{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2U7T4","uniProtkbId":"A0A0Q2U7T4_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":56,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52709.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"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"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52709.1"}],"value":"AN277_0201820"}]}],"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":"OAX52709.1"}],"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":127,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"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":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"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":205,"modifier":"EXACT"},"end":{"value":206,"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":239,"modifier":"EXACT"},"end":{"value":239,"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":262,"modifier":"EXACT"},"end":{"value":264,"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":341,"modifier":"EXACT"},"end":{"value":341,"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":"UP000053171"}],"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-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52709.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52709.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000002","properties":[{"key":"ProteinId","value":"OAX52709.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684555.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2U7T4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"37923.BK826_08535","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61261972","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_01220","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.763","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"Proteomes","id":"UP000053171","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSESTATPVEITTRPEPGRILLKAPRRGKPPKHLADFDLAGRKEFLTELGHPGFRASQLSTHYFDHLTTDPQRMTDLPAATREEMVAAAMPQLLTEVRTLEADGGDTIKSVYRLFDGALVESVLMRYEHRVTMCISSQAGCGMNCPFCATGQAGLTRNLSTAEIVEQVVAGARRLKSMQGLEQAEHGTEATRPLRVSNIVFMGMGEALANYKASLGAVHRLIDPSPEGLGISARGITMSTVGLVPGIRKFTMENLPVTLALSLHAPDDELRDELIPINTRWKVDEALDAAYDYYRQTGRRVSIEYALIRDINDQGWRADLLGKKLAQRGRGWVHVNPIPLNPTPGSKWTASRPGVEQNFVERLRAHGIPTTVRDTRGSDIDGACGQLAAAS","length":391,"molWeight":42789,"crc64":"07FD84B9748414FB","md5":"34D64ADFD9241038A7B0B95ABC0B4A1D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI0006EBE090"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q3EPZ6","uniProtkbId":"A0A0Q3EPZ6_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":58,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52908.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"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":"OAX52908.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52908.1"}],"value":"AN277_0200640"}]}],"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":"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":"OAX52908.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":16,"modifier":"EXACT"},"end":{"value":149,"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":247,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":471,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"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":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":92,"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":118,"modifier":"EXACT"},"end":{"value":120,"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":120,"modifier":"EXACT"},"end":{"value":120,"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":157,"modifier":"EXACT"},"end":{"value":157,"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":172,"modifier":"EXACT"},"end":{"value":172,"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":187,"modifier":"EXACT"},"end":{"value":187,"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":245,"modifier":"EXACT"},"end":{"value":245,"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":245,"modifier":"EXACT"},"end":{"value":245,"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":350,"modifier":"EXACT"},"end":{"value":350,"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":368,"modifier":"EXACT"},"end":{"value":368,"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":394,"modifier":"EXACT"},"end":{"value":394,"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":397,"modifier":"EXACT"},"end":{"value":397,"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":403,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":422,"modifier":"EXACT"},"end":{"value":422,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":440,"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":"UP000053171"}],"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-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52908.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52908.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52908.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684332.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q3EPZ6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"37923.BK826_04115","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263067","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.840","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00113","properties":[{"key":"RectionId","value":"UER00532"}]},{"database":"UniPathway","id":"UPA00973","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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":"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":"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":"MTSAPQSEATGAPTAVIVLAAGAGTRMKSALPKVMHPIGGRSMVEHAVATARELAPQHLAVVVRHQRERVAEHVAAFDAEALLVDQDEIPGTGRAVEVAVDALDGLGAPLEGTVVVTYGDVPLLTPATIGELTRFHREAGNAVTVLTTHLAEPGGYGRIIRNEGGEVTAIVEAKDATAEQLAITEVNSGIYAFDAAVLRDSLREVTTENAQGEKYLTDVLSIARTHGHRTSALSVADRWEVEGANDRVQLSRLGRVLNDRITERHMRAGVSIVDPATTWIDATVSIGEDVTILPGTQLHGTTVIETGATVGPDTTLTDVLVGEGAEVVRTHGSDAEIGPGASVGPFAYLRPGTWLGEGGKIGTFCETKNAQIGAGSKLPHLSYAGDVTIGEHSNIGAASVFVNYDGVNKHRSVIGSHVRMGSDNMYVAPVTVGDGAYSGAGTVIRQDVPAGALAINDAPQRTIEGWVERKRPGTAAADAAARAQRAAHAQHDGEEG","length":496,"molWeight":51682,"crc64":"D476751A5D3BF1A7","md5":"10E7AC9FF85B1E9755B845C6184EC7F0"},"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,"Compositional bias":1,"Active site":1,"Binding site":19},"uniParcId":"UPI0006EBA249"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NRZ2","uniProtkbId":"A0A199NRZ2_9MICC","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-10-05","entryVersion":36,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51466.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"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"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51466.1"}],"value":"AN277_0208600"}]}],"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":"OAX51466.1"}],"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":87,"modifier":"EXACT"},"end":{"value":87,"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":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"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":185,"modifier":"EXACT"},"end":{"value":185,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":185,"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":55,"modifier":"EXACT"},"end":{"value":57,"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":116,"modifier":"EXACT"},"end":{"value":116,"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":147,"modifier":"EXACT"},"end":{"value":148,"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":"UP000053171"}],"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-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51466.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51466.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000018","properties":[{"key":"ProteinId","value":"OAX51466.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A199NRZ2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00245","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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":"PS51274","properties":[{"key":"EntryName","value":"GATASE_COBBQ"},{"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":"MVSPPNTAPRAVGVLALQGGVAEHLRMLESLGADARKVRHPADLEGLDALVLPGGESSTIDRLTRTFGLREPLIDFARAGHPVLGTCAGLILLARTIRDPAPGQRSLGLLDAAVARNAFGPQTSSAEALLTWGGSARPEGTVRAAFIRAPEVVEHGPDVEVLARFEGRVVAVRQGRVLGISFHPELTGDTTVHRELLGLIPD","length":202,"molWeight":21272,"crc64":"6991B6042C1518EF","md5":"C6EA1F0D8CCC9CF39EDF496DDDBC693A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI0007E8127A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NSZ3","uniProtkbId":"A0A199NSZ3_9MICC","entryAudit":{"firstPublicDate":"2016-11-02","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-11-02","entryVersion":43,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51723.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"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":"OAX51723.1"}],"value":"AN277_0207375"}]}],"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":"OAX51723.1"}],"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":27,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":558,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":292,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"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":"Active site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":407,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":539,"modifier":"EXACT"},"end":{"value":539,"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":541,"modifier":"EXACT"},"end":{"value":541,"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":36,"modifier":"EXACT"},"end":{"value":36,"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":36,"modifier":"EXACT"},"end":{"value":36,"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":37,"modifier":"EXACT"},"end":{"value":42,"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":94,"modifier":"EXACT"},"end":{"value":94,"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":94,"modifier":"EXACT"},"end":{"value":94,"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":166,"modifier":"EXACT"},"end":{"value":166,"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":173,"modifier":"EXACT"},"end":{"value":175,"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":213,"modifier":"EXACT"},"end":{"value":218,"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":213,"modifier":"EXACT"},"end":{"value":218,"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":249,"modifier":"EXACT"},"end":{"value":249,"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":249,"modifier":"EXACT"},"end":{"value":249,"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":267,"modifier":"EXACT"},"end":{"value":267,"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":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":411,"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":431,"modifier":"EXACT"},"end":{"value":431,"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":492,"modifier":"EXACT"},"end":{"value":492,"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":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51723.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51723.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000013","properties":[{"key":"ProteinId","value":"OAX51723.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684700.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A199NSZ3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263247","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000053171","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:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIGSRPVVNESKTASAQHSTDRKITRQIFVTGGVASSLGKGLTASSLGRLLRSRGLSVTMQKLDPYLNVDPGTMNPFQHGEVFVTDDGAETDLDIGHYERFLDENLDASANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKARMRRRATGEPDAPDIIITEIGGTVGDIESQPFLEAARQVRRDVGRRHVFFLHVSLIPYIGPSGEMKTKPTQHSVAALRGLGIIPDALVLRSAKEVSESLKAKVGSACDVDTEAVIACPDAPSIYDIPKTLYRQGLDAYILDYLGLDYQPADFTEWDKLLRTVHQPSHEVTVGLVGKYIDLPDAYLSVSEALRAGGFANDAKVSIKWIASDLCQDPEGAARQLADVDAICVPGGFGIRGLEGKLGALRYAREHRIPTLGLCLGLQCMVMEYARSVVGLPEASSTEFDPETSTPIIATMEEQKQFVDGAGDLGGTMRLGLYDAKLTEGSVVAGAYGATEVKERHRHRYEVNNAYREQLEEAGLVISGTSPDGSLVEFVELPAEVHPYYVSTQAHPELLSRPTRSHPLFRGLIAAALAR","length":563,"molWeight":61127,"crc64":"D11BFECD37AE3934","md5":"077500729B0E1CEE9CF41712D27F5742"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":4,"Binding site":16},"uniParcId":"UPI0006EB9B7A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NT80","uniProtkbId":"A0A199NT80_9MICC","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-10-05","entryVersion":33,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52025.