntryName","value":"Diverse_Acyl-CoA_DH"}]},{"database":"PANTHER","id":"PTHR42803","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42803:SF1","properties":[{"key":"EntryName","value":"BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12806","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGHYKSNLRDLEFNLFEVFKRQDLLGSGPYADLDEDTVRSILDEVNRLAEGPLADSFEDADRNPPAFDPATGTVTMPESFKKSFKAWMDSEWYRLDLAPDFGGSGAPRSLTWAVAEQVLGANPAVYMFASGPGFAQILWHIGTPEQKRFAELALERQWGATMVLTEPDAGSDVGAGRTKAVQQPDGTWHIEGVKRFITSAEHDMAENIFHLVLARPEGAGPGTKGLSMFLVPKYLVDVETGELGERNGAYVTNVEKKMGLKVSTTCELTLGEKHPAVGYLVGGVHEGIKQMFLVIEYARMMVGTKAIATLSTGYLNALEYAKERVQGADMTQMTDKSAPRVTITHHPDVRRSLMTQKAYAEGMRALVQLTATYQDAVQIAEFEGRKDEQAEKVNDLLLPIVKGFGSERAYALLGAESLQTFGGSGFLQDYPVEQYIRDSKIDTLYEGTTAIQGQDLFFRKILRDNGEALKVLAGQIRAFAGSGAGNGRLKNERALLGKALEDVQGILNPMIGWALGSMENPKELYRVGLNTSRLLLALGDLIVAWLLCRQAEVALTALGGDGVSDSDQAFYTGKVAAAQFFCQTVLPRLASDRAVTEATTLDVMELPEEAF","length":611,"molWeight":66776,"crc64":"316820A3A9F0966A","md5":"9174501169BB4E954532601A0D379BC0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":9,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI00124E4153"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M5D1","uniProtkbId":"A0A6I4M5D1_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99356.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Asp/Glu-ADT subunit B"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"6.3.5.6"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"6.3.5.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Glutamyl-tRNA(Gln) amidotransferase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Glu-ADT subunit B"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99356.1"}],"value":"gatB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99356.1"}],"value":"F8568_002940"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Catalytic subunit of the Asp/Glu-tRNA(Asn/Gln) amidotransferase complex GatCAB. GatCAB allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the multi-step transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). This subunit specifically recognizes tRNA(Gln) and tRNA(Asn), and mediates the transamidation of misloaded Glu and Asp respectively by catalyzing formation of the activated gamma-phospho-intermediate and its subsequent aminolysis using ammonia produced by the gatA subunit. Recognizes the first base pair and the D-loop of its specific tRNA substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-phospho-L-aspartyl-tRNA(Asn) + NH4(+) = L-asparaginyl-tRNA(Asn) + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57920"},{"database":"Rhea","id":"RHEA-COMP:9674"},{"database":"Rhea","id":"RHEA-COMP:15033"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:78515"},{"database":"ChEBI","id":"CHEBI:142450"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-phospho-L-glutamyl-tRNA(Gln) + NH4(+) = L-glutaminyl-tRNA(Gln) + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57912"},{"database":"Rhea","id":"RHEA-COMP:9681"},{"database":"Rhea","id":"RHEA-COMP:15032"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:78521"},{"database":"ChEBI","id":"CHEBI:142449"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-tRNA(Asn) + ATP = 4-phospho-L-aspartyl-tRNA(Asn) + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57916"},{"database":"Rhea","id":"RHEA-COMP:9677"},{"database":"Rhea","id":"RHEA-COMP:15033"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:78516"},{"database":"ChEBI","id":"CHEBI:142450"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-tRNA(Asn) + L-glutamine + ATP + H2O = L-asparaginyl-tRNA(Asn) + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14513"},{"database":"Rhea","id":"RHEA-COMP:9674"},{"database":"Rhea","id":"RHEA-COMP:9677"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:78515"},{"database":"ChEBI","id":"CHEBI:78516"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097075"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamyl-tRNA(Gln) + ATP = 5-phospho-L-glutamyl-tRNA(Gln) + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57908"},{"database":"Rhea","id":"RHEA-COMP:9684"},{"database":"Rhea","id":"RHEA-COMP:15032"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:78520"},{"database":"ChEBI","id":"CHEBI:142449"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl-tRNA(Gln) + L-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17521"},{"database":"Rhea","id":"RHEA-COMP:9681"},{"database":"Rhea","id":"RHEA-COMP:9684"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:78520"},{"database":"ChEBI","id":"CHEBI:78521"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047407"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Binds 2 Mg(2+) ions, a primary Mg(2+) ion involved in positioning of the gamma-carbonyl group of the amino acid in Glu-tRNA(Gln), and a secondary transient Mg(2+) ion that participates in phosphoryl transfer by polarizing the gamma-phosphate group of ATP."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Component of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase complex composed of GatA, GatB and GatC"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"The C-terminal tail domain, an anti-parallel amphiphilic helix bundle, is involved in discriminating and binding specific tRNAs. Probably recognizes the tRNA(Gln)-specific D-loop structure"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"The N-terminal cradle domain recognizes the first base of the acceptor tRNA stem"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Belongs to the GatB/GatE family. GatB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99356.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"Asn/Gln amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00845"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"Cradle","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Region","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":431,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"Tail","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Compositional bias","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99356.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99356.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99356.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151591444.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M5D1","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050567","properties":[{"key":"GoTerm","value":"F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070681","properties":[{"key":"GoTerm","value":"P:glutaminyl-tRNAGln biosynthesis via transamidation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006412","properties":[{"key":"GoTerm","value":"P:translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.10.410:FF:000001","properties":[{"key":"EntryName","value":"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.410","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00121","properties":[{"key":"EntryName","value":"GatB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017959","properties":[{"key":"EntryName","value":"Asn/Gln-tRNA_amidoTrfase_suB/E"}]},{"database":"InterPro","id":"IPR006075","properties":[{"key":"EntryName","value":"Asn/Gln-tRNA_Trfase_suB/E_cat"}]},{"database":"InterPro","id":"IPR018027","properties":[{"key":"EntryName","value":"Asn/Gln_amidotransferase"}]},{"database":"InterPro","id":"IPR003789","properties":[{"key":"EntryName","value":"Asn/Gln_tRNA_amidoTrase-B-like"}]},{"database":"InterPro","id":"IPR004413","properties":[{"key":"EntryName","value":"GatB"}]},{"database":"InterPro","id":"IPR023168","properties":[{"key":"EntryName","value":"GatB_Yqey_C_2"}]},{"database":"InterPro","id":"IPR017958","properties":[{"key":"EntryName","value":"Gln-tRNA_amidoTrfase_suB_CS"}]},{"database":"InterPro","id":"IPR014746","properties":[{"key":"EntryName","value":"Gln_synth/guanido_kin_cat_dom"}]},{"database":"NCBIfam","id":"NF004012","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004013","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004014","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00133","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11659","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11659:SF0","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02934","properties":[{"key":"EntryName","value":"GatB_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02637","properties":[{"key":"EntryName","value":"GatB_Yqey"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00845","properties":[{"key":"EntryName","value":"GatB_Yqey"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF89095","properties":[{"key":"EntryName","value":"GatB/YqeY motif"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55931","properties":[{"key":"EntryName","value":"Glutamine synthetase/guanido kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01234","properties":[{"key":"EntryName","value":"GATB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPYDEALAKYEPVLGLETHIELGTASKMFCGCPTTFGADPNTQVCPVCLGLPGSLPVTNHAAIEGIIKIGLALNCTIVEWCRFARKNYFYPDMPKDFQISQYDEPLCVDGHLDVEVDGETYRIEIERVHMEEDTGKSLHVGGSTGRIHGADHSLVDYNRAGIPLVEIVTKPIAATGDKAPLVARAYATELRELVRSLGVSDVRMEEGSMRCDVNVSLMPRGASQWGTRTETKNVNSLRSVERAVRSEIERQAGVLDAGERVVQETRHFHEDTGRSTSGRSKEEAQDYRYFPEPDLVPMAPSREWVEELRASLPELPAARRRRVQAEWGLSDLELRDVVNAGAVDLIEATIAAGADAGAARKWWMNELSRRATEQNVELAELPITPEQVARIQAMVSAGELNDKLARQVFEGVLAGEGGPDEVVAARGLKVVSDEGELASIIDQVIADNAAVADKIRSGKVAAAGALVGAVMKATRGQADAGRARELILEKLAAS","length":494,"molWeight":53660,"crc64":"EB10B01E3A23C508","md5":"5D854726FF9DA1F03970F79811DE1E86"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Compositional bias":1,"Binding site":10},"uniParcId":"UPI00124F4980"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M6S0","uniProtkbId":"A0A6I4M6S0_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":26,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99460.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99460.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99460.1"}],"value":"F8568_003515"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99460.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"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":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":198,"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":231,"modifier":"EXACT"},"end":{"value":231,"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":254,"modifier":"EXACT"},"end":{"value":256,"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":330,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"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-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99460.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99460.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99460.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151591249.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M6S0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR006638","properties":[{"key":"EntryName","value":"Elp3/MiaA/NifB-like_rSAM"}]},{"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":"SMART","id":"SM00729","properties":[{"key":"EntryName","value":"Elp3"},{"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":"MSATTEPATAGAAPKKTPAKLVFAAPRRGKPPRHLADLTRAERREAVAELGEKPFRADQLSRHYFARLVDDPAKMTDLPAAVRERLVSELLPSLLTPVRELDCDGGRTLKTVWKAFDGVLFESVLMRYPDRATMCVSSQAGCGMNCPFCATGQAGLTRNLSTAEIVEQVAAGARAMARGRIPGGPGRVSNIVFMGMGEPLANYKAVIGAVHRITDPAPAGLGISQRSVTVSTVGLVPAIEKLAAEDMSVRLAVSLHAPDDELRDDLVPINNRWKVAEVLDAAWAYAERSGRRVSIEYALIKDVNDQAWRADLLGRLLRGHLVHVNLIPLNPTPGSKWTASRPEDEREFVRRLEAHGVPVTVRDTRGREIDGACGQLAAATKD","length":382,"molWeight":41354,"crc64":"48E9B876B4B84E4F","md5":"6508B189569F2DF47CCDA0F9F5745F86"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":2,"Binding site":7},"uniParcId":"UPI00124CAF5A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M8A2","uniProtkbId":"A0A6I4M8A2_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01240.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate--fructose 6-phosphate 1-phosphotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"2.7.1.90"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"6-phosphofructokinase, pyrophosphate dependent"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-dependent phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-PFK"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate-dependent 6-phosphofructose-1-kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"pfp"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01240.1"}],"value":"F8568_012775"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13613"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57634"}],"ecNumber":"2.7.1.90","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Non-allosteric"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01240.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33019"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"diphosphate","id":"ChEBI:CHEBI:33019"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Important for catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"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_01976"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01240.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01240.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000008","properties":[{"key":"ProteinId","value":"MWA01240.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151593738.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000008.