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52025.1"}],"value":"AN277_0205685"}]}],"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":"OAX52025.1"}],"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":168,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":416,"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":190,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":432,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":284,"modifier":"EXACT"},"end":{"value":284,"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":294,"modifier":"EXACT"},"end":{"value":294,"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":313,"modifier":"EXACT"},"end":{"value":316,"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":339,"modifier":"EXACT"},"end":{"value":339,"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":357,"modifier":"EXACT"},"end":{"value":357,"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":361,"modifier":"EXACT"},"end":{"value":361,"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":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52025.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52025.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000009","properties":[{"key":"ProteinId","value":"OAX52025.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_064725378.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAIUDH010000001.1"}]},{"database":"AlphaFoldDB","id":"A0A199NT80","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000053171","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":"MRIVLGIGGGIAAYKAAILLRLLKESGHDVVPLPTDTALRFVGAPTWEALSGHPVNTSVFDEVQAVNHVRQAEDADLVLIAPATADLLARIAAGRADDLLSATVLTATCPVVLAPAMHTQMWTNPATRDNVALLRSRGLRVIEPAVGRLTGADSGPGRLPEPADIARQALAAVSAAGLTPKEATRLARLRVLVTAGGTREALDPVRYLGNRSSGKQGIAVARAAADAGAVAHLVLAHAEVPAPQPTTMLSLSRVSSALQLRERVGELIRQEAPDVVVMAAAVADFRPAAYAETKIKKDPGTQDAPGIELVRNPDILRGIVTDRESDRTPEQPGPVIVGFAAETGSAQASVAELGRAKLESKGCDVLVVNEVGAQKVFGRDETAATILTRRPDGEVEEQEVAGTKDELAAALWRAVLRLIDDQSRRTASSASA","length":432,"molWeight":45224,"crc64":"4467E3C11EDABAD0","md5":"AA341B94E557E4FEDD48DCF5133BEA38"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI0007E8B3AA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NTL3","uniProtkbId":"A0A199NTL3_9MICC","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-10-05","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52424.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein nucleotidyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein adenylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.108"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Protein uridylyltransferase YdiU"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"2.7.7.-"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"ydiU"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"selO"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52424.1"}],"value":"AN277_0203485"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Nucleotidyltransferase involved in the post-translational modification of proteins. It can catalyze the addition of adenosine monophosphate (AMP) or uridine monophosphate (UMP) to a protein, resulting in modifications known as AMPylation and UMPylation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-histidyl-[protein] + UTP = N(tele)-(5'-uridylyl)-L-histidyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83891"},{"database":"Rhea","id":"RHEA-COMP:9745"},{"database":"Rhea","id":"RHEA-COMP:20239"},{"database":"ChEBI","id":"CHEBI:29979"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:233474"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + ATP = 3-O-(5'-adenylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58120"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:15073"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:142516"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-seryl-[protein] + UTP = O-(5'-uridylyl)-L-seryl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:64604"},{"database":"Rhea","id":"RHEA-COMP:9863"},{"database":"Rhea","id":"RHEA-COMP:16635"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:156051"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-threonyl-[protein] + ATP = 3-O-(5'-adenylyl)-L-threonyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54292"},{"database":"Rhea","id":"RHEA-COMP:11060"},{"database":"Rhea","id":"RHEA-COMP:13847"},{"database":"ChEBI","id":"CHEBI:30013"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:138113"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + ATP = O-(5'-adenylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54288"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:13846"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"}],"ecNumber":"2.7.7.108","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-tyrosyl-[protein] + UTP = O-(5'-uridylyl)-L-tyrosyl-[protein] + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:83887"},{"database":"Rhea","id":"RHEA-COMP:10136"},{"database":"Rhea","id":"RHEA-COMP:20238"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:90602"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009747"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"value":"Belongs to the SELO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52424.1"}],"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":99,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":503,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":478,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}]},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":85,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":152,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":217,"modifier":"EXACT"},"end":{"value":217,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00692"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52424.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52424.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000004","properties":[{"key":"ProteinId","value":"OAX52424.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_064725081.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_LJBJ02000004.1"}]},{"database":"AlphaFoldDB","id":"A0A199NTL3","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000053171","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0070733","properties":[{"key":"GoTerm","value":"F:AMPylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_00692","properties":[{"key":"EntryName","value":"YdiU_SelO"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003846","properties":[{"key":"EntryName","value":"SelO"}]},{"database":"PANTHER","id":"PTHR32057","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32057:SF14","properties":[{"key":"EntryName","value":"PROTEIN ADENYLYLTRANSFERASE SELO, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02696","properties":[{"key":"EntryName","value":"SelO"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MRSSFLQDLPELGIPWRAQPAPEPHSVLVNDGLAEQLGLDPQRLRAPAGAAFLTGTALPAGTRPAALAYAGHQFGGWSPRLGDGRALLLGDLPDAAAGFPEAVASPGPAAPGDPADADVDAPARETPDPASLRELHLKGTGRTPFARGGADGNAVLGPMLREHVVGEFLHAVGIPTTRSLGVAATGARVPRPDRADPRRTVELPGAVLARVAHSHVRVGTFQYALSTGGPELVRRLAHWCITRHHPEAADAANPPLELYRRVVFAQARLVAAWEAVSFVHGVMNTDNMALSGQGIDYGPCAFLDAHDPDAVFSSIDRTGRYRYRNQAAAAQWNLARCAEALLPVLDAEPDRAVDLAQEALAEFPSAYEAERLRLFAARIGVRVQTRGQEAAECGDSPDRADAGGLAEPAQVPARGAVAGSRAGAARPAASVVEDLLGLMAEHAADHTDTFRALIPVAETGDPAQLAADGSRSGSTRPGAEHAEEGTRDEPGGGAEPPLDPSLAADPRFREWLARWHQLGPDPALMRRSAPRVVPRNHALQEALDAAEAGEIGPVREILDAVSHPFEHRPGGTRLLAPSGSQARGFTTYCGT","length":591,"molWeight":62137,"crc64":"0F1C3424CDE833D1","md5":"56D3BA361B24B4DF4DE65D88D13E8880"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":3,"Compositional bias":3,"Active site":1,"Binding site":11},"uniParcId":"UPI0007E78DD1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NTQ9","uniProtkbId":"A0A199NTQ9_9MICC","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-10-05","entryVersion":42,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51983.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"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":"OAX51983.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51983.1"}],"value":"AN277_0205710"}]}],"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":"OAX51983.1"}],"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":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":870,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":952,"modifier":"EXACT"},"end":{"value":1095,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":952,"modifier":"EXACT"},"end":{"value":1107,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":715,"modifier":"EXACT"},"end":{"value":715,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":754,"modifier":"EXACT"},"end":{"value":754,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":756,"modifier":"EXACT"},"end":{"value":756,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":761,"modifier":"EXACT"},"end":{"value":761,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":786,"modifier":"EXACT"},"end":{"value":786,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":787,"modifier":"EXACT"},"end":{"value":787,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":788,"modifier":"EXACT"},"end":{"value":788,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":789,"modifier":"EXACT"},"end":{"value":789,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":829,"modifier":"EXACT"},"end":{"value":829,"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":829,"modifier":"EXACT"},"end":{"value":829,"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":829,"modifier":"EXACT"},"end":{"value":829,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":841,"modifier":"EXACT"},"end":{"value":841,"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":843,"modifier":"EXACT"},"end":{"value":843,"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":843,"modifier":"EXACT"},"end":{"value":843,"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"}}],"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":"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":"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":"UP000053171"}],"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"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51983.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51983.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000009","properties":[{"key":"ProteinId","value":"OAX51983.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_064725352.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JAIUDH010000001.1"}]},{"database":"AlphaFoldDB","id":"A0A199NTQ9","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":"UP000053171","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":"2"}]},{"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"}]}],"sequence":{"value":"MPRRTDLHSVLVIGSGPIVIGQAAEFDYSGTQALRVLKDEGIRVILVNSNPATIMTDPEFADATYIEPITPETVEKIIAKERPDAILPTLGGQTALNTAIALDERGALERYGVELIGANIAAINLGEDREAFKGVVERCGAESARSEIVHSMDEALAAAERLGYPMVVRPSFTMGGLGSGMAYDEADLHRIAGAGIQYSPTSEVLLEESILGWKEYELEMMRDRNDNVVVVCSIENFDPVGVHTGDSITVAPALTLTDREYQKMRDVAIAVIREVGVDTGGCNIQFAVDPATGRVVVIEMNPRVSRSSALASKATGFPIAKIATKLSLGYTLDEIPNDITRKTPASFEPTLDYVVVKVPRFAFEKFPAADPTLTTTMKSVGEAMALGRSFTEALQKAMRSLEQKDGAFDFAAETLDRDALDELVEATRTPTTQRIHQVRRALAAGAGVERMYEATGIDPWFLDQLQLLNEVAERVRADPDLTPDTLREAKRHGFSDAQIAAIAHTREDVVRGVRHALGIRPVFKTVDTCAAEFEAFTPYHYSAYDQEDEVAPHEGESIMILGSGPNRIGQGIEFDYSCVHASMVLREAGYETVMVNCNPETVSTDYDVSTRLYFEPLTLEDVLEVIEEERRTGGLKGVYVQLGGQTPLKLAAQLQEAGVPILGTTPEAIDLAEDRGEFAQVLERAGLISPKNGTASTFAEAKRIADGIGYPVLVRPSYVLGGRGMEIVYDEASLAAYLEHATEVSPSQPALIDKFLEDAIEIDVDALFDGTDLYMGGVMEHIEEAGIHSGDSACTLPPVTLGPDVIDRVCAATRGIAEGVGVRGLINIQFAVASDILYVIEANPRASRTVPFVSKATGVQLAKAAALIGVGRSIRELTEHGVLPSHMDGARIPEGTAIAVKEAVLPFSRFRTPEGVVVDALLSPEMRSTGEVMGLDPYFDTAFAKGQAAVGSPLPTEGRVFVSVANRDKRSAVVYVKMLQDLGFEIVTTGGTAQVLRRNGIPCTVVPKLGDVAEGERSVVDMIREGQIDLIFNTPSGGSARGDGYEIRAAATSVGVPLMTTLSQFGASIQSIAAQREHSWDVLSLQEHEASLAQRAQEAPAAEGDRA","length":1107,"molWeight":119048,"crc64":"2D75D6298698A993","md5":"1BCE65A1B79F24C4FB1398EDD0A79352"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":38},"uniParcId":"UPI0007E5CF32"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NU65","uniProtkbId":"A0A199NU65_9MICC","entryAudit":{"firstPublicDate":"2016-10-05","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-10-05","entryVersion":34,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52138.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Phosphoribosyl-AMP cyclohydrolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"PRA-CH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"3.5.4.19"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"hisI"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52138.1"}],"value":"AN277_0204805"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20049"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58435"},{"database":"ChEBI","id":"CHEBI:59457"}],"ecNumber":"3.5.4.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000024"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22828"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:59457"},{"database":"ChEBI","id":"CHEBI:73183"}],"ecNumber":"3.6.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001460"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005204"}],"value":"Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005169"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Belongs to the PRA-CH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007731"}],"value":"In the C-terminal section; belongs to the PRA-PH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008299"}],"value":"In the N-terminal section; belongs to the PRA-CH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52138.1"}],"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":43,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Phosphoribosyl-AMP cyclohydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01502"}]},{"type":"Region","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":92,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023102"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0368","category":"Biological process","name":"Histidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52138.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52138.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000007","properties":[{"key":"ProteinId","value":"OAX52138.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_064725239.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_LJBJ02000007.1"}]},{"database":"AlphaFoldDB","id":"A0A199NU65","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00031","properties":[{"key":"RectionId","value":"UER00008"}]},{"database":"Proteomes","id":"UP000053171","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:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004635","properties":[{"key":"GoTerm","value":"F:phosphoribosyl-AMP cyclohydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004636","properties":[{"key":"GoTerm","value":"F:phosphoribosyl-ATP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000105","properties":[{"key":"GoTerm","value":"P:L-histidine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.10.20.810:FF:000001","properties":[{"key":"EntryName","value":"Histidine biosynthesis bifunctional protein HisIE"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.810","properties":[{"key":"EntryName","value":"Phosphoribosyl-AMP cyclohydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01021","properties":[{"key":"EntryName","value":"HisI"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR026660","properties":[{"key":"EntryName","value":"PRA-CH"}]},{"database":"InterPro","id":"IPR002496","properties":[{"key":"EntryName","value":"PRib_AMP_CycHydrolase_dom"}]},{"database":"InterPro","id":"IPR038019","properties":[{"key":"EntryName","value":"PRib_AMP_CycHydrolase_sf"}]},{"database":"NCBIfam","id":"NF000768","properties":[{"key":"EntryName","value":"hisI"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42945","properties":[{"key":"EntryName","value":"HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42945:SF11","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYL-AMP CYCLOHYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01502","properties":[{"key":"EntryName","value":"PRA-CH"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF141734","properties":[{"key":"EntryName","value":"HisI-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNTPETPAQQPELDPAIRERLKLDPQGLVAAIIQQHDTGEVLMLGWMDPEALRRTLTTGRVTFWSRSRRAYWRKGDTSGHCQYVRSVALDCDGDALLVRVEQIGAACHTGTRTCFDADPLPAVVGDPQQTPADPAAPAADRQPPKEDRP","length":149,"molWeight":16396,"crc64":"B04725D285720CEB","md5":"463582B38FEA48338836A0884E564175"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":6},"uniParcId":"UPI0007E65CEB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NUL1","uniProtkbId":"A0A199NUL1_9MICC","entryAudit":{"firstPublicDate":"2016-11-02","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-11-02","entryVersion":49,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52774.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"pfkA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52774.1"}],"value":"AN277_0202180"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","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":"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":"OAX52774.1"}],"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":298,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"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:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI: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":126,"modifier":"EXACT"},"end":{"value":128,"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":163,"modifier":"EXACT"},"end":{"value":163,"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":170,"modifier":"EXACT"},"end":{"value":172,"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":222,"modifier":"EXACT"},"end":{"value":222,"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":266,"modifier":"EXACT"},"end":{"value":266,"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":272,"modifier":"EXACT"},"end":{"value":275,"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":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Important for substrate specificity; cannot use PPi as phosphoryl donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"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:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"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-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52774.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52774.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000002","properties":[{"key":"ProteinId","value":"OAX52774.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684619.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A199NUL1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"37923.BK826_07895","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61262037","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_01545","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802503at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000053171","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:InterPro"}]},{"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":"MKIGLLTSGGDCPGLNAVIRGAVLNGVKTYDDEFVGFRDGWRGLVEDDIMDLPRTKVRGLARTGGTILGTSRTNPYDGPHGGPENISIVLEKNQIDAVVAIGGEGTLAGARRLADAGLPVVGVPKTIDNDLNGTDYTFGFDTAVQIATDAMDRLRTTGESHHRCMVAEVMGRHVGWIALHSGMAAGAHAVLIPEQQVPMTQVAEWAKEVHDRGRSPLVVVAEGFIPEGFDEVMHDKGVEKDGRPRLGGIGEYVTREIEKLTGIETRNTTLGHIQRGGSPTSFDRVLATRFGMNVVDLVHDKEWGKMVALHGTDVVRVGFHEALDSGLKEVPQDRWEEAKTLFGR","length":344,"molWeight":37159,"crc64":"4F217EC3E3D98A5F","md5":"111FFAE1C31A53129BDCF0AD991C93DF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":10,"Site":1},"uniParcId":"UPI0006EBA279"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A199NVE7","uniProtkbId":"A0A199NVE7_9MICC","entryAudit":{"firstPublicDate":"2016-11-02","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2016-11-02","entryVersion":47,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52696.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional NAD(P)H-hydrate repair enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Nicotinamide nucleotide repair protein"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"NAD(P)H-hydrate epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"5.1.99.6"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52696.1"}],"value":"AN277_0201730"}]}],"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":"OAX52696.1"}],"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":6,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":541,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":62,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"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":177,"modifier":"EXACT"},"end":{"value":177,"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":273,"modifier":"EXACT"},"end":{"value":273,"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":327,"modifier":"EXACT"},"end":{"value":327,"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":376,"modifier":"EXACT"},"end":{"value":376,"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":444,"modifier":"EXACT"},"end":{"value":448,"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":473,"modifier":"EXACT"},"end":{"value":473,"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":474,"modifier":"EXACT"},"end":{"value":474,"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":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52696.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52696.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000002","properties":[{"key":"ProteinId","value":"OAX52696.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684543.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_LJBJ02000002.1"}]},{"database":"AlphaFoldDB","id":"A0A199NVE7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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":"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":"MVLNAYTAAQITATEKPHLAAGAPLMARAAHALAVEAARMLRHRPSGAYGADVVVLAGAGNNGGDALHAGALLRARGARVTAVLTGSEAHEEGLAALRGAGGFVLTLSEAGAQEGARAAAGADLIIDGMLGTGGRGGLREAPAELVRRIQESTGRNTEHRSAGGWARPLVLACDVPSGLDATTGAVAGPVLAADATVTFIGIKTGLLATPKPSLVGRIRCADLGIGADLPAPALREAEDEDFPRYWSVPVEGDQKYSRGVLGTVAGSDQYPGAGLMCVHAAVRAGAGMVRFVGGDALASALAVSTPEAVRSEHVGAHRVQAWAVGSGATDRAQQAQVEQALDAGVPVLADAAAIEMLAHRAADGDPAPAHVLLTPHAGELAQALEWVARLAPERGERLVRAAREAGLPEDEEVQTSPSRTQIEAAPFVWVRAAREALGGTLLLKGTTTLVAAPDGTVWAHRGNSAWLSTAGSGDTLSGILGAGLAAHRARVEAGRAEGADGEWAGVAAAGLLVQRGISTAAPGPVPPTVAAERIPEVLGRLADGQ","length":545,"molWeight":55040,"crc64":"0C2DB4D9D95F1142","md5":"26BE83CFE7410D16C9BFBA9378BDDB70"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI0006EBD6DB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2U874","uniProtkbId":"A0A0Q2U874_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-01-20","entryVersion":48,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52905.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"Ribosomal RNA small subunit methyltransferase A"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"2.1.1.182"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"16S rRNA dimethyladenosine transferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"16S rRNA dimethylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"S-adenosylmethionine-6-N', N'-adenosyl(rRNA) dimethyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"rsmA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"ksgA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52905.1"}],"value":"AN277_0200620"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"Specifically dimethylates two adjacent adenosines (A1518 and A1519) in the loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S particle. May play a critical role in biogenesis of 30S subunits"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(1518)/adenosine(1519) in 16S rRNA + 4 S-adenosyl-L-methionine = N(6)-dimethyladenosine(1518)/N(6)-dimethyladenosine(1519) in 16S rRNA + 4 S-adenosyl-L-homocysteine + 4 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19609"},{"database":"Rhea","id":"RHEA-COMP:10232"},{"database":"Rhea","id":"RHEA-COMP:10233"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74493"}],"ecNumber":"2.1.1.182","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. rRNA adenine N(6)-methyltransferase family. RsmA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52905.1"}],"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":37,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Ribosomal RNA adenine methylase transferase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00650"}]},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01026"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01026"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01026"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01026"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01026"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01026"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00607"}],"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_00607"}],"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_00607"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52905.