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M8A2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0047334","properties":[{"key":"GoTerm","value":"F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01976","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR012829","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02483","properties":[{"key":"EntryName","value":"PFK_mixed"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF52","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVGVLTGGGDCPGLNAVIRAVVRKGVQVFGYEFVGFRAGWRGPLEGDTVALDVQAVRGILPRGGTILGSSRTNPVKVEGGVERIKDNLAGLGVDALIAIGGEDTLGVARELYANGVNVVGVPKTIDNDLNATDYTFGFDTAVNIGMEAVDRLHTTAESHHRALICEVMGRHAGWIALHVGMAAGANVILIPERPFDIDKVVEYVESRFKTRYAPIIVVSEGAHPMDGQMQLQTGERDAFGHVRLGGIGQALADEIEKRTGKEARATVLGHIQRGGTPTAFDRVLATRFGLQAIDAVRDGDYGKMVALQGTDIVRVGLDEATKELKTVPLERYAEAEVFFG","length":341,"molWeight":36412,"crc64":"E5127F4B876FBB1A","md5":"DF73896BF9FF7DCD17CCE632D348AD50"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":8,"Site":2},"uniParcId":"UPI00124D2A79"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MAK8","uniProtkbId":"A0A6I4MAK8_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01284.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"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":"MWA01284.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01284.1"}],"value":"F8568_012995"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Catalyzes two sequential steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine. In the second step the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Catalyzes two steps in the biosynthesis of coenzyme A. In the first step cysteine is conjugated to 4'-phosphopantothenate to form 4-phosphopantothenoylcysteine, in the latter compound is decarboxylated to form 4'-phosphopantotheine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(R)-4'-phosphopantothenate + L-cysteine + CTP = N-[(R)-4-phosphopantothenoyl]-L-cysteine + CMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19397"},{"database":"ChEBI","id":"CHEBI:10986"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"6.3.2.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-[(R)-4-phosphopantothenoyl]-L-cysteine + H(+) = (R)-4'-phosphopantetheine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16793"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:59458"},{"database":"ChEBI","id":"CHEBI:61723"}],"ecNumber":"4.1.1.36","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Binds 1 FMN per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 2/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"Cofactor biosynthesis; coenzyme A biosynthesis; CoA from (R)-pantothenate: step 3/5"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the C-terminal section; belongs to the PPC synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364078"}],"value":"In the N-terminal section; belongs to the HFCD (homo-oligomeric flavin containing Cys decarboxylase) superfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01284.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":398,"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":191,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"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":290,"modifier":"EXACT"},"end":{"value":290,"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":308,"modifier":"EXACT"},"end":{"value":311,"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":327,"modifier":"EXACT"},"end":{"value":327,"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"}},{"type":"Binding site","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":345,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}}],"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":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01284.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01284.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000008","properties":[{"key":"ProteinId","value":"MWA01284.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151593773.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000008.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MAK8","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0071513","properties":[{"key":"GoTerm","value":"C:phosphopantothenoylcysteine decarboxylase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004632","properties":[{"key":"GoTerm","value":"F:phosphopantothenate--cysteine ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004633","properties":[{"key":"GoTerm","value":"F:phosphopantothenoylcysteine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015937","properties":[{"key":"GoTerm","value":"P:coenzyme A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0015941","properties":[{"key":"GoTerm","value":"P:pantothenate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.10300","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1950","properties":[{"key":"EntryName","value":"Flavin prenyltransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02225","properties":[{"key":"EntryName","value":"CoaBC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR035929","properties":[{"key":"EntryName","value":"CoaB-like_sf"}]},{"database":"InterPro","id":"IPR005252","properties":[{"key":"EntryName","value":"CoaBC"}]},{"database":"InterPro","id":"IPR007085","properties":[{"key":"EntryName","value":"DNA/pantothenate-metab_flavo_C"}]},{"database":"InterPro","id":"IPR036551","properties":[{"key":"EntryName","value":"Flavin_trans-like"}]},{"database":"InterPro","id":"IPR003382","properties":[{"key":"EntryName","value":"Flavoprotein"}]},{"database":"NCBIfam","id":"TIGR00521","properties":[{"key":"EntryName","value":"coaBC_dfp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359","properties":[{"key":"EntryName","value":"HOMO-OLIGOMERIC FLAVIN CONTAINING CYS DECARBOXYLASE FAMILY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14359:SF6","properties":[{"key":"EntryName","value":"PHOSPHOPANTOTHENOYLCYSTEINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04127","properties":[{"key":"EntryName","value":"DFP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02441","properties":[{"key":"EntryName","value":"Flavoprotein"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102645","properties":[{"key":"EntryName","value":"CoaB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52507","properties":[{"key":"EntryName","value":"Homo-oligomeric flavin-containing Cys decarboxylases, HFCD"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSRKPRVVLGVSAGIAAYKVCELLRRLTESGHDVTVVPTRDALRFVGEPTWAALSGNPVSTEVWDGVARVPHVRLGQDADLVFVAPATADLLARAAHGLADDLLTNTLLTARCPVVFAPAMHTEMWEHPATRANVATLRARGAIVVEPASGRLTGKDTGPGRLPDPAELFEAARRVLDRGAVQPDLAGRHVVVSAGGTREPLDPVRFIGNRSSGLQGYALARTAAARGARVTLVAANVALPDPAGARVVPVGSAEEMRKAVLEAAGDADAVVMAAAVADFRPVDYRGSKIKKAEGAEPEPIRLAKNPDILAELGERRRAGQVIVGFAAETDDVLANGRAKLARKRSDLLVVNQVGEDLTFGRPDNAAVILGADGSSTEVERGAKEALADVVWDLVAARLDPLPAD","length":406,"molWeight":42621,"crc64":"A52763B372609308","md5":"C13C3BB39FE5303270AC531BB1E3F28D"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI00124DFD1F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MAL7","uniProtkbId":"A0A6I4MAL7_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03288.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Sulfate adenylyltransferase subunit 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"2.7.7.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"ATP-sulfurylase large subunit"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Sulfate adenylate transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"SAT"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenylyl-sulfate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"2.7.1.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"APS kinase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"ATP adenosine-5'-phosphosulfate 3'-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Adenosine-5'-phosphosulfate kinase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03288.1"}],"value":"cysN"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"cysC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03288.1"}],"value":"F8568_023495"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002357"}],"value":"APS kinase catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Catalyzes the synthesis of activated sulfate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"With CysD forms the ATP sulfurylase (ATPS) that catalyzes the adenylation of sulfate producing adenosine 5'-phosphosulfate (APS) and diphosphate, the first enzymatic step in sulfur assimilation pathway. APS synthesis involves the formation of a high-energy phosphoric-sulfuric acid anhydride bond driven by GTP hydrolysis by CysN coupled to ATP hydrolysis by CysD"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049370"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Heterodimer composed of CysD, the smaller subunit, and CysN"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"value":"Belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005438"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007237"}],"value":"In the N-terminal section; belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. CysN/NodQ subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03288.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"Tr-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51722"}]},{"type":"Region","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"G1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"G2","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"G3","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"G4","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"G5","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01059"}]},{"type":"Region","location":{"start":{"value":594,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":468,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00065"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00062"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03288.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03288.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000018","properties":[{"key":"ProteinId","value":"MWA03288.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151595825.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000018.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MAL7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00140","properties":[{"key":"RectionId","value":"UER00204"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04166","properties":[{"key":"EntryName","value":"CysN_ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03695","properties":[{"key":"EntryName","value":"CysN_NodQ_II"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04095","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000119","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase subunit 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00065","properties":[{"key":"EntryName","value":"Adenylyl_sulf_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00062","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_sub1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR041757","properties":[{"key":"EntryName","value":"CysN_GTP-bd"}]},{"database":"InterPro","id":"IPR044138","properties":[{"key":"EntryName","value":"CysN_II"}]},{"database":"InterPro","id":"IPR044139","properties":[{"key":"EntryName","value":"CysN_NoDQ_III"}]},{"database":"InterPro","id":"IPR031157","properties":[{"key":"EntryName","value":"G_TR_CS"}]},{"database":"InterPro","id":"IPR054696","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011779","properties":[{"key":"EntryName","value":"SO4_adenylTrfase_lsu"}]},{"database":"InterPro","id":"IPR000795","properties":[{"key":"EntryName","value":"T_Tr_GTP-bd_dom"}]},{"database":"InterPro","id":"IPR050100","properties":[{"key":"EntryName","value":"TRAFAC_GTPase_members"}]},{"database":"InterPro","id":"IPR009000","properties":[{"key":"EntryName","value":"Transl_B-barrel_sf"}]},{"database":"InterPro","id":"IPR009001","properties":[{"key":"EntryName","value":"Transl_elong_EF1A/Init_IF2_C"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003478","properties":[{"key":"EntryName","value":"cysN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02034","properties":[{"key":"EntryName","value":"CysN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003013","properties":[{"key":"EntryName","value":"PRK03846.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004035","properties":[{"key":"EntryName","value":"PRK05506.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23115","properties":[{"key":"EntryName","value":"TRANSLATION FACTOR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22594","properties":[{"key":"EntryName","value":"GTP-eEF1A_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00009","properties":[{"key":"EntryName","value":"GTP_EFTU"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00315","properties":[{"key":"EntryName","value":"ELONGATNFCT"}]},{"database":"SUPFAM","id":"SSF50465","properties":[{"key":"EntryName","value":"EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF50447","properties":[{"key":"EntryName","value":"Translation proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00301","properties":[{"key":"EntryName","value":"G_TR_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51722","properties":[{"key":"EntryName","value":"G_TR_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MARTGDDLVTLDIEEYLRRHERKSMLRFITCGSVDDGKSTLIGRLLYDSKLVFSDHLAELEKESKTVGTQGGDLDFALLVDGLAAEREQGITIDVAYRFFSTERRKFIVADTPGHEQYTRNMVTGASTADLAVILVDARKGMLTQTRRHSYLVSLLGIRHIVLAVNKLDLLDYSQRRFDEIAEEYRRFAETIGLDDVVCIPISALQGDNILRKSAKTPWYSGPTLVGHLETVGIADERDSGPFRLPVQWVNRPNLDFRGFSGQIAGGTVRPGDRVRVLPSGRESTVARIVTSDGDLDTAVADQSVTLVLTDDIDVSRGDVIAAADAAPGTADQFEAQLVWMSEERMLPGRAYLLKSATSTAIAQLAAPKYAVNVNTLDRTAARTLGLNEIGVVNLRLDRELPFDPYTENRDMGGFIIIDRFTQDTVAAGMLKFALRRAQNVHKQSLDIDRRARAGSKGQRPAVVWFTGLSGAGKSTIANLVEKRLHDQGFHTYLLDGDNVRHGLNADLGFTDADRVENIRRVVEVAWLLADAGLIVLASFIAPFRAERARARERIGAEEFFEVHVDAPLEVVEARDRKGLYAKARRGELANFTGIDSPYEPPDAPDVHLDAGGTHAPEELADQVIERLREAGVLQPAADV","length":640,"molWeight":70527,"crc64":"F34C4D1FC24F7C41","md5":"848D6343C5FCBCEC2D482C19D73D52BE"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":2,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":6,"Binding site":3},"uniParcId":"UPI00124EE8B9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MB90","uniProtkbId":"A0A6I4MB90_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01277.