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52905.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52905.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684329.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JALXSL010000065.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2U874","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.837","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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:0052908","properties":[{"key":"GoTerm","value":"F:16S rRNA (adenine(1518)-N(6)/adenine(1519)-N(6))-dimethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0031167","properties":[{"key":"GoTerm","value":"P:rRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.8.100:FF:000003","properties":[{"key":"EntryName","value":"Ribosomal RNA small subunit methyltransferase A"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.150:FF:000023","properties":[{"key":"EntryName","value":"Ribosomal RNA small subunit methyltransferase A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.100","properties":[{"key":"EntryName","value":"Ribosomal RNA adenine dimethylase-like, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00607","properties":[{"key":"EntryName","value":"16SrRNA_methyltr_A"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001737","properties":[{"key":"EntryName","value":"KsgA/Erm"}]},{"database":"InterPro","id":"IPR023165","properties":[{"key":"EntryName","value":"rRNA_Ade_diMease-like_C"}]},{"database":"InterPro","id":"IPR020596","properties":[{"key":"EntryName","value":"rRNA_Ade_Mease_Trfase_CS"}]},{"database":"InterPro","id":"IPR020598","properties":[{"key":"EntryName","value":"rRNA_Ade_methylase_Trfase_N"}]},{"database":"InterPro","id":"IPR011530","properties":[{"key":"EntryName","value":"rRNA_adenine_dimethylase"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"NCBIfam","id":"TIGR00755","properties":[{"key":"EntryName","value":"ksgA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11727","properties":[{"key":"EntryName","value":"DIMETHYLADENOSINE TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11727:SF7","properties":[{"key":"EntryName","value":"DIMETHYLADENOSINE TRANSFERASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00398","properties":[{"key":"EntryName","value":"RrnaAD"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00650","properties":[{"key":"EntryName","value":"rADc"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01131","properties":[{"key":"EntryName","value":"RRNA_A_DIMETH"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51689","properties":[{"key":"EntryName","value":"SAM_RNA_A_N6_MT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTAPLLGPAEIRQMAARAGIQPTKTLGQNFVIDANTIRRIVTTARVDAGEVVLEVGPGLGSLTLGLLDAAARVVAVEIDPPLAAQLPETVRRFRPESADRLDVVLHDALTVTELPAQPDALVANLPYNVAVPVLLHLLAQFPSITHGLVMVQDEVADRLAAAPGSKVYGVPSVKARWFGEVSKAGVIGTNVFWPAPKIRSGLVAFRRYERPLAEDVTRREVFAVIDAAFAQRRKTLRAALAGWAGSAGRAGEILTAAGIDPTLRGERLGIEGFIGIARAGRC","length":283,"molWeight":30024,"crc64":"9FD52544AE9D8192","md5":"4A1DA379C2D5009B569E75E0E33FDAEE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":6},"uniParcId":"UPI0006EB98B4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2URJ6","uniProtkbId":"A0A0Q2URJ6_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2016-01-20","entryVersion":39,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52758.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Isopentenyl-diphosphate delta-isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"IPP isomerase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"5.3.3.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Isopentenyl diphosphate:dimethylallyl diphosphate isomerase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Isopentenyl pyrophosphate isomerase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Type 2 isopentenyl diphosphate isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"IDI-2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"fni"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52758.1"}],"value":"AN277_0202090"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Involved in the biosynthesis of isoprenoids. Catalyzes the 1,3-allylic rearrangement of the homoallylic substrate isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate (DMAPP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"isopentenyl diphosphate = dimethylallyl diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23284"},{"database":"ChEBI","id":"CHEBI:57623"},{"database":"ChEBI","id":"CHEBI:128769"}],"ecNumber":"5.3.3.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"NADPH","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57783"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025810"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Homooctamer. Dimer of tetramers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Belongs to the IPP isomerase type 2 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52758.1"}],"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":163,"modifier":"EXACT"},"end":{"value":349,"modifier":"EXACT"}},"description":"FMN-dependent dehydrogenase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01070"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":5,"modifier":"EXACT"},"end":{"value":6,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":274,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":294,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0414","category":"Biological process","name":"Isoprene biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00354"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52758.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52758.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000002","properties":[{"key":"ProteinId","value":"OAX52758.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684603.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP113782.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2URJ6","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.819","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004452","properties":[{"key":"GoTerm","value":"F:isopentenyl-diphosphate delta-isomerase 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:0070402","properties":[{"key":"GoTerm","value":"F:NADPH binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016491","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008299","properties":[{"key":"GoTerm","value":"P:isoprenoid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00354","properties":[{"key":"EntryName","value":"Idi_2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR000262","properties":[{"key":"EntryName","value":"FMN-dep_DH"}]},{"database":"InterPro","id":"IPR011179","properties":[{"key":"EntryName","value":"IPdP_isomerase"}]},{"database":"NCBIfam","id":"TIGR02151","properties":[{"key":"EntryName","value":"IPP_isom_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43665","properties":[{"key":"EntryName","value":"ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43665:SF1","properties":[{"key":"EntryName","value":"ISOPENTENYL-DIPHOSPHATE DELTA-ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01070","properties":[{"key":"EntryName","value":"FMN_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF003314","properties":[{"key":"EntryName","value":"IPP_isomerase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51395","properties":[{"key":"EntryName","value":"FMN-linked oxidoreductases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGQRKDDHLHLAAGQQRQLHRDPVPTDWDDVRLLHEALAGIEAEDVDLSVTLPWAGERGPVRWPVPFYLNGMTGGSEHTGAVNAALGEAAAATGLPIATGSMSMYLKDPSTLPSFRVLREANPEGFVMANLSAEATPDQARRVVEALEADALQIHINAVQETVMPEGARGFSAWCDGIAALAEQLPVPVVVKEVGCGMTRTTLAKLARAGVQLVDVAGRGGTDFARIENDRRDGRDYAFLQGFGQSAPMVLLDALGARAGTRLPALLASGGVRHPYDVVRGLALGARAVGVAGTFLHAVLAEDPAGSAGPVAPDGAERLTGLIRAWTERLRELCALLGVRTPAELTRTDVLVEGRLAHAAALRGADLAALAARSETTAFEEDRA","length":385,"molWeight":40554,"crc64":"6DB34378DCC704A3","md5":"BFFB49E749228D14D8715CA252040358"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":10},"uniParcId":"UPI0006EB91C6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2URM5","uniProtkbId":"A0A0Q2URM5_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":53,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52805.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"GMP synthase [glutamine-hydrolyzing]"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"6.3.5.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"GMP synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Glutamine amidotransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52805.1"}],"value":"guaA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52805.1"}],"value":"AN277_0201635"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002332"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Catalyzes the synthesis of GMP from XMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XMP + L-glutamine + ATP + H2O = GMP + L-glutamate + AMP + diphosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11680"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:58115"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.5.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005153"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52805.1"}],"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":196,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"GMPS ATP-PPase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51553"}]},{"type":"Active site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":171,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00886"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0332","category":"Biological process","name":"GMP biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00344"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52805.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52805.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000002","properties":[{"key":"ProteinId","value":"OAX52805.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A0Q2URM5","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_01040","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.909","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00189","properties":[{"key":"RectionId","value":"UER00296"}]},{"database":"Proteomes","id":"UP000053171","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003921","properties":[{"key":"GoTerm","value":"F:GMP synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01742","properties":[{"key":"EntryName","value":"GATase1_GMP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01997","properties":[{"key":"EntryName","value":"GMP_synthase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.300.10:FF:000002","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000001","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000001","properties":[{"key":"EntryName","value":"GMP synthase [glutamine-hydrolyzing]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00344","properties":[{"key":"EntryName","value":"GMP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001962","properties":[{"key":"EntryName","value":"Asn_synthase"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR001674","properties":[{"key":"EntryName","value":"GMP_synth_C"}]},{"database":"InterPro","id":"IPR004739","properties":[{"key":"EntryName","value":"GMP_synth_GATase"}]},{"database":"InterPro","id":"IPR022955","properties":[{"key":"EntryName","value":"GMP_synthase"}]},{"database":"InterPro","id":"IPR025777","properties":[{"key":"EntryName","value":"GMPS_ATP_PPase_dom"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF000848","properties":[{"key":"EntryName","value":"guaA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00884","properties":[{"key":"EntryName","value":"guaA_Cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00888","properties":[{"key":"EntryName","value":"guaA_Nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922:SF2","properties":[{"key":"EntryName","value":"GMP SYNTHASE [GLUTAMINE-HYDROLYZING]"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11922","properties":[{"key":"EntryName","value":"GMP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00733","properties":[{"key":"EntryName","value":"Asn_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00958","properties":[{"key":"EntryName","value":"GMP_synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00097","properties":[{"key":"EntryName","value":"ANTSNTHASEII"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"PRINTS","id":"PR00096","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54810","properties":[{"key":"EntryName","value":"GMP synthetase C-terminal dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51553","properties":[{"key":"EntryName","value":"GMPS_ATP_PPASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEDRPVLVVDYGAQYAQLIARRVRDARVYSEIVPHTMSAQDMLAKNPAAIILSGGPASVYAPEAPAGDPALFEAGVPVFGICYGFQVMARALGGTVARTGLREYGATQATLSGGASFLAGTPVTQNVWMSHGDSVTEAPAGFEVLATTDGAPVAAFVDADRRLAGVQWHPEVRHSDYGQQVLESFLFEVAGLEPTWTTGNVIEEQVERIRAQVGDAKVICALSGGVDSSVAAALVHRAVGDQLTCFFIDHGLLREGEREQVEQDYAETMGIRVVTIDESERFLSALEGVTDPETKRKTIGREFIRSFEDAQRKLVAEIEGPAEDIRFLVQGTLYPDVVESGGGEGAANIKSHHNVGGLPEDLQFELVEPLRTLFKDEVRAIGRQLGVPEKIVARQPFPGPGLGIRVIGEVTRENLRILRAADAIARAELTRAGLDEEVWQMPVVLLSQVRSVGVQGDGRTYGHPIVLRPVSSEDAMTADWSRLPYDLLARISNRITNEVEEVNRVVLDVTSKPPGTIEWE","length":520,"molWeight":56384,"crc64":"E5B121BC53657BB3","md5":"2625B607401633BE28FF7CA2C33F8094"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":3,"Binding site":1},"uniParcId":"UPI0006EBD484"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2URX4","uniProtkbId":"A0A0Q2URX4_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-01-20","entryVersion":56,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52976.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Uridylate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"UK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"2.7.4.22"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Uridine monophosphate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"UMP kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"UMPK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52976.1"}],"value":"pyrH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52976.1"}],"value":"AN277_0201070"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Catalyzes the reversible phosphorylation of UMP to UDP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UMP + ATP = UDP + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24400"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57865"},{"database":"ChEBI","id":"CHEBI:58223"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.22","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047767"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Inhibited by UTP"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004791"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007614"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Belongs to the UMP kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52976.1"}],"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":14,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"Aspartate/glutamate/uridylate kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00696"}]},{"type":"Binding site","location":{"start":{"value":18,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57865"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"UMP","id":"ChEBI:CHEBI:57865"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57865"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"UMP","id":"ChEBI:CHEBI:57865"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57865"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"UMP","id":"ChEBI:CHEBI:57865"}},{"type":"Binding site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"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_01220"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52976.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52976.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52976.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684400.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2URX4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"37923.BK826_10235","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263155","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_07135","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.982","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00275"}]},{"database":"Proteomes","id":"UP000053171","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:0033862","properties":[{"key":"GoTerm","value":"F:UMP kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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:0006225","properties":[{"key":"GoTerm","value":"P:UDP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04254","properties":[{"key":"EntryName","value":"AAK_UMPK-PyrH-Ec"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1160.10:FF:000001","properties":[{"key":"EntryName","value":"Uridylate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1160.10","properties":[{"key":"EntryName","value":"Acetylglutamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01220_B","properties":[{"key":"EntryName","value":"PyrH_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036393","properties":[{"key":"EntryName","value":"AceGlu_kinase-like_sf"}]},{"database":"InterPro","id":"IPR001048","properties":[{"key":"EntryName","value":"Asp/Glu/Uridylate_kinase"}]},{"database":"InterPro","id":"IPR011817","properties":[{"key":"EntryName","value":"Uridylate_kinase"}]},{"database":"InterPro","id":"IPR015963","properties":[{"key":"EntryName","value":"Uridylate_kinase_bac"}]},{"database":"NCBIfam","id":"TIGR02075","properties":[{"key":"EntryName","value":"pyrH_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42833","properties":[{"key":"EntryName","value":"URIDYLATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42833:SF4","properties":[{"key":"EntryName","value":"URIDYLATE KINASE PUMPKIN, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00696","properties":[{"key":"EntryName","value":"AA_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005650","properties":[{"key":"EntryName","value":"Uridylate_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53633","properties":[{"key":"EntryName","value":"Carbamate kinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPDETPRLAPTRRRVLLKLSGEVFGGGRVGIDTGVVRRIAEQIASTVGQAETAIVVGGGNFFRGAELSVAGMDRSRADYMGMLGTVMNSLALQDFLEQAGVETRVQSAIQMAQVAENYIPRRAIRHLEKDRVVIFGAGAGLPYFSTDTVAAQRALEVHADEVLVAKNGVDGVYTADPKTNPDAKRLRHLTYDEALQRDIRVMDQTAFSLCRDNDVTMRVFGMEGEGNVASAILGEQIGTLVTA","length":243,"molWeight":26240,"crc64":"CC5490D89357B8F8","md5":"53D5E76EAD180C4D0DB8F14FAF15AC4A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":9},"uniParcId":"UPI0006EB9F4E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2XHP4","uniProtkbId":"A0A0Q2XHP4_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":50,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51740.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01389"}],"value":"DNA helicase RecQ"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01389"}],"value":"5.6.2.4"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51740.1"}],"value":"AN277_0207275"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005446"}],"value":"Belongs to the helicase family. RecQ subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51740.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51192"}]},{"type":"Domain","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"Helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51194"}]},{"type":"Domain","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"Rhodanese","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50206"}]},{"type":"Domain","location":{"start":{"value":530,"modifier":"EXACT"},"end":{"value":601,"modifier":"EXACT"}},"description":"HRDC","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50967"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51740.1"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00541"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51740.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX51740.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000013","properties":[{"key":"ProteinId","value":"OAX51740.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684717.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_LDRG01000205.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2XHP4","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.355","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"Proteomes","id":"UP000053171","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0043590","properties":[{"key":"GoTerm","value":"C:bacterial nucleoid"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030894","properties":[{"key":"GoTerm","value":"C:replisome"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009378","properties":[{"key":"GoTerm","value":"F:four-way junction helicase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016787","properties":[{"key":"GoTerm","value":"F:hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003676","properties":[{"key":"GoTerm","value":"F:nucleic acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006260","properties":[{"key":"GoTerm","value":"P:DNA replication"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009432","properties":[{"key":"GoTerm","value":"P:SOS response"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd17920","properties":[{"key":"EntryName","value":"DEXHc_RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18794","properties":[{"key":"EntryName","value":"SF2_C_RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.80:FF:000002","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000156","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase recQ"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000296","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase RecQ"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.80","properties":[{"key":"EntryName","value":"HRDC domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011545","properties":[{"key":"EntryName","value":"DEAD/DEAH_box_helicase_dom"}]},{"database":"InterPro","id":"IPR004589","properties":[{"key":"EntryName","value":"DNA_helicase_ATP-dep_RecQ"}]},{"database":"InterPro","id":"IPR006293","properties":[{"key":"EntryName","value":"DNA_helicase_ATP-dep_RecQ_bac"}]},{"database":"InterPro","id":"IPR014001","properties":[{"key":"EntryName","value":"Helicase_ATP-bd"}]},{"database":"InterPro","id":"IPR001650","properties":[{"key":"EntryName","value":"Helicase_C-like"}]},{"database":"InterPro","id":"IPR010997","properties":[{"key":"EntryName","value":"HRDC-like_sf"}]},{"database":"InterPro","id":"IPR002121","properties":[{"key":"EntryName","value":"HRDC_dom"}]},{"database":"InterPro","id":"IPR044876","properties":[{"key":"EntryName","value":"HRDC_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR032284","properties":[{"key":"EntryName","value":"RecQ_Zn-bd"}]},{"database":"InterPro","id":"IPR001763","properties":[{"key":"EntryName","value":"Rhodanese-like_dom"}]},{"database":"InterPro","id":"IPR018982","properties":[{"key":"EntryName","value":"RQC_domain"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"NCBIfam","id":"TIGR01389","properties":[{"key":"EntryName","value":"recQ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00614","properties":[{"key":"EntryName","value":"recQ_fam"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13710:SF105","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE Q1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13710","properties":[{"key":"EntryName","value":"DNA HELICASE RECQ FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00270","properties":[{"key":"EntryName","value":"DEAD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00271","properties":[{"key":"EntryName","value":"Helicase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00570","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16124","properties":[{"key":"EntryName","value":"RecQ_Zn_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09382","properties":[{"key":"EntryName","value":"RQC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00487","properties":[{"key":"EntryName","value":"DEXDc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00490","properties":[{"key":"EntryName","value":"HELICc"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00341","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00956","properties":[{"key":"EntryName","value":"RQC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47819","properties":[{"key":"EntryName","value":"HRDC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51192","properties":[{"key":"EntryName","value":"HELICASE_ATP_BIND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51194","properties":[{"key":"EntryName","value":"HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50967","properties":[{"key":"EntryName","value":"HRDC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50206","properties":[{"key":"EntryName","value":"RHODANESE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEVLRTVFGYDSFRGDQAAIIHRVTAGGDAVVLMPTGGGKSLCYQIPAILREGTGVVVSPLIALMQDQVEALEAVGIRAAYLNSSLDLEQARTVERGLLAGDYDLVYLAPERLVQERTLDLLGRTRLALFAIDEAHCVSQWGHDFRKDYLGLSVLADRFPGVPRIALTATATAATHRELTERLALQGAEHFVASFDRPNIQYRITEKNSARQQLLRLIRTEHDGEAGIVYCLSRRRVEQTAAWLRDQGVDAMAYHAGMSEAQRAEGQRRFLREDGVVMVATIAFGMGIDKPDVRFVAHLDLPKSVEGYYQETGRAGRDGLPATAWLAYGLQDVVQLRRMIDESEGSEEHRRVQRAHLDAMLALCETTDCRRVQILRYFGQETGPCGNCDTCLNPPASWDATVPVQKLLSAVVRLDRERGQRFGAQQIIAVLRGTPNERSTRSRHDQLSVWGIGADLSETAWRAVIRQLLARGILAATGEYGTLELAGPAGPILRGEQTVTLRVTPERTAKVARSRTGATGSRSTVAAELGEEDREVFERLRAWRTEQAREQGVPAYVVFPDATLIELARARPSSSAALAEVSGVGAKKLERYGEAVLRVLA","length":601,"molWeight":66164,"crc64":"FB691569AF7AEB6B","md5":"1957DCC63A75AA089AF82778C16C2983"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":4},"uniParcId":"UPI0006EB9123"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2XHZ0","uniProtkbId":"A0A0Q2XHZ0_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-01-20","entryVersion":54,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52704.