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"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":"MWA01277.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01277.1"}],"value":"F8568_012960"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01277.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1122,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5050900329"},{"type":"Domain","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":682,"modifier":"EXACT"},"end":{"value":873,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":955,"modifier":"EXACT"},"end":{"value":1104,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":955,"modifier":"EXACT"},"end":{"value":1122,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":1100,"modifier":"EXACT"},"end":{"value":1122,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"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":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":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"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":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"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":248,"modifier":"EXACT"},"end":{"value":248,"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":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"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":291,"modifier":"EXACT"},"end":{"value":291,"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":305,"modifier":"EXACT"},"end":{"value":305,"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":305,"modifier":"EXACT"},"end":{"value":305,"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":305,"modifier":"EXACT"},"end":{"value":305,"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":305,"modifier":"EXACT"},"end":{"value":305,"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":305,"modifier":"EXACT"},"end":{"value":305,"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":307,"modifier":"EXACT"},"end":{"value":307,"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":307,"modifier":"EXACT"},"end":{"value":307,"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":718,"modifier":"EXACT"},"end":{"value":718,"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":757,"modifier":"EXACT"},"end":{"value":757,"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":759,"modifier":"EXACT"},"end":{"value":759,"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":764,"modifier":"EXACT"},"end":{"value":764,"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":791,"modifier":"EXACT"},"end":{"value":791,"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":792,"modifier":"EXACT"},"end":{"value":792,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":832,"modifier":"EXACT"},"end":{"value":832,"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":844,"modifier":"EXACT"},"end":{"value":844,"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":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":"3"}},{"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":"3"}},{"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":"Binding site","location":{"start":{"value":846,"modifier":"EXACT"},"end":{"value":846,"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":846,"modifier":"EXACT"},"end":{"value":846,"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":"UP000462055"}],"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-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01277.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01277.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000008","properties":[{"key":"ProteinId","value":"MWA01277.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151593768.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000008.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MB90","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00171"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000014","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_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":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"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":"MPRRTDLKSVLVIGSGPIVIGQACEFDYSGTQACRVLKAEGLRVTLVNSNPATIMTDPEFADATYVEPITPEVVEKIIAKERPDALLPTLGGQTALNTAIALFESGVLARYGVELIGADVDAIQAGENREKFKEIVAKVAAEQGLNAASARSVICHTMDEVTAAAGELGYPLVVRPSFTMGGRGSGFAHDEDELRRIAGAGLDASPTGEVLLEESILGWKEYELEVMRDRADNVVIVCSIENLDPMGVHTGDSITVAPAMTLTDREYQNMRDVAIAVIREVGVDTGGCNIQFAVHPGTGRMIVIEMNPRVSRSSALASKATGFPIAKIAARLAIGYTLDEIPNDITRETPASFEPTLDYVVVKVPRFAFEKFPGADPTLTTHMKSVGEAMAIGRCFTEALQKALRSLESKGSSFGWSGAADDAALLESARRPHEGRLRDVQRALWAGASVQEVYEATGIDPWFLDQIAAINEIAEEIRTADDALTRDKLLRAKRHGFSDAQIGELRGLSEEVVRELRHALGVRPVYLTVDTCAAEFAAQTPYLYSAYDEETEVPPGEKPKVIILGSGPNRIGQGVEFDYSCVHASFALAAAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVVYAEQRSGEVAGVIVQLGGQTPLGLAQKLKDAGVPIVGTSPESIHLAEERGAFGRVLHRAGLLAPKHGTATSYEEALEIAAEIGYPVLVRPSYVLGGRGMEIVYDDTTLESYMARATEASPEHPVLVDRFLDEAIEIDVDALYDGEELYLGGVMEHIEEAGIHSGDSACALPPITLGHDDVRRIRESTEALAAGIGVRGLMNVQYALSAGVLYVLEANPRASRTVPFVSKATAVQLAKAAARVMMGATIAELRAEGLLPASGDGGTLPLDAPIAVKEAVLPFDRFRNERGQGVDTVLGPEMRSTGEVMGIDEVFGTAFAKSQQAAYGSLPTKGRAFVSVANRDKRHMVFPVKRLADLGFEILATEGTAEVLRRNGVRAKIVRKHSEGPGPDGEPTIVRRVLDGEVDLIVNTPFGSPGQSGPRLDGYEIRTAAVLRGVPCVTTVQGLAAAVQGIEAVAGGQVGVRSLQEHAERLSGAHGRAGAVTRAGDGTVAPG","length":1122,"molWeight":119665,"crc64":"7540CF927CB72916","md5":"6981635375FA2B3535BD55FD92A11CA4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Chain":1,"Domain":3,"Region":3,"Binding site":38,"Lipidation":2},"uniParcId":"UPI00124E3E8B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MES8","uniProtkbId":"A0A6I4MES8_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04193.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"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":"MWA04193.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04193.1"}],"value":"F8568_028200"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04193.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":138,"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":236,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":483,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":15,"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":26,"modifier":"EXACT"},"end":{"value":26,"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":79,"modifier":"EXACT"},"end":{"value":79,"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":84,"modifier":"EXACT"},"end":{"value":85,"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":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"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":234,"modifier":"EXACT"},"end":{"value":234,"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":339,"modifier":"EXACT"},"end":{"value":339,"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":357,"modifier":"EXACT"},"end":{"value":357,"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":372,"modifier":"EXACT"},"end":{"value":372,"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: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":386,"modifier":"EXACT"},"end":{"value":386,"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":392,"modifier":"EXACT"},"end":{"value":393,"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":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":446,"modifier":"EXACT"},"end":{"value":446,"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":"UP000462055"}],"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-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04193.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04193.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000025","properties":[{"key":"ProteinId","value":"MWA04193.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151596718.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000025.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MES8","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00113","properties":[{"key":"RectionId","value":"UER00532"}]},{"database":"UniPathway","id":"UPA00973","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010932","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSADSPAAVIVLAAGEGTRMKSRTLKVLHELGGRAMLGHVLAAARELGPRRIVAVVGHRREQAVAYLGEHAPDVEPVVQEVQGGTGHAVRMALEQTGSLDGTVVVTNGDHPLLRGETLAALVRTHETAGNAVTVLTTEMPDATGYGRMIRAADGSVEAIVEHKDATEAQRAVTEINVGMYAFDGTLLEDALKRVTTDNAGGEEYLTDVVAILRGDGHRAGAHLVADWAETQGVNDRVQLAQARRQLNDRILEAHMRAGVTIIDPASTWIDVDVTAEPDAVVHPGTQLHGRTHLEAGASVGPNCTLTDTRVGADASVVNAVCVEAEIGPEASVGPFAYLRPGTRLSRKGKIGTYVETKNAEIGEGTKVPHLTYVGDAEIGDHSNIGASSVFVNYDGVRKHRSVIGSHVKVGSDNMIVAPVTVGDGAYTAAGSVIIQDVPPGAMAVARARQRNVEGWVERKRPGTPAAEAAEAARRAAEGGDDPA","length":483,"molWeight":50597,"crc64":"3E2CC21BCE2B183C","md5":"7242BDD0904E086D50FADE2A02A6EBA0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":4,"Active site":1,"Binding site":19},"uniParcId":"UPI00124CD7CE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MGE7","uniProtkbId":"A0A6I4MGE7_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":27,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01296.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Riboflavin biosynthesis protein RibBA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"4.1.99.12"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase II"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"ribBA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01296.1"}],"value":"F8568_013055"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043932"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049295"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004853"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01296.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"DHBP synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":418,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"Proton acceptor; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":44,"modifier":"EXACT"},"end":{"value":44,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":272,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":369,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":180,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"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_01283"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022619"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01296.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA01296.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000008","properties":[{"key":"ProteinId","value":"MWA01296.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151593784.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000008.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MGE7","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00399"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01283","properties":[{"key":"EntryName","value":"RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"InterPro","id":"IPR016299","properties":[{"key":"EntryName","value":"Riboflavin_synth_RibBA"}]},{"database":"NCBIfam","id":"NF006803","properties":[{"key":"EntryName","value":"PRK09311.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGSDGFNGSDGPSGSGIFDPIEEAVADIAAGRAVVVVDDEDRENEGDVIFAASKATPELLTFTIRYTSGVICVPMEGADLDRLQIPLMTAQNSERMRTAYTVSVDARLGVSTGISAADRARTIRTLADSASEPRDLVRPGHIFPLRYREGGVLRRRGHTEAAVDLARMAGLAPAGVLAEVVNEDGTMARLPELQVFAKEHGLKLISIEQLAEHRRRTEAMVTRVVETRLPNRYGMWRAVGFSSEIDGGEHLALVLGEIGDGEDVLVRAHSECLTGDVLHSERCDCGTQLDAAMERIAAEGRGVVVYLRGHEGRGIGLLAKLRAYVLQDAGADTVDANLELGLPADAREYSNAAHMLRDLGVRSIRVLTNNPDKLKGLDGFGLDVRGRETMPVVVTEHNRRYLTVKRDRLGHEIEGLS","length":418,"molWeight":45252,"crc64":"DF6533810D05BFB9","md5":"59A54893921B7F6A4597DCEECE1AE9EB"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Active site":2,"Binding site":16,"Site":2},"uniParcId":"UPI00124D7D42"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MHT4","uniProtkbId":"A0A6I4MHT4_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2020-08-12","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03714.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"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":"MWA03714.1"}],"value":"F8568_025680"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025153"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADHX = (6S)-NADHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32215"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:64075"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000013"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADPHX = (6S)-NADPHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32227"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:64077"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000909"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADHX + ADP = AMP + phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32223"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32235"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009524"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the C-terminal section; belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006001"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the N-terminal section; belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03714.