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015972"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"DNA-directed RNA polymerase subunit alpha"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"RNAP subunit alpha"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012418"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"2.7.7.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"RNA polymerase subunit alpha"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032524"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Transcriptase subunit alpha"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"rpoA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52704.1"}],"value":"AN277_0201795"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"DNA-dependent RNA polymerase catalyzes the transcription of DNA into RNA using the four ribonucleoside triphosphates as substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"RNA(n) + a ribonucleoside 5'-triphosphate = RNA(n+1) + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21248"},{"database":"Rhea","id":"RHEA-COMP:14527"},{"database":"Rhea","id":"RHEA-COMP:17342"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61557"},{"database":"ChEBI","id":"CHEBI:140395"}],"ecNumber":"2.7.7.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Homodimer. The RNAP catalytic core consists of 2 alpha, 1 beta, 1 beta' and 1 omega subunit. When a sigma factor is associated with the core the holoenzyme is formed, which can initiate transcription"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"The N-terminal domain is essential for RNAP assembly and basal transcription, whereas the C-terminal domain is involved in interaction with transcriptional regulators and with upstream promoter elements"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007123"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"value":"Belongs to the RNA polymerase alpha chain family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52704.1"}],"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":18,"modifier":"EXACT"},"end":{"value":227,"modifier":"EXACT"}},"description":"DNA-directed RNA polymerase RpoA/D/Rpb3-type","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00662"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"Alpha N-terminal domain (alpha-NTD)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}]},{"type":"Region","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Alpha C-terminal domain (alpha-CTD)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}]},{"type":"Region","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022478"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0240","category":"Cellular component","name":"DNA-directed RNA polymerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00059"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52704.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52704.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000002","properties":[{"key":"ProteinId","value":"OAX52704.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684551.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2XHZ0","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61261967","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_01195","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.758","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"Proteomes","id":"UP000053171","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003899","properties":[{"key":"GoTerm","value":"F:DNA-directed RNA polymerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046983","properties":[{"key":"GoTerm","value":"F:protein dimerization activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006351","properties":[{"key":"GoTerm","value":"P:DNA-templated transcription"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06928","properties":[{"key":"EntryName","value":"RNAP_alpha_NTD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.20:FF:000001","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.170.120.12:FF:000001","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.20","properties":[{"key":"EntryName","value":"5' to 3' exonuclease, C-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.120.12","properties":[{"key":"EntryName","value":"DNA-directed RNA polymerase, insert domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1360.10","properties":[{"key":"EntryName","value":"RNA polymerase, RBP11-like subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00059","properties":[{"key":"EntryName","value":"RNApol_bact_RpoA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011262","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_insert"}]},{"database":"InterPro","id":"IPR011263","properties":[{"key":"EntryName","value":"DNA-dir_RNA_pol_RpoA/D/Rpb3"}]},{"database":"InterPro","id":"IPR011773","properties":[{"key":"EntryName","value":"DNA-dir_RpoA"}]},{"database":"InterPro","id":"IPR036603","properties":[{"key":"EntryName","value":"RBP11-like"}]},{"database":"InterPro","id":"IPR011260","properties":[{"key":"EntryName","value":"RNAP_asu_C"}]},{"database":"InterPro","id":"IPR036643","properties":[{"key":"EntryName","value":"RNApol_insert_sf"}]},{"database":"NCBIfam","id":"NF003513","properties":[{"key":"EntryName","value":"PRK05182.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003514","properties":[{"key":"EntryName","value":"PRK05182.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003519","properties":[{"key":"EntryName","value":"PRK05182.2-5"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02027","properties":[{"key":"EntryName","value":"rpoA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01000","properties":[{"key":"EntryName","value":"RNA_pol_A_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03118","properties":[{"key":"EntryName","value":"RNA_pol_A_CTD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01193","properties":[{"key":"EntryName","value":"RNA_pol_L"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00662","properties":[{"key":"EntryName","value":"RPOLD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47789","properties":[{"key":"EntryName","value":"C-terminal domain of RNA polymerase alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56553","properties":[{"key":"EntryName","value":"Insert subdomain of RNA polymerase alpha subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55257","properties":[{"key":"EntryName","value":"RBP11-like subunits of RNA polymerase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLIAQRPSLSEEVVAENRSRFTISPLEPGFGYTLGNSLRRTLLSSIPGAAVTSIRIDGVLHEFSTVDGVKEDVTEIILNIKKLSISSENDEPVVAYLRKQGPGEITAADIEVPAGVEIHNPDLHIATLNAQGAFSAELTVERGRGYVSAQQNKAGAGESEIGRIPVDSIYSPVLKVTFRVAATRVEQRTDFDSLVLDVETKEVIAPRDAVASAGNTLVELFGLARELNTEAEGIEVGPSPADESMAQDLALPIEDLDMSVRSYNCLKREGINTVGELVSRSEADLMDIRNFGQKSIDEVKEKLQELGMSLKDSPAGFEPFAAVDEEEDEEETSF","length":334,"molWeight":36162,"crc64":"FBC00D2DF7DC9DB4","md5":"7F64E0D57DE92484AFCED6B383672D6F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Compositional bias":1},"uniParcId":"UPI0006EBB2F2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2XIF7","uniProtkbId":"A0A0Q2XIF7_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":60,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52863.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Bifunctional protein FolD"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Methylenetetrahydrofolate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"1.5.1.5"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Methenyltetrahydrofolate cyclohydrolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"3.5.4.9"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"folD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52863.1"}],"value":"AN277_0200310"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Catalyzes the oxidation of 5,10-methylenetetrahydrofolate to 5,10-methenyltetrahydrofolate and then the hydrolysis of 5,10-methenyltetrahydrofolate to 10-formyltetrahydrofolate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methenyltetrahydrofolate + H2O = (6R)-10-formyltetrahydrofolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23700"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57455"},{"database":"ChEBI","id":"CHEBI:195366"}],"ecNumber":"3.5.4.9","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + NADP(+) = (6R)-5,10-methenyltetrahydrofolate + NADPH","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22812"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57455"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.5.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Belongs to the tetrahydrofolate dehydrogenase/cyclohydrolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52863.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"Tetrahydrofolate dehydrogenase/cyclohydrolase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00763"}]},{"type":"Domain","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":306,"modifier":"EXACT"}},"description":"Tetrahydrofolate dehydrogenase/cyclohydrolase NAD(P)-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02882"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":21,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023102"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0368","category":"Biological process","name":"Histidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01576"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52863.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52863.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52863.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684287.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2XIF7","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263000","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_06360","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.1692","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00193","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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:0004477","properties":[{"key":"GoTerm","value":"F:methenyltetrahydrofolate cyclohydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004488","properties":[{"key":"GoTerm","value":"F:methylenetetrahydrofolate dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01080","properties":[{"key":"EntryName","value":"NAD_bind_m-THF_DH_Cyclohyd"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10860:FF:000005","properties":[{"key":"EntryName","value":"C-1-tetrahydrofolate synthase, cytoplasmic, putative"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, chain A, domain 1"},{"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_01576","properties":[{"key":"EntryName","value":"THF_DHG_CYH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR000672","properties":[{"key":"EntryName","value":"THF_DH/CycHdrlase"}]},{"database":"InterPro","id":"IPR020630","properties":[{"key":"EntryName","value":"THF_DH/CycHdrlase_cat_dom"}]},{"database":"InterPro","id":"IPR020631","properties":[{"key":"EntryName","value":"THF_DH/CycHdrlase_NAD-bd_dom"}]},{"database":"NCBIfam","id":"NF010789","properties":[{"key":"EntryName","value":"PRK14193.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48099:SF5","properties":[{"key":"EntryName","value":"C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR48099","properties":[{"key":"EntryName","value":"C-1-TETRAHYDROFOLATE SYNTHASE, CYTOPLASMIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00763","properties":[{"key":"EntryName","value":"THF_DHG_CYH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02882","properties":[{"key":"EntryName","value":"THF_DHG_CYH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00085","properties":[{"key":"EntryName","value":"THFDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTTQQHSEQEQNGQQGPQILDGRATAAAIKEELREQVAELRARGIVPGLGTVLVGDDPASHSYVKGKHRDCAEVGLASIRRDLPGDITQEELEAVIDELNADPACTGYIVQLPLPQHIDTNAILERIDPAKDADGLHPMNLGRLVLDVYGQGDAPLPCTPAGIVELIRRHGLDVKGKDVAVLGRGITVGRPLGLLLSRRDVNATVTLAHTGTRDLDEVLAAADIIVAAIGVPHAVRAHQVKEGAILLDVGVSRVMDPVTGKKKLVGDISPEAAEKASWLSPNPGGVGPMTRAMLLVNVVQAAQRAADAA","length":310,"molWeight":32651,"crc64":"4A590EEC51AC3F18","md5":"9E4D1D4D739A47E27E42B32DE879AED7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":1,"Binding site":2},"uniParcId":"UPI0006EB8320"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2XIG2","uniProtkbId":"A0A0Q2XIG2_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":48,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52870.