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":118,"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":122,"modifier":"EXACT"},"end":{"value":128,"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":151,"modifier":"EXACT"},"end":{"value":151,"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":154,"modifier":"EXACT"},"end":{"value":154,"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":248,"modifier":"EXACT"},"end":{"value":248,"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":312,"modifier":"EXACT"},"end":{"value":312,"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":361,"modifier":"EXACT"},"end":{"value":361,"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":398,"modifier":"EXACT"},"end":{"value":402,"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":427,"modifier":"EXACT"},"end":{"value":427,"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":428,"modifier":"EXACT"},"end":{"value":428,"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":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03714.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03714.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000021","properties":[{"key":"ProteinId","value":"MWA03714.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151596252.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000021.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MHT4","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRYAHEVGKVRAAEQALMARLPDGALMQRAAAGLASVCARVLPAVYGARVVLLVGGGDNGGDALYAGARLARRGARVRAVQAGSKIHEGGLAALRAAGGRLLGGDPADAVAGADLIVDGLTGIGGTGALRDPHARLAALASAATGTVVACDVPSGVDAGTGRVEGEAVHADITVTFGTHKPGLLIDPGAARCGVVELVDIGLGDDLPDPDVVAARPADVRPPEPGPESDKYRRGVVGILAGGDEYTGAAVLSTGGAVHGGAGMVRFASVAHPVELVRQRWPEVVTTVLEPGPHDPKVLERVGRVQAWVAGPGLGTGDAAESLLAAVLATDLPVLVDADGLTVLARRRGLLLRPAPTVLTPHAGELSRLLGVPREDIEARRLEHVRRAAAELSATVLLKGSTTLVAEQDRPVRVNPTGTPRLATAGTGDVLSGLIGALLAGGMPALDAAASGAYLHGLAARLASAPHPSVAEAPISAYDVITALPDAFRSL","length":490,"molWeight":49400,"crc64":"A43CA4BA2D13DD45","md5":"2CC272A2F2B4623D55300FAEE7B67B9B"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI00124C710A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MJ09","uniProtkbId":"A0A6I4MJ09_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03661.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"Acetyl-coenzyme A carboxylase carboxyl transferase subunit alpha"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"ACCase subunit alpha"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"Acetyl-CoA carboxylase carboxyltransferase subunit alpha"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"2.1.3.15"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Acetyl-coenzyme A carboxylase carboxyl transferase subunit beta"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"value":"ACCase subunit beta"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Acetyl-CoA carboxylase carboxyltransferase subunit beta"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03661.1"}],"value":"accD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"accA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03661.1"}],"value":"F8568_025415"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025280"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Component of the acetyl coenzyme A carboxylase (ACC) complex. Biotin carboxylase (BC) catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the transcarboxylase to acetyl-CoA to form malonyl-CoA"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"Component of the acetyl coenzyme A carboxylase (ACC) complex. First, biotin carboxylase catalyzes the carboxylation of biotin on its carrier protein (BCCP) and then the CO(2) group is transferred by the carboxyltransferase to acetyl-CoA to form malonyl-CoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-carboxybiotinyl-L-lysyl-[protein] + acetyl-CoA = N(6)-biotinyl-L-lysyl-[protein] + malonyl-CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54728"},{"database":"Rhea","id":"RHEA-COMP:10505"},{"database":"Rhea","id":"RHEA-COMP:10506"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:83144"},{"database":"ChEBI","id":"CHEBI:83145"}],"ecNumber":"2.1.3.15","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004956"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"Lipid metabolism; malonyl-CoA biosynthesis; malonyl-CoA from acetyl-CoA: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"Acetyl-CoA carboxylase is a heterohexamer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits each of ACCase subunit alpha (AccA) and ACCase subunit beta (AccD)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011664"}],"value":"Acetyl-CoA carboxylase is a heterotetramer composed of biotin carboxyl carrier protein (AccB), biotin carboxylase (AccC) and two subunits of ACCase subunit beta/alpha"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"value":"Belongs to the AccA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"value":"Belongs to the AccD/PCCB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006276"}],"value":"In the C-terminal section; belongs to the AccA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010284"}],"value":"In the N-terminal section; belongs to the AccD/PCCB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03661.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"CoA carboxyltransferase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50980"}]},{"type":"Domain","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":540,"modifier":"EXACT"}},"description":"CoA carboxyltransferase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50989"}]},{"type":"Zinc finger","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"C4-type","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}]},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03661.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00823"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"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_00823"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01395"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03661.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA03661.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000021","properties":[{"key":"ProteinId","value":"MWA03661.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151596203.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000021.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MJ09","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00655","properties":[{"key":"RectionId","value":"UER00711"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009317","properties":[{"key":"GoTerm","value":"C:acetyl-CoA carboxylase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003989","properties":[{"key":"GoTerm","value":"F:acetyl-CoA carboxylase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016743","properties":[{"key":"GoTerm","value":"F:carboxyl- or carbamoyltransferase 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:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:2001295","properties":[{"key":"GoTerm","value":"P:malonyl-CoA biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00823","properties":[{"key":"EntryName","value":"AcetylCoA_CT_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01395","properties":[{"key":"EntryName","value":"AcetylCoA_CT_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR034733","properties":[{"key":"EntryName","value":"AcCoA_carboxyl_beta"}]},{"database":"InterPro","id":"IPR001095","properties":[{"key":"EntryName","value":"Acetyl_CoA_COase_a_su"}]},{"database":"InterPro","id":"IPR000438","properties":[{"key":"EntryName","value":"Acetyl_CoA_COase_Trfase_b_su"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR011763","properties":[{"key":"EntryName","value":"COA_CT_C"}]},{"database":"InterPro","id":"IPR011762","properties":[{"key":"EntryName","value":"COA_CT_N"}]},{"database":"InterPro","id":"IPR041010","properties":[{"key":"EntryName","value":"Znf-ACC"}]},{"database":"NCBIfam","id":"NF041504","properties":[{"key":"EntryName","value":"AccA_sub"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00515","properties":[{"key":"EntryName","value":"accD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42853","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42853:SF3","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A CARBOXYLASE CARBOXYL TRANSFERASE SUBUNIT ALPHA, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03255","properties":[{"key":"EntryName","value":"ACCA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01039","properties":[{"key":"EntryName","value":"Carboxyl_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17848","properties":[{"key":"EntryName","value":"Zn_ribbon_ACC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01070","properties":[{"key":"EntryName","value":"ACCCTRFRASEB"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50989","properties":[{"key":"EntryName","value":"COA_CT_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50980","properties":[{"key":"EntryName","value":"COA_CT_NTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDTLTGGPPAAGAGSPAAGWRCCPGCRSVTYGRTLERNLRVCPECGRHQPLTAPERLAMLLDEGSVVTFEPELADTDPLGFTDTLPYGERRATARARTGLTEAVLCATGTLGGRPVVAAVMDFRFMGGSLGGGVGELITQAGELALRERRPLLIVSASGGARMQEGALSLMQMAKTSQMLGRLDEAGLLTVSLVTDPTFGGVAASFATLADVVVAEPGARLGFAGPRVIEQTIRRPLPTGFQTAEFLLERGLIDLICPRGELRATLARLVEMGRPSPEPVPRPGRAGAAALVTDPAELPERDPWETVRRARDLGRPSTLDYARLAFDDFLELHGDRLGKDCPAIVGGPALLGGTPVMLVGTQKGHTVGELTAREFGMASPAGYRKAARLMRLAGKLGLPVVTLIDTPGAHPGLEAEENGQAFAIAENLRLMAGLAVPSVAVVTGEGGSGGALALAVADRVLMHADAVYSVISPEGCAAILWNDAAAAPRAAAALGVDSARLLRLGVVDAVIPEPGPGAPDDALATAERLRDALLTVLADLTRTPAAERGARRYARFRAFGANPTEGGPAR","length":571,"molWeight":59303,"crc64":"C1E49AF952CDD042","md5":"CE6AE8E80A78E5501D23672D2DF83939"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":2,"Zinc finger":1,"Binding site":4},"uniParcId":"UPI00124E2E72"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MJ42","uniProtkbId":"A0A6I4MJ42_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA02629.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA02629.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA02629.1"}],"value":"F8568_020075"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA02629.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":134,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-100)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA02629.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA02629.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000015","properties":[{"key":"ProteinId","value":"MWA02629.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151595108.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000015.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MJ42","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF0","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSENTEAAAGQCPVAHQRAPHPTQGGGNRGWWPDRLNLKLLAKNPPMTNPLGEDFNYAEAFNSLDLDAVKQDIATVLTDSQDWWPADFGNYGPLIIRMAWHSAGTYRVSDGRGGAGAGQQRFAPLNSWPDNASLDKARRVLWPVKKKYGRKISWADLMILAGNVALETMGLKTFGFAGGREDAWEADEDVFWGPETAWLDDERYSGDRELEKPLAAVQMGLIYVNPEGPNGNPDPLAAARDIRETFKRMAMNDEETVALIAGGHTFGKTHGAAPADAIGPEPEGAPLEDQGLGWKSTHGTGKGRDSHTSGLEVTWTPTPTKWDNSFFEILFGYEWELDKSPSGANQWRPKNGAGANTVPDPEDGTLNRAPGMLTTDLSLRFDPIYEPISRRFKDNPQEFADAFARAWFKLTHRDMGPIQRYLGPEVPSETLVWQDPVPAVDHELVDAQDVAALKARLLDSGLSVSQLAATAWASAASFRGTDKRGGANGARIRLEPQRSWEVNNPAELATVLRTLEQVQQAFNAEQTGGKKISLADLIILGGCAAVEKAAKDAGHDIVVPFTPGRTDASQEQTDVESFEVMEPTHDGFRNYLAKGNILPGEFLLIDRANLLTLSAPEMTVLVGGLRVLGVNHGQSDLGVLTDRPGQLTNDFFVNLLDMGTVWKQTNEESEIYEGRDASGEVKWTGSRVDLVFGANSELRAVAEVYASDDAKEKFVQDFVAAWDKVMNLDRYDLR","length":734,"molWeight":80414,"crc64":"7BB2B1204513B70B","md5":"BBEA2E249721BC2230F497BDCB86E65C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI00124C199F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MK10","uniProtkbId":"A0A6I4MK10_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":22,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04494.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ATP-dependent zinc metalloprotease FtsH"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"3.4.24.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04494.1"}],"value":"hflB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"ftsH"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04494.1"}],"value":"F8568_029775"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Multi-pass membrane protein","id":"SL-9909"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003651"}],"value":"Belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010044"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the C-terminal section; belongs to the peptidase M41 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"value":"In the central section; belongs to the AAA ATPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04494.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Transmembrane","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Domain","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":632,"modifier":"EXACT"},"end":{"value":659,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}]},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":501,"modifier":"EXACT"},"end":{"value":501,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":573,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01458"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04494.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04494.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000027","properties":[{"key":"ProteinId","value":"MWA04494.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A6I4MK10","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004222","properties":[{"key":"GoTerm","value":"F:metalloendopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030163","properties":[{"key":"GoTerm","value":"P:protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19501","properties":[{"key":"EntryName","value":"RecA-like_FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.760:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent zinc metalloprotease FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.720.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.760","properties":[{"key":"EntryName","value":"Peptidase M41"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01458","properties":[{"key":"EntryName","value":"FtsH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR041569","properties":[{"key":"EntryName","value":"AAA_lid_3"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR003960","properties":[{"key":"EntryName","value":"ATPase_AAA_CS"}]},{"database":"InterPro","id":"IPR005936","properties":[{"key":"EntryName","value":"FtsH"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011546","properties":[{"key":"EntryName","value":"Pept_M41_FtsH_extracell"}]},{"database":"InterPro","id":"IPR000642","properties":[{"key":"EntryName","value":"Peptidase_M41"}]},{"database":"InterPro","id":"IPR037219","properties":[{"key":"EntryName","value":"Peptidase_M41-like"}]},{"database":"NCBIfam","id":"TIGR01241","properties":[{"key":"EntryName","value":"FtsH_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076:SF97","properties":[{"key":"EntryName","value":"ATP-DEPENDENT ZINC METALLOPROTEASE YME1L1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23076","properties":[{"key":"EntryName","value":"METALLOPROTEASE M41 FTSH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17862","properties":[{"key":"EntryName","value":"AAA_lid_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06480","properties":[{"key":"EntryName","value":"FtsH_ext"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01434","properties":[{"key":"EntryName","value":"Peptidase_M41"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140990","properties":[{"key":"EntryName","value":"FtsH protease domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00674","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPDVPSKRPAPQPSEAAAQRAGSTERDRRESVPPRNDPERPWRAEGVPERPKRAGGGFGGWRPRRNTSLFWLLLLVVFGLSYVSMHYTGQQDKVSVPYTAFTQQVQAGNVKDVYTKGYQIQGKLKSAQQVPGQKDPKKTYTAFETLRPAFADDKIYTEMVSKGVEVEAKPVNEDRGLLANLALSLLPTLLFVGLWIGVMVWLQRRMTGGGGGGLMGGFGRSPKPVAPDEKRATFADVAGIDEVEAELSEVVDFLKDPGKYRRMGARVPRGVLLTGAPGTGKTLLARAVAGEANVPFYSAAASEFIEMVVGVGAARVRELFTEARKTAPSIIFIDEIDTIGRARGSGASLGGHDEREQTLNQILTEMDGFSGSEGVVVIAATNRPDILDPALMRPGRFDRQVAVSPPDLDGRVAILRVHTREVPLGGDADIVSVAKMTPGMTGAELANLVNEAALLAVKRDKGAVDMDDFQTALEKVQLGTRRALVMPYEERRRTSYHESGHGLLGMLQPGADPVRKITIVPHGRALGVTVSTPDSDRYAYDERYLRGRIIGALGGMAAEELVFGVITTGSESDLEQVTKIARGMVGRWGMSPKVGPLSILPSDGMEPMGQYAAQGTLDAVDLEARRIVDECYAEALETLRAHRDQLDSLAAALLEAETLDEEAAYSAAGITRSITEVDLSKTPTRG","length":686,"molWeight":74031,"crc64":"A8277DA752146D64","md5":"A555B145C70148EDD64D8FD2E0E20DB8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Transmembrane":2,"Domain":1,"Region":1,"Coiled coil":1,"Compositional bias":1,"Active site":1,"Binding site":4},"uniParcId":"UPI00124C6166"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MM72","uniProtkbId":"A0A6I4MM72_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":26,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA05057.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"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":"MWA05057.1"}],"value":"F8568_032780"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA05057.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":542,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":392,"modifier":"EXACT"},"end":{"value":392,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":524,"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":526,"modifier":"EXACT"},"end":{"value":526,"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":23,"modifier":"EXACT"},"end":{"value":23,"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":23,"modifier":"EXACT"},"end":{"value":23,"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":24,"modifier":"EXACT"},"end":{"value":29,"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":81,"modifier":"EXACT"},"end":{"value":81,"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":81,"modifier":"EXACT"},"end":{"value":81,"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":151,"modifier":"EXACT"},"end":{"value":151,"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":158,"modifier":"EXACT"},"end":{"value":160,"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":198,"modifier":"EXACT"},"end":{"value":203,"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":198,"modifier":"EXACT"},"end":{"value":203,"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":234,"modifier":"EXACT"},"end":{"value":234,"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":234,"modifier":"EXACT"},"end":{"value":234,"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":252,"modifier":"EXACT"},"end":{"value":252,"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":365,"modifier":"EXACT"},"end":{"value":365,"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":393,"modifier":"EXACT"},"end":{"value":396,"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":416,"modifier":"EXACT"},"end":{"value":416,"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":477,"modifier":"EXACT"},"end":{"value":477,"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":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA05057.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA05057.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000033","properties":[{"key":"ProteinId","value":"MWA05057.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151597555.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000033.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MM72","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPSAATGRSRPTKHLFVTGGVASSLGKGLTASSLGRLLTLRGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTDDGAETDLDIGHYERFLDTELHGSANVTTGQVYSNVIAKERRGEYLGDTVQVIPHITNEIKDRIRGMADDTEVDIVITEVGGTVGDIESLPFLESVRQIRHEIGRDNCFFLHVSLLPYIGPSGELKTKPTQHSVAALRSIGIQPDAIVCRSDRPITDGLKHKISLMCDVDREAVVSAVDAASIYDIPKVLHAEGLDAYVVRRLGLPFRDVDWGAWDRLLRRVHKPAREVTIALVGKYIDLPDAYLSVTEALRHGGFGNDAKVHIRWVKSDDCATPEGAERELDGVDGVLIPGGFGVRGIEGKLGAIRHAREHRVPLLGICLGLQCMVIEAARDLGGLAGAGSAEFDAATAHPVVATMADQVDVVAGERDMGGTMRLGLYPADLADGSVVRELYGEAKVSERHRHRYEVNNAYRGRLEEAGLRFSGLSPDGRLVEYVELPRETHPFFVGTQAHPEFRSRPTRPHPLFTGLVAAAIEYAGARAADASDAS","length":560,"molWeight":60786,"crc64":"375DC846F0926E93","md5":"D4D6BC534B4E3870CF6A059FA1D4339C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":16},"uniParcId":"UPI00124D04A1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MNI1","uniProtkbId":"A0A6I4MNI1_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04339.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"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":"MWA04339.1"}],"value":"F8568_028965"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04339.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":345,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":40,"modifier":"EXACT"},"end":{"value":40,"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":123,"modifier":"EXACT"},"end":{"value":129,"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":165,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"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":200,"modifier":"EXACT"},"end":{"value":200,"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":394,"modifier":"EXACT"},"end":{"value":394,"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":418,"modifier":"EXACT"},"end":{"value":421,"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":474,"modifier":"EXACT"},"end":{"value":474,"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":478,"modifier":"EXACT"},"end":{"value":478,"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":232,"modifier":"EXACT"},"end":{"value":232,"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":"MWA04339.1"}],"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":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04339.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA04339.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000026","properties":[{"key":"ProteinId","value":"MWA04339.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151596856.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000026.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4MNI1","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRPTTAQARPLDGLAATLGIGRGDRDDRGGAQVTGITHDSRAVRPGDVYAALPGTRTHGAEFCAQAAAAGAVAILTDAAGRGRAAATGLPVLVVADVRARLGEAAAWVYGEPGRDITLIGITGTSGKSTTAFLVEAGLRAAGITTGLVGGVEIRVADERVPSALTTPEATDLHALLAMMRERGVGAAAMEVSSHALVQGRVGGAHYDVAVFTNLSQDHLDYHPTMQDYFLAKARLFTPEYARVGVVNLDDHYGRELLGLARIPMTTFSASGDPAADWRAEDVRVGADGSVFRVVGPGGVEADASVRLAGPFNVANALAAIVALVEAGLRLDAAVHGVASLAGVPGRLERVDEGQDFVALVDYSHKPGAVEAVLTALRPVTEGTLAVVLGCGGDRDRGKRPLMGEAAARLADMAYFTNDNPRSEDPLAILAAMVEGGLKVPQRHRAHIVVEPDRAAAIALAVGRARRGDVLVVAGKGHEQGQYAAGEVQPFDDREVVREALRRAAPREAK","length":509,"molWeight":52874,"crc64":"7D1FADEAB6414566","md5":"B39C1C0BA12307A018B73351758341DB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI00124BFB4A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4MVS6","uniProtkbId":"A0A6I4MVS6_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA06436.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase subunit PdxT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"4.3.3.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pdx2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase glutaminase subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"3.5.1.2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA06436.1"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA06436.1"}],"value":"F8568_040045"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054599"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31507"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"4.3.3.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047992"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Belongs to the glutaminase PdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"value":"Belongs to the glutamine amidotransferase pdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA06436.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA06436.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MWA06436.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000051","properties":[{"key":"ProteinId","value":"MWA06436.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A6I4MVS6","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00245","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTVPPIRAIPERFSHVTSAVPTIGVLALQGDVREHARALEQAGARTLNVRRAEELDQVDGLVLPGGESTTMWRLARAFELLEPLRKRIEAGLPAYGSCAGMIMLADRIRDGVAGQETVGGIDMTVRRNAFGRQVDSFESNVPLTGMGDTPYHAVFIRAPWVESVGDAVEVLGRAESGPNAGRIVAVRQGRLMATSFHPELTGDFRVHHYFADLVRRAMRKED","length":223,"molWeight":24384,"crc64":"3B9CEE0D6150A2D2","md5":"B8E7FD6E08EDDEA3103563361AD553D5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI00124DDD48"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4LZN4","uniProtkbId":"A0A6I4LZN4_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":20,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98922.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"N-acetylmuramic acid 6-phosphate etherase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"MurNAc-6-P etherase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"4.2.1.126"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"N-acetylmuramic acid 6-phosphate hydrolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"N-acetylmuramic acid 6-phosphate lyase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"murQ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98922.1"}],"value":"F8568_000685"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Specifically catalyzes the cleavage of the D-lactyl ether substituent of MurNAc 6-phosphate, producing GlcNAc 6-phosphate and D-lactate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-D-muramate 6-phosphate + H2O = N-acetyl-D-glucosamine 6-phosphate + (R)-lactate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26410"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16004"},{"database":"ChEBI","id":"CHEBI:57513"},{"database":"ChEBI","id":"CHEBI:58722"}],"ecNumber":"4.2.1.126","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Amino-sugar metabolism; N-acetylmuramate degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"A lyase-type mechanism (elimination/hydration) is suggested for the cleavage of the lactyl ether bond of MurNAc 6-phosphate, with the formation of an alpha,beta-unsaturated aldehyde intermediate with (E)-stereochemistry, followed by the syn addition of water to give product"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"value":"Belongs to the GCKR-like family. MurNAc-6-P etherase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98922.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"SIS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51464"}]},{"type":"Active site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}]},{"type":"Active site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00068"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98922.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ98922.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000001","properties":[{"key":"ProteinId","value":"MVZ98922.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151590081.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000001.