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019965"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR01816"}],"value":"Succinate dehydrogenase flavoprotein subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012792"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"value":"1.3.5.1"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52870.1"}],"value":"AN277_0200355"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a quinone + succinate = fumarate + a quinol","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:40523"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:29806"},{"database":"ChEBI","id":"CHEBI:30031"},{"database":"ChEBI","id":"CHEBI:132124"}],"ecNumber":"1.3.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049220"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"value":"Flavinylated by SdhE, about 5% flavinylation occurs in the absence of SdhE."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004894"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"value":"Carbohydrate metabolism; tricarboxylic acid cycle; fumarate from succinate (bacterial route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011591"}],"value":"Part of an enzyme complex containing four subunits: a flavoprotein (FrdA), an iron-sulfur protein (FrdB), and two hydrophobic anchor proteins (FrdC and FrdD)"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004170"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004170"}],"value":"Peripheral membrane protein","id":"SL-9903"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008040"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"value":"Belongs to the FAD-dependent oxidoreductase 2 family. FRD/SDH subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52870.1"}],"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":400,"modifier":"EXACT"}},"description":"FAD-dependent oxidoreductase 2 FAD-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00890"}]},{"type":"Domain","location":{"start":{"value":454,"modifier":"EXACT"},"end":{"value":586,"modifier":"EXACT"}},"description":"Fumarate reductase/succinate dehydrogenase flavoprotein-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02910"}]},{"type":"Active site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000171-1"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Modified residue","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Tele-8alpha-FAD histidine","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-4"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR611281-3"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"id":"KW-0813","category":"Biological process","name":"Transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022532"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362051"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52870.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52870.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52870.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684294.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP113782.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2XIG2","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.1481","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00223","properties":[{"key":"RectionId","value":"UER01005"}]},{"database":"Proteomes","id":"UP000053171","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:0047571","properties":[{"key":"GoTerm","value":"F:3-oxosteroid 1-dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008177","properties":[{"key":"GoTerm","value":"F:succinate dehydrogenase (quinone) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009061","properties":[{"key":"GoTerm","value":"P:anaerobic respiration"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0022900","properties":[{"key":"GoTerm","value":"P:electron transport chain"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006099","properties":[{"key":"GoTerm","value":"P:tricarboxylic acid cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.90.700.10:FF:000001","properties":[{"key":"EntryName","value":"Mitochondrial succinate dehydrogenase flavoprotein subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.50.60:FF:000026","properties":[{"key":"EntryName","value":"Succinate dehydrogenase flavoprotein subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.100:FF:000001","properties":[{"key":"EntryName","value":"Succinate dehydrogenase flavoprotein subunit (SdhA)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.100","properties":[{"key":"EntryName","value":"Fumarate reductase/succinate dehydrogenase flavoprotein-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"4.10.80.40","properties":[{"key":"EntryName","value":"succinate dehydrogenase protein domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.700.10","properties":[{"key":"EntryName","value":"Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003953","properties":[{"key":"EntryName","value":"FAD-dep_OxRdtase_2_FAD-bd"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR003952","properties":[{"key":"EntryName","value":"FRD_SDH_FAD_BS"}]},{"database":"InterPro","id":"IPR037099","properties":[{"key":"EntryName","value":"Fum_R/Succ_DH_flav-like_C_sf"}]},{"database":"InterPro","id":"IPR015939","properties":[{"key":"EntryName","value":"Fum_Rdtase/Succ_DH_flav-like_C"}]},{"database":"InterPro","id":"IPR030664","properties":[{"key":"EntryName","value":"SdhA/FrdA/AprA"}]},{"database":"InterPro","id":"IPR027477","properties":[{"key":"EntryName","value":"Succ_DH/fumarate_Rdtase_cat_sf"}]},{"database":"InterPro","id":"IPR011281","properties":[{"key":"EntryName","value":"Succ_DH_flav_su_fwd"}]},{"database":"InterPro","id":"IPR014006","properties":[{"key":"EntryName","value":"Succ_Dhase_FrdA_Gneg"}]},{"database":"NCBIfam","id":"TIGR01816","properties":[{"key":"EntryName","value":"sdhA_forward"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01812","properties":[{"key":"EntryName","value":"sdhA_frdA_Gneg"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11632","properties":[{"key":"EntryName","value":"SUCCINATE DEHYDROGENASE 2 FLAVOPROTEIN SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11632:SF51","properties":[{"key":"EntryName","value":"SUCCINATE DEHYDROGENASE [UBIQUINONE] FLAVOPROTEIN SUBUNIT, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00890","properties":[{"key":"EntryName","value":"FAD_binding_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02910","properties":[{"key":"EntryName","value":"Succ_DH_flav_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000171","properties":[{"key":"EntryName","value":"SDHA_APRA_LASPO"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00368","properties":[{"key":"EntryName","value":"FADPNR"}]},{"database":"PRINTS","id":"PR00411","properties":[{"key":"EntryName","value":"PNDRDTASEI"}]},{"database":"SUPFAM","id":"SSF51905","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46977","properties":[{"key":"EntryName","value":"Succinate dehydrogenase/fumarate reductase flavoprotein C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56425","properties":[{"key":"EntryName","value":"Succinate dehydrogenase/fumarate reductase flavoprotein, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00504","properties":[{"key":"EntryName","value":"FRD_SDH_FAD_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MQVHKYDVVIVGAGGAGMRAAIEAGQRARTAVLTKIYPTRSHTGAAQGGMCAALANVEEDNWEWHTFDTIKGGDYLVDQDAAEVMAKEAIDAVLDLEKMGLPFNRTPEGKIDQRRFGGHTRDHGKAPVRRACYAADRTGHMILQTLYQNCVKHNVEFFNEYYVLDLIMVEVDGMKRPAGVVSYDLASGEIHVFQAKSVVFASGGTGKIFKTTSNAHTLTGDGMAIAFRNGLPLEDMEFVQFHPTGLAGLGILVSEAARGEGGILRNSEGERFMERYAPTIKDLAPRDIVARSMANEVREGRGCGPNKDYVLLDLTHLEPAHIDAKLPDITEFARTYLGVEPYTEPVPVFPTAHYAMGGIPTTIDAEVYRNSEETVPGLYAAGEVACVSVHGSNRLGTNSLLDINVFGKRAGIKAAEYALEADFLPVPEDATRRTEELLELMRNGHGEEKVGQIRRELQDTMDADMQVFRTEETIHRALDKIAELQDRYTRISIQDQGKRFNLDLLEAVELGFLLELAKVMSVAALHREESRGGHFREDFPNRDDEKFMKHSMAYLDTEAETDHVAGIRLETKPVIFTRYEPMERKY","length":586,"molWeight":65114,"crc64":"1D9826899C14FB43","md5":"BA2386BC60DC46BB9433A08DCD4BC034"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":9,"Modified residue":1},"uniParcId":"UPI0006EB29A9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2XIH2","uniProtkbId":"A0A0Q2XIH2_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":57,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52889.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Fumarate hydratase class II"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Fumarase C"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"4.2.1.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Aerobic fumarase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Iron-independent fumarase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52889.1"}],"value":"aspA"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"fumC"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52889.1"}],"value":"AN277_0200505"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Involved in the TCA cycle. Catalyzes the stereospecific interconversion of fumarate to L-malate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-malate = fumarate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12460"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15589"},{"database":"ChEBI","id":"CHEBI:29806"}],"ecNumber":"4.2.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Carbohydrate metabolism; tricarboxylic acid cycle; (S)-malate from fumarate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"There are 2 substrate-binding sites: the catalytic A site, and the non-catalytic B site that may play a role in the transfer of substrate or product between the active site and the solvent. Alternatively, the B site may bind allosteric effectors"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009084"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"value":"Belongs to the class-II fumarase/aspartase family. Fumarase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52889.1"}],"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":15,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"Fumarate lyase-like N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00206"}]},{"type":"Domain","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":465,"modifier":"EXACT"}},"description":"Fumarase C C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10415"}]},{"type":"Active site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]},{"type":"Active site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"in site B","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":326,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022532"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00743"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52889.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52889.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52889.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684313.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2XIH2","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"37923.BK826_04245","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263040","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_06560","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.220","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9802809at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00223","properties":[{"key":"RectionId","value":"UER01007"}]},{"database":"Proteomes","id":"UP000053171","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:0004333","properties":[{"key":"GoTerm","value":"F:fumarate hydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006106","properties":[{"key":"GoTerm","value":"P:fumarate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006099","properties":[{"key":"GoTerm","value":"P:tricarboxylic acid cycle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.275.10:FF:000001","properties":[{"key":"EntryName","value":"Fumarate hydratase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.200.10:FF:000001","properties":[{"key":"EntryName","value":"Fumarate hydratase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.40.30","properties":[{"key":"EntryName","value":"Fumarase/aspartase (C-terminal domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.200.10","properties":[{"key":"EntryName","value":"Fumarase/aspartase (Central domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.275.10","properties":[{"key":"EntryName","value":"Fumarase/aspartase (N-terminal domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00743","properties":[{"key":"EntryName","value":"FumaraseC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005677","properties":[{"key":"EntryName","value":"Fum_hydII"}]},{"database":"InterPro","id":"IPR024083","properties":[{"key":"EntryName","value":"Fumarase/histidase_N"}]},{"database":"InterPro","id":"IPR018951","properties":[{"key":"EntryName","value":"Fumarase_C_C"}]},{"database":"InterPro","id":"IPR022761","properties":[{"key":"EntryName","value":"Fumarate-Lyase-like_N"}]},{"database":"InterPro","id":"IPR020557","properties":[{"key":"EntryName","value":"Fumarate_lyase_CS"}]},{"database":"InterPro","id":"IPR000362","properties":[{"key":"EntryName","value":"Fumarate_lyase_fam"}]},{"database":"InterPro","id":"IPR008948","properties":[{"key":"EntryName","value":"L-Aspartase-like"}]},{"database":"NCBIfam","id":"NF008909","properties":[{"key":"EntryName","value":"PRK12273.