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4LZN4","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00342","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097367","properties":[{"key":"GoTerm","value":"F:carbohydrate derivative binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016835","properties":[{"key":"GoTerm","value":"F:carbon-oxygen lyase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016803","properties":[{"key":"GoTerm","value":"F:ether hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046348","properties":[{"key":"GoTerm","value":"P:amino sugar catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097173","properties":[{"key":"GoTerm","value":"P:N-acetylmuramic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0009254","properties":[{"key":"GoTerm","value":"P:peptidoglycan turnover"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd05007","properties":[{"key":"EntryName","value":"SIS_Etherase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.1080","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":"1"}]},{"database":"HAMAP","id":"MF_00068","properties":[{"key":"EntryName","value":"MurQ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005488","properties":[{"key":"EntryName","value":"Etherase_MurQ"}]},{"database":"InterPro","id":"IPR005486","properties":[{"key":"EntryName","value":"Glucokinase_regulatory_CS"}]},{"database":"InterPro","id":"IPR040190","properties":[{"key":"EntryName","value":"MURQ/GCKR"}]},{"database":"InterPro","id":"IPR001347","properties":[{"key":"EntryName","value":"SIS_dom"}]},{"database":"InterPro","id":"IPR046348","properties":[{"key":"EntryName","value":"SIS_dom_sf"}]},{"database":"NCBIfam","id":"NF003915","properties":[{"key":"EntryName","value":"PRK05441.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009222","properties":[{"key":"EntryName","value":"PRK12570.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10088","properties":[{"key":"EntryName","value":"GLUCOKINASE REGULATORY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10088:SF4","properties":[{"key":"EntryName","value":"GLUCOKINASE REGULATORY PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22645","properties":[{"key":"EntryName","value":"GKRP_SIS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53697","properties":[{"key":"EntryName","value":"SIS domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01272","properties":[{"key":"EntryName","value":"GCKR"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51464","properties":[{"key":"EntryName","value":"SIS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIDCELPTEGRNPRTLDVDTLPTLEVLHLINTEDATVPMVVAGVLPEVARLVDLAVDSLRAGGRVHYFGAGTSGRLAVIDAAELPPTFGIWGRVVAHHAGGPGALSQAISDVEDDMELGMRDAREVQPGDIAIGIAASGRTPYVIGALRAATAGGARTALISCNPRTPYGEEVEVHIGLATGPEVISGSTRMKAGTATKLVLNSFSTTLMIRMGRTYSNLMVSVNALNSKLRARLVRILTEATGMDARTCENALTEAGGNTRVALVSLLGEVPAARATVVLEETDGGVREALQRLRSA","length":298,"molWeight":31213,"crc64":"EF990C65572DF059","md5":"EAD0583AAD631F06C4EE3ECBF8693995"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2},"uniParcId":"UPI00124EEBF8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M028","uniProtkbId":"A0A6I4M028_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99237.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"value":"Mycothiol S-conjugate amidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"value":"3.5.1.115"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99237.1"}],"value":"mca"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99237.1"}],"value":"F8568_002305"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"value":"A mycothiol (MSH, N-acetylcysteinyl-glucosaminyl-inositol) S-conjugate amidase, it recycles conjugated MSH to the N-acetyl cysteine conjugate (AcCys S-conjugate, a mercapturic acid) and the MSH precursor. Involved in MSH-dependent detoxification of a number of alkylating agents and antibiotics"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"mycothiol S-conjugate + H2O = an N-acetyl-L-cysteine-S-conjugate + 1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36543"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58718"},{"database":"ChEBI","id":"CHEBI:58886"},{"database":"ChEBI","id":"CHEBI:59633"}],"ecNumber":"3.5.1.115","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29033"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"value":"Belongs to the MshB deacetylase family. Mca subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99237.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"id":"KW-0216","category":"Biological process","name":"Detoxification"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01482"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99237.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99237.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99237.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A6I4M028","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016811","properties":[{"key":"GoTerm","value":"F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010126","properties":[{"key":"GoTerm","value":"P:mycothiol metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010127","properties":[{"key":"GoTerm","value":"P:mycothiol-dependent detoxification"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.50.10320","properties":[{"key":"EntryName","value":"LmbE-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01482","properties":[{"key":"EntryName","value":"Mca"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003737","properties":[{"key":"EntryName","value":"GlcNAc_PI_deacetylase-related"}]},{"database":"InterPro","id":"IPR024078","properties":[{"key":"EntryName","value":"LmbE-like_dom_sf"}]},{"database":"InterPro","id":"IPR017811","properties":[{"key":"EntryName","value":"Mca"}]},{"database":"NCBIfam","id":"TIGR03446","properties":[{"key":"EntryName","value":"mycothiol_Mca"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12993:SF11","properties":[{"key":"EntryName","value":"N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12993","properties":[{"key":"EntryName","value":"N-ACETYLGLUCOSAMINYL-PHOSPHATIDYLINOSITOL DE-N-ACETYLASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02585","properties":[{"key":"EntryName","value":"PIG-L"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102588","properties":[{"key":"EntryName","value":"LmbE-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVTHGERPRLLTVHAHPDDESSKGAATLAKYAAEGADVLVATCTGGERGSVLNPALDRPEVRADLPAIRRREMAAAREILGVRQRFLGFTDSGLPGDGEDLPAGCFALEPLADAARPLVALVREFRPHVVITYDETGGYPHPDHIKTHQVTAEAFDAAADPDRYPGTGAPWRPVKLYYQGAFSRDWFQALHDGMLARGLESPMGPVLAEWPDGAARLETTTRVPCAEYFGVRDRALLAHATQIDPDAGFMLHPRDVEREVWPTEDYHLARSHVETELPESDLFAGLPVTVPAG","length":294,"molWeight":32094,"crc64":"FD9214EC7C93E6F4","md5":"EB0925CCB3AEFFF7050197BE69221989"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Binding site":3},"uniParcId":"UPI00124D5D0F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M0B4","uniProtkbId":"A0A6I4M0B4_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99172.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Phosphoribosylformylglycinamidine synthase subunit PurQ"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"FGAM synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"6.3.5.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Formylglycinamide ribonucleotide amidotransferase subunit I"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"FGAR amidotransferase I"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"FGAR-AT I"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Glutaminase PurQ"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"3.5.1.2"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Phosphoribosylformylglycinamidine synthase subunit I"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99172.1"}],"value":"purQ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99172.1"}],"value":"F8568_001970"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17129"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:147286"},{"database":"ChEBI","id":"CHEBI:147287"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99172.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00421"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99172.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99172.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000001","properties":[{"key":"ProteinId","value":"MVZ99172.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151590537.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000001.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M0B4","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00128"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004642","properties":[{"key":"GoTerm","value":"F:phosphoribosylformylglycinamidine synthase activity"},{"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:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01740","properties":[{"key":"EntryName","value":"GATase1_FGAR_AT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000019","properties":[{"key":"EntryName","value":"Phosphoribosylformylglycinamidine synthase subunit PurQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00421","properties":[{"key":"EntryName","value":"PurQ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR010075","properties":[{"key":"EntryName","value":"PRibForGlyAmidine_synth_PurQ"}]},{"database":"NCBIfam","id":"TIGR01737","properties":[{"key":"EntryName","value":"FGAM_synth_I"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002957","properties":[{"key":"EntryName","value":"purQ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47552","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47552:SF1","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13507","properties":[{"key":"EntryName","value":"GATase_5"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001586","properties":[{"key":"EntryName","value":"FGAM_synth_I"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01211","properties":[{"key":"EntryName","value":"GATase_5"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDAARVGVITFPGSLDDKDAARAVRLAGAEPVALWHADHDLRGVDAVVLPGGFSYGDYLRAGAIARFAPLMTELVAAAKAGLPVLGICNGFQVLCESHLLPGALLPNAGLHFVCRDQRLRVENAGTAWTSEYTEGQELVIPVKNADGRYTADRETLAELADSGRIVARYLDLNPNGSLDDIAGICNEAGNVVGLMPHPEHAAESLTGPSTDGLGFFTSIVKRLVNA","length":226,"molWeight":23815,"crc64":"D217BD5F5CA482EE","md5":"275B2FA64E0E5227B6857D5DC6019EF5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"CAUTION":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI00124C5D88"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M0I3","uniProtkbId":"A0A6I4M0I3_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99397.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"3-isopropylmalate dehydratase large subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"4.2.1.33"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"Alpha-IPM isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"IPMI"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"Isopropylmalate isomerase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99397.1"}],"value":"leuC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99397.1"}],"value":"F8568_003170"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"Catalyzes the isomerization between 2-isopropylmalate and 3-isopropylmalate, via the formation of 2-isopropylmaleate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R,3S)-3-isopropylmalate = (2S)-2-isopropylmalate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32287"},{"database":"ChEBI","id":"CHEBI:1178"},{"database":"ChEBI","id":"CHEBI:35121"}],"ecNumber":"4.2.1.33","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000491"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"Binds 1 [4Fe-4S] cluster per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004729"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"Heterodimer of LeuC and LeuD"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"value":"Belongs to the aconitase/IPM isomerase family. LeuC type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99397.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"Aconitase/3-isopropylmalate dehydratase large subunit alpha/beta/alpha","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00330"}]},{"type":"Region","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":446,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023304"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0100","category":"Biological process","name":"Branched-chain amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022430"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0432","category":"Biological process","name":"Leucine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01026"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99397.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99397.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99397.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151591150.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M0I3","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00048","properties":[{"key":"RectionId","value":"UER00071"}]},{"database":"UniPathway","id":"UPA00946","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003861","properties":[{"key":"GoTerm","value":"F:3-isopropylmalate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009098","properties":[{"key":"GoTerm","value":"P:L-leucine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01583","properties":[{"key":"EntryName","value":"IPMI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.499.10:FF:000006","properties":[{"key":"EntryName","value":"3-isopropylmalate dehydratase large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.499.10:FF:000007","properties":[{"key":"EntryName","value":"3-isopropylmalate dehydratase large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.499.10","properties":[{"key":"EntryName","value":"Aconitase, domain 3"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01026","properties":[{"key":"EntryName","value":"LeuC_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004430","properties":[{"key":"EntryName","value":"3-IsopropMal_deHydase_lsu"}]},{"database":"InterPro","id":"IPR015931","properties":[{"key":"EntryName","value":"Acnase/IPM_dHydase_lsu_aba_1/3"}]},{"database":"InterPro","id":"IPR001030","properties":[{"key":"EntryName","value":"Acoase/IPM_deHydtase_lsu_aba"}]},{"database":"InterPro","id":"IPR018136","properties":[{"key":"EntryName","value":"Aconitase_4Fe-4S_BS"}]},{"database":"InterPro","id":"IPR036008","properties":[{"key":"EntryName","value":"Aconitase_4Fe-4S_dom"}]},{"database":"InterPro","id":"IPR050067","properties":[{"key":"EntryName","value":"IPM_dehydratase_rel_enz"}]},{"database":"InterPro","id":"IPR033941","properties":[{"key":"EntryName","value":"IPMI_cat"}]},{"database":"NCBIfam","id":"TIGR00170","properties":[{"key":"EntryName","value":"leuC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004016","properties":[{"key":"EntryName","value":"PRK05478.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009116","properties":[{"key":"EntryName","value":"PRK12466.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43822:SF9","properties":[{"key":"EntryName","value":"3-ISOPROPYLMALATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43822","properties":[{"key":"EntryName","value":"HOMOACONITASE, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00330","properties":[{"key":"EntryName","value":"Aconitase"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00415","properties":[{"key":"EntryName","value":"ACONITASE"}]},{"database":"SUPFAM","id":"SSF53732","properties":[{"key":"EntryName","value":"Aconitase iron-sulfur domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00450","properties":[{"key":"EntryName","value":"ACONITASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01244","properties":[{"key":"EntryName","value":"ACONITASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGRTLAEKVYDAHVVRRAEGEPDLLYIDLHLVHEVTSPQAFDGLRMAGRQVRRPDLTIATEDHNVPTTDLLKPIADPVSRTQVETLRKNCSDFGIRLHPMGDDGQGIVHVIGPQLGLTQPGMTVVCGDSHTSTHGAFGALAFGIGTSEVEHVLATQTLPQIQPKTMAVTVNGTLPDGVTAKDLILAIIAKIGTGGGQGHIIEYRGEAVRSLSMEGRMTVCNMSIEAGARAGMIAPDETTFAYLKGRPNAPQGEDWDKAVEYWTSLRTDDDAVFDKEVVIDAAELTPFVTWGTNPGQGLPLAESVPDPATIDDPVKRQNAERALEYMGLTAGTPLRDIEVDTVFVGSCTNGRIEDLRAVAGVLKGRKVADGVRMLVVPGSMEVKKQAEEEGLDRVIAASGAEWREAGCSMCLAMNPDKLTPGERSASTSNRNFEGRQGPGGRTHLVSPAVAAATAVTGRLAAPADL","length":465,"molWeight":49494,"crc64":"70D7173E93BA3776","md5":"660298880EC64AF31CD39604BB4448CD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Binding site":3},"uniParcId":"UPI00124F2385"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M0N3","uniProtkbId":"A0A6I4M0N3_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2020-08-12","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99447.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019179"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"value":"Ribonuclease HII"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"value":"RNase HII"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012180"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"value":"3.1.26.4"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"value":"rnhB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99447.1"}],"value":"F8568_003450"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004065"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003515"}],"value":"Endonuclease that specifically degrades the RNA of RNA-DNA hybrids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Endonucleolytic cleavage to 5'-phosphomonoester.","ecNumber":"3.1.26.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01319"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003515"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01319"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01319"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01319"}],"value":"Manganese or magnesium. Binds 1 divalent metal ion per monomer in the absence of substrate. May bind a second metal ion after substrate binding."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007383"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003515"}],"value":"Belongs to the RNase HII family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99447.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"RNase H type-2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51975"}]},{"type":"Region","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01319"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":36,"modifier":"EXACT"},"end":{"value":36,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01319"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01319"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00052"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99447.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99447.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99447.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151591228.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M0N3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0032299","properties":[{"key":"GoTerm","value":"C:ribonuclease H2 complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004523","properties":[{"key":"GoTerm","value":"F:RNA-DNA hybrid ribonuclease activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043137","properties":[{"key":"GoTerm","value":"P:DNA replication, removal of RNA primer"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006298","properties":[{"key":"GoTerm","value":"P:mismatch repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd07182","properties":[{"key":"EntryName","value":"RNase_HII_bacteria_HII_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.420.10","properties":[{"key":"EntryName","value":"Ribonuclease H-like superfamily/Ribonuclease H"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00052_B","properties":[{"key":"EntryName","value":"RNase_HII_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022898","properties":[{"key":"EntryName","value":"RNase_HII"}]},{"database":"InterPro","id":"IPR001352","properties":[{"key":"EntryName","value":"RNase_HII/HIII"}]},{"database":"InterPro","id":"IPR024567","properties":[{"key":"EntryName","value":"RNase_HII/HIII_dom"}]},{"database":"InterPro","id":"IPR012337","properties":[{"key":"EntryName","value":"RNaseH-like_sf"}]},{"database":"InterPro","id":"IPR036397","properties":[{"key":"EntryName","value":"RNaseH_sf"}]},{"database":"NCBIfam","id":"NF000595","properties":[{"key":"EntryName","value":"PRK00015.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF000598","properties":[{"key":"EntryName","value":"PRK00015.2-2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10954","properties":[{"key":"EntryName","value":"RIBONUCLEASE H2 SUBUNIT A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10954:SF18","properties":[{"key":"EntryName","value":"RIBONUCLEASE HII"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01351","properties":[{"key":"EntryName","value":"RNase_HII"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53098","properties":[{"key":"EntryName","value":"Ribonuclease H-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51975","properties":[{"key":"EntryName","value":"RNASE_H_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKGRPLRFTPRRDAGLHAYERALEHAGLSPVAGVDEAGRGACAGPLVVAAVILHGGRGGRIDGLTDSKMLTPARREELYAEITRRARAWSAVIIPCHDIDRIGLHRCNVTGMRRALAALDTRPAYVLSDGFPVPGLEAPGLAVIKGDQVAACVAAASIVAKVTRDRIMVDLHERYPQYGFDVHKGYVTRAHGAALAEHGPCPEHRFSYVNVGRALRNNGEVALGEETEGEVPGEGRTEGARA","length":242,"molWeight":25893,"crc64":"D34E9BC6550F8165","md5":"F1883A73DFD691663AA95D374D24D271"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":3},"uniParcId":"UPI00124D7491"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M0S9","uniProtkbId":"A0A6I4M0S9_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99362.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Ketol-acid reductoisomerase (NADP(+))"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"KARI"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"1.1.1.86"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Acetohydroxy-acid isomeroreductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"AHIR"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Alpha-keto-beta-hydroxylacyl reductoisomerase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99362.1"}],"value":"ilvC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99362.1"}],"value":"F8568_002970"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Involved in the biosynthesis of branched-chain amino acids (BCAA). Catalyzes an alkyl-migration followed by a ketol-acid reduction of (S)-2-acetolactate (S2AL) to yield (R)-2,3-dihydroxy-isovalerate. In the isomerase reaction, S2AL is rearranged via a Mg-dependent methyl migration to produce 3-hydroxy-3-methyl-2-ketobutyrate (HMKB). In the reductase reaction, this 2-ketoacid undergoes a metal-dependent reduction by NADPH to yield (R)-2,3-dihydroxy-isovalerate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) = (2S)-2-acetolactate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22068"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:49072"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:58476"}],"ecNumber":"1.1.1.86","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049021"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R,3R)-2,3-dihydroxy-3-methylpentanoate + NADP(+) = (S)-2-ethyl-2-hydroxy-3-oxobutanoate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13493"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:49256"},{"database":"ChEBI","id":"CHEBI:49258"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.86","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Binds 2 magnesium ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004885"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004864"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 2/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010318"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01198"}],"value":"Belongs to the ketol-acid reductoisomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99362.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"KARI N-terminal Rossmann","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51850"}]},{"type":"Domain","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"KARI C-terminal knotted","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51851"}]},{"type":"Active site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01197"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01197"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01197"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01197"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01197"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01198"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01198"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01198"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01198"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01198"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01198"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023304"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"id":"KW-0100","category":"Biological process","name":"Branched-chain amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00435"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99362.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99362.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99362.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151591085.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M0S9","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00047","properties":[{"key":"RectionId","value":"UER00056"}]},{"database":"UniPathway","id":"UPA00049","properties":[{"key":"RectionId","value":"UER00060"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004455","properties":[{"key":"GoTerm","value":"F:ketol-acid reductoisomerase 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:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009099","properties":[{"key":"GoTerm","value":"P:L-valine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.720:FF:000023","properties":[{"key":"EntryName","value":"Ketol-acid reductoisomerase (NADP(+))"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.240.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00435","properties":[{"key":"EntryName","value":"IlvC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008927","properties":[{"key":"EntryName","value":"6-PGluconate_DH-like_C_sf"}]},{"database":"InterPro","id":"IPR013023","properties":[{"key":"EntryName","value":"KARI"}]},{"database":"InterPro","id":"IPR000506","properties":[{"key":"EntryName","value":"KARI_C"}]},{"database":"InterPro","id":"IPR013116","properties":[{"key":"EntryName","value":"KARI_N"}]},{"database":"InterPro","id":"IPR014359","properties":[{"key":"EntryName","value":"KARI_prok"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"NF004017","properties":[{"key":"EntryName","value":"ilvC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00465","properties":[{"key":"EntryName","value":"ilvC"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009940","properties":[{"key":"EntryName","value":"PRK13403.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21371","properties":[{"key":"EntryName","value":"KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21371:SF1","properties":[{"key":"EntryName","value":"KETOL-ACID REDUCTOISOMERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01450","properties":[{"key":"EntryName","value":"KARI_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07991","properties":[{"key":"EntryName","value":"KARI_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000116","properties":[{"key":"EntryName","value":"IlvC_gammaproteo"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48179","properties":[{"key":"EntryName","value":"6-phosphogluconate dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51851","properties":[{"key":"EntryName","value":"KARI_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51850","properties":[{"key":"EntryName","value":"KARI_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFYDDAADLSVIQGRHVAIIGYGSQGHAHALSLRDSGVDVRVGLREGSASREKAEAEGLRVVTPAEAAEEADLVMLLAPDHHHREIFEKDIKPALVEGDALFFGHGFSIRYGLVQPPEGVDVAMVAPKGPGHLVRRQFVAGRGVPVIVAVERDASGNAWPLALSYAKGIGGLRAGGIKTTFTEETETDLFGEQAVLCGGASELVKAGFEVLTEAGYQPEVAYFEVLHELKLIVDLMYEGGISKMYWSVSDNAEYGGYSRGPRVITPETKAAMKKLLGEIQSGEYAKELVEEFEGGQAQFGKYREQLAEHPIEKTGAELRPMMSWIND","length":327,"molWeight":35461,"crc64":"9ECD5D0631553657","md5":"58CB40CD4789D1D3EB62F1F5AFEE6BF0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":11},"uniParcId":"UPI00124F384A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M0T9","uniProtkbId":"A0A6I4M0T9_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2020-08-12","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99372.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013053"}],"value":"branched-chain-amino-acid transaminase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013053"}],"value":"2.6.1.42"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99372.1"}],"value":"F8568_003020"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-isoleucine + 2-oxoglutarate = (S)-3-methyl-2-oxopentanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24801"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:35146"},{"database":"ChEBI","id":"CHEBI:58045"}],"ecNumber":"2.6.1.42","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048798"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-leucine + 2-oxoglutarate = 4-methyl-2-oxopentanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18321"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:17865"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57427"}],"ecNumber":"2.6.1.42","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049229"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-valine + 2-oxoglutarate = 3-methyl-2-oxobutanoate + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24813"},{"database":"ChEBI","id":"CHEBI:11851"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57762"}],"ecNumber":"2.6.1.42","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048212"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004824"}],"value":"Amino-acid biosynthesis; L-isoleucine biosynthesis; L-isoleucine from 2-oxobutanoate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005072"}],"value":"Amino-acid biosynthesis; L-leucine biosynthesis; L-leucine from 3-methyl-2-oxobutanoate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004931"}],"value":"Amino-acid biosynthesis; L-valine biosynthesis; L-valine from pyruvate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009320"}],"value":"Belongs to the class-IV pyridoxal-phosphate-dependent aminotransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99372.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Modified residue","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006468-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022576"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99372.1"}],"id":"KW-0032","category":"Molecular function","name":"Aminotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023304"}],"id":"KW-0100","category":"Biological process","name":"Branched-chain amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99372.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99372.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99372.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99372.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151591101.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M0T9","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00047","properties":[{"key":"RectionId","value":"UER00058"}]},{"database":"UniPathway","id":"UPA00048","properties":[{"key":"RectionId","value":"UER00073"}]},{"database":"UniPathway","id":"UPA00049","properties":[{"key":"RectionId","value":"UER00062"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0004084","properties":[{"key":"GoTerm","value":"F:branched-chain-amino-acid:2-oxoglutarate transaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009098","properties":[{"key":"GoTerm","value":"P:L-leucine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0009099","properties":[{"key":"GoTerm","value":"P:L-valine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd01557","properties":[{"key":"EntryName","value":"BCAT_beta_family"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.10.10","properties":[{"key":"EntryName","value":"D-amino Acid Aminotransferase, subunit A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001544","properties":[{"key":"EntryName","value":"Aminotrans_IV"}]},{"database":"InterPro","id":"IPR036038","properties":[{"key":"EntryName","value":"Aminotransferase-like"}]},{"database":"InterPro","id":"IPR005786","properties":[{"key":"EntryName","value":"B_amino_transII"}]},{"database":"InterPro","id":"IPR043132","properties":[{"key":"EntryName","value":"BCAT-like_C"}]},{"database":"InterPro","id":"IPR043131","properties":[{"key":"EntryName","value":"BCAT-like_N"}]},{"database":"InterPro","id":"IPR033939","properties":[{"key":"EntryName","value":"BCAT_family"}]},{"database":"NCBIfam","id":"TIGR01123","properties":[{"key":"EntryName","value":"ilvE_II"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009897","properties":[{"key":"EntryName","value":"PRK13357.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11825:SF44","properties":[{"key":"EntryName","value":"BRANCHED-CHAIN-AMINO-ACID AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11825","properties":[{"key":"EntryName","value":"SUBGROUP IIII AMINOTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01063","properties":[{"key":"EntryName","value":"Aminotran_4"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006468","properties":[{"key":"EntryName","value":"BCAT1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56752","properties":[{"key":"EntryName","value":"D-aminoacid aminotransferase-like PLP-dependent enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDTLDFEITLTERPATAAERERVLADPGFGRYFTDHMITVRYSAERGWHDAKLEPYGPIPMDPASQVFHYAQELFEGLKAYKQPDGSIVTFRPFMNAARMNRSARRMAMPEIPEQLFVDAVELLVRTDKEWVPGAEGHSLYLRPFMFATTRALGVNSPANEFLFMVIASPSGLYYPRGIKPVSVWLSQDYTRAAPGGTGEAKFGGNYAASFAGQAEAVEQGCDQVVWLDAVEHRWVEEVGSMNLMFVYGSGSRARLLTPALTGTLLAGVTRDSMLKLAPDLGIPAEEGKISIDEWQAGCASGEITEVFGCGTAAIISPVGRVRGRDREWTIGDGEPGEISMRLRQELVGIQYGTRPDPYGWVHKIV","length":367,"molWeight":40494,"crc64":"C2030C2BA0140E7B","md5":"9802E180B1C96A68F833A0413508A64C"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":3,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Modified residue":1},"uniParcId":"UPI00124E59F9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A6I4M0Z7","uniProtkbId":"A0A6I4M0Z7_9ACTN","entryAudit":{"firstPublicDate":"2020-08-12","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2020-08-12","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomadura physcomitrii","taxonId":2650748,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99432.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Streptosporangiales","Thermomonosporaceae","Actinomadura"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Chromosome partition protein Smc"}}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99432.1"}],"value":"smc"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99432.1"}],"value":"F8568_003370"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Required for chromosome condensation and partitioning"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Contains large globular domains required for ATP hydrolysis at each terminus and a third globular domain forming a flexible hinge near the middle of the molecule. These domains are separated by coiled-coil structures"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"value":"Belongs to the SMC family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99432.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":532,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"SMC hinge","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00968"}]},{"type":"Region","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":979,"modifier":"EXACT"},"end":{"value":998,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":673,"modifier":"EXACT"},"end":{"value":812,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":854,"modifier":"EXACT"},"end":{"value":923,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Coiled coil","location":{"start":{"value":1004,"modifier":"EXACT"},"end":{"value":1066,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}]},{"type":"Compositional bias","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":332,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":39,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023054"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01894"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000462055"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-8BGAHRMGQJ798","citationType":"submission","authors":["Zhuang X."],"title":"Actinomadura physcomitrii sp. nov., a novel actinomycete isolated from moss [Physcomitrium sphaericum (Ludw) Fuernr].","publicationDate":"DEC-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99432.1"}],"value":"LD22","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MVZ99432.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WBMS02000002","properties":[{"key":"ProteinId","value":"MVZ99432.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_151591202.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WBMS02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A6I4M0Z7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000462055","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005694","properties":[{"key":"GoTerm","value":"C:chromosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030261","properties":[{"key":"GoTerm","value":"P:chromosome condensation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0007059","properties":[{"key":"GoTerm","value":"P:chromosome segregation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006260","properties":[{"key":"GoTerm","value":"P:DNA replication"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0007062","properties":[{"key":"GoTerm","value":"P:sister chromatid cohesion"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.300:FF:000901","properties":[{"key":"EntryName","value":"Chromosome partition protein Smc"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000984","properties":[{"key":"EntryName","value":"Chromosome partition protein Smc"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1060.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.1620","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":"HAMAP","id":"MF_01894","properties":[{"key":"EntryName","value":"Smc_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR003395","properties":[{"key":"EntryName","value":"RecF/RecN/SMC_N"}]},{"database":"InterPro","id":"IPR024704","properties":[{"key":"EntryName","value":"SMC"}]},{"database":"InterPro","id":"IPR010935","properties":[{"key":"EntryName","value":"SMC_hinge"}]},{"database":"InterPro","id":"IPR036277","properties":[{"key":"EntryName","value":"SMC_hinge_sf"}]},{"database":"InterPro","id":"IPR011890","properties":[{"key":"EntryName","value":"SMC_prok"}]},{"database":"NCBIfam","id":"TIGR02168","properties":[{"key":"EntryName","value":"SMC_prok_B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43977","properties":[{"key":"EntryName","value":"STRUCTURAL MAINTENANCE OF CHROMOSOMES PROTEIN 3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06470","properties":[{"key":"EntryName","value":"SMC_hinge"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02463","properties":[{"key":"EntryName","value":"SMC_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005719","properties":[{"key":"EntryName","value":"SMC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00968","properties":[{"key":"EntryName","value":"SMC_hinge"},{"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":"SSF75553","properties":[{"key":"EntryName","value":"Smc hinge domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYLKTLTLRGFKSFASSTTLKFEPGITAVVGPNGSGKSNVVDALAWVMGEQGAKSLRGGKMEDVIFAGTANRAPLGRAEVVLTIDNADGALPIDYTEVTISRLMFRSGSSEYAINGDSCRLLDIQELLSDSGIGREMHVIIGQGQLDRVLHSGPEGRRAVIEEAAGVLKHRKRKEKALRKLDAMQANLTRVQDLTTELRRQLKPLGKQAEIARRAAVIQADLRDARLRLLADDLVTLRTKLEQEAADEAAIRERRAETERALGEAQEREAVLEAEEAEQAPKLAQVQDTWFRLSALKERLRGVGDLAGERHRNAAEAREEERRGRDPEDMEREAAEIREQEEMLRAALDEAQDGLADAVEQRTGAEEALAAEERRLQAAARAAADRREELARLRGRVEALRSKAQAGRSEIGRLADARDEAAQRAETAQAEFEAFEAEVVEDPALAAEHEAAQEALATAKDAAEAARAAVDGPRRALREARSAVAAARTADQAAQKQATALQARIEALNLTLASAADGGEALLAAGADGSVEGVLGTVASLLAVRPGYETAVAAALGDAAQAIAVGSLDTAEAALTLLRSRDAGRAGLLVGGGAPGGSERVPGVDYAADAVTVPDAVRPALEHLLSGVAVVDDVPAAAALVRREPALRAVTRDGDLVGAHWAQGGAAGGGQSLLQMRATLDQATEDLAAAETAAETAAEELTAAAEAEQSAQAALDAAQAAANQAQNGVNQAQSDLDRVRARLREFDAQAAQEAKRAARLEADVRAARGEAERLTKALDAANESLERDTEAAEELAMRLAEAEEAAEVADDAGHDTEARDELAERCRVLRSAEMEARLAVRTAEERVQAITGRADALERGARREREERARAAERRARRELQARTAKAVLKGARTALDRIELSLAAAVRQREAAEQAKAAREAELKVVRTQVRELSGTLERLVNVVHGNEVARAEQRLRLEQLEQRALEEFGLEVESLVGEYGPDQPVPPDPDKGEDAEPAPYVRAVQEKRAKAAERQLNQLGKVNPLALEEFAALEERHAFLTSQLDDLKKTQRELLALVKEVDDRVQQVFAAAYDDTAREFERIFARLFPGGEGSLSLTEPEDMLATGVEVAARPPGKKVKRLSLLSGGERSLVAIAFLVAVFKARPSPFYVLDEVEAALDDTNTQRLITVFEELRESSQLIVITHQKRTMEGADALYGVSMRGDGVTQVVSQRLREQEPA","length":1222,"molWeight":131567,"crc64":"6922114BE06B6E91","md5":"0FDDC447876C2EE3196FE055519150FE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Coiled coil":5,"Compositional bias":1,"Binding site":1},"uniParcId":"UPI00124C0649"}}]}