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11444","properties":[{"key":"EntryName","value":"ASPARTATEAMMONIA/ARGININOSUCCINATE/ADENYLOSUCCINATE LYASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11444:SF22","properties":[{"key":"EntryName","value":"FUMARATE HYDRATASE CLASS II"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10415","properties":[{"key":"EntryName","value":"FumaraseC_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00206","properties":[{"key":"EntryName","value":"Lyase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00145","properties":[{"key":"EntryName","value":"ARGSUCLYASE"}]},{"database":"PRINTS","id":"PR00149","properties":[{"key":"EntryName","value":"FUMRATELYASE"}]},{"database":"SUPFAM","id":"SSF48557","properties":[{"key":"EntryName","value":"L-aspartase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00163","properties":[{"key":"EntryName","value":"FUMARATE_LYASES"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDTTEYRIEHDTMGEVQVPKDALYRAQTQRAVQNFPISGSTLESAHIAALALVKKAAAQANEELGVLDADRARAIRDAADAVAAHTYDEHFPIDVFQTGSGTSSNMNANEVLATLATRALEDQGIEVHPNDHVNASQSSNDVFPTSVHVAVTGALIKDLIPALDTLASSLEAKAEQFADVVKSGRTHLMDATPVTLGQEFSGYAAQVRYGIERIEASLPRVAEVPLGGTAVGTGINTPDGFSARVIELLAEETGLPLTEARNHFEAQANRDGLIEASGQLRNIAYSLMKICNDIRWMGSGPNTGLGELHIPDLQPGSSIMPGKVNPVICEAVIQVAAQVIGNDTTIALSSTNGAFELNVGIPVMAKNLLESIRLLANSSRVMAEKMVDGLEANEERARFLAEASPSTVTPMNKLIGYEAAAKIAKHAVAHKTTVREAVEQLGYVERGEVTEQQLDEALDVTRMLGRR","length":468,"molWeight":50005,"crc64":"4F02642F3714A669","md5":"AC0E6EF8EC0440FA6E6EBF70798B31B6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":6,"Site":1},"uniParcId":"UPI0006EB4820"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2XIJ3","uniProtkbId":"A0A0Q2XIJ3_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-01-20","entryVersion":54,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52909.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Ribose-phosphate pyrophosphokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"RPPK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"2.7.6.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"5-phospho-D-ribosyl alpha-1-diphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Phosphoribosyl diphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Phosphoribosyl pyrophosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"P-Rib-PP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"PRPP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"PRPPase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"prs"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52909.1"}],"value":"AN277_0200645"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Involved in the biosynthesis of the central metabolite phospho-alpha-D-ribosyl-1-pyrophosphate (PRPP) via the transfer of pyrophosphoryl group from ATP to 1-hydroxyl of ribose-5-phosphate (Rib-5-P)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribose 5-phosphate + ATP = 5-phospho-alpha-D-ribose 1-diphosphate + AMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15609"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:78346"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.6.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049535"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Binds 2 Mg(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Metabolic intermediate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1-diphosphate from D-ribose 5-phosphate (route I): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"value":"Belongs to the ribose-phosphate pyrophosphokinase family. Class I subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52909.1"}],"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":14,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"Ribose-phosphate pyrophosphokinase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13793"}]},{"type":"Active site","location":{"start":{"value":203,"modifier":"EXACT"},"end":{"value":203,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}]},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}},{"type":"Binding site","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022727"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0545","category":"Biological process","name":"Nucleotide biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00583"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"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_00583"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52909.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52909.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52909.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684333.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2XIJ3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263068","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_06700","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.841","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00087","properties":[{"key":"RectionId","value":"UER00172"}]},{"database":"Proteomes","id":"UP000053171","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:0002189","properties":[{"key":"GoTerm","value":"C:ribose phosphate diphosphokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004749","properties":[{"key":"GoTerm","value":"F:ribose phosphate diphosphokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006015","properties":[{"key":"GoTerm","value":"P:5-phosphoribose 1-diphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006164","properties":[{"key":"GoTerm","value":"P:purine nucleotide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0009156","properties":[{"key":"GoTerm","value":"P:ribonucleoside monophosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000007","properties":[{"key":"EntryName","value":"Ribose-phosphate pyrophosphokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00583_B","properties":[{"key":"EntryName","value":"RibP_PPkinase_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000842","properties":[{"key":"EntryName","value":"PRib_PP_synth_CS"}]},{"database":"InterPro","id":"IPR029099","properties":[{"key":"EntryName","value":"Pribosyltran_N"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR005946","properties":[{"key":"EntryName","value":"Rib-P_diPkinase"}]},{"database":"InterPro","id":"IPR037515","properties":[{"key":"EntryName","value":"Rib-P_diPkinase_bac"}]},{"database":"NCBIfam","id":"NF002320","properties":[{"key":"EntryName","value":"PRK01259.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002844","properties":[{"key":"EntryName","value":"PRK03092.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01251","properties":[{"key":"EntryName","value":"ribP_PPkin"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10210","properties":[{"key":"EntryName","value":"RIBOSE-PHOSPHATE DIPHOSPHOKINASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10210:SF41","properties":[{"key":"EntryName","value":"RIBOSE-PHOSPHATE PYROPHOSPHOKINASE 1, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14572","properties":[{"key":"EntryName","value":"Pribosyl_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13793","properties":[{"key":"EntryName","value":"Pribosyltran_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01400","properties":[{"key":"EntryName","value":"Pribosyltran_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00114","properties":[{"key":"EntryName","value":"PRPP_SYNTHASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSKLTNPGEKKLALVSGRAHPELAEQISKNLGCDLLPVSAYDFANGETYVRYEDSVRGADCFVLQSHPAPINDWLMEQIIMIDALKRASARRITVIAPFYPYARQDKKHKGREPISARLIADLYKTAGADRIMSVDLHTAQIQGFFDGPVDHLMAIPILANYVRDKVGTEGVTVVSPDTGRVRVAEQWAELLGGAPLGFVHKTRDISVPNQAVAKTVVGDVKGRTCVLIDDMIDTAGTISGAVSVLREAGAKDVIIAATHPVFSGPAVERLKDSGATEVVVTNTLPVPEERRFEGLTVLSIAPLIARAIKEVFEDGSVTSLFNGVS","length":327,"molWeight":35255,"crc64":"7A64CE1E937A4B5C","md5":"A1959D15CB5E879A43E7F01F9B64E60B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":7},"uniParcId":"UPI0006EB4C29"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2XIK6","uniProtkbId":"A0A0Q2XIK6_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-01-20","entryVersion":42,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52930.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050038"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Peptidyl-tRNA hydrolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Pth"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013260"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"3.1.1.29"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"pth"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52930.1"}],"value":"AN277_0200760"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Catalyzes the release of premature peptidyl moieties from peptidyl-tRNA molecules trapped in stalled 50S ribosomal subunits, and thus maintains levels of free tRNAs and 50S ribosomes"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Hydrolyzes ribosome-free peptidyl-tRNAs (with 1 or more amino acids incorporated), which drop off the ribosome during protein synthesis, or as a result of ribosome stalling"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N-acyl-L-alpha-aminoacyl-tRNA + H2O = an N-acyl-L-amino acid + a tRNA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:54448"},{"database":"Rhea","id":"RHEA-COMP:10123"},{"database":"Rhea","id":"RHEA-COMP:13883"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:59874"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:138191"}],"ecNumber":"3.1.1.29","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00038063"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"value":"Belongs to the PTH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52930.1"}],"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":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}]},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":17,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17843"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"ligand":{"name":"tRNA","id":"ChEBI:CHEBI:17843"}},{"type":"Site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Discriminates between blocked and unblocked aminoacyl-tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}]},{"type":"Site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Stabilizes the basic form of H active site to accept a proton","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00083"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52930.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52930.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52930.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684354.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2XIK6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263091","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_06815","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.864","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"OrthoDB","id":"9800507at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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:0004045","properties":[{"key":"GoTerm","value":"F:peptidyl-tRNA hydrolase 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:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0072344","properties":[{"key":"GoTerm","value":"P:rescue of stalled cytosolic ribosome"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00462","properties":[{"key":"EntryName","value":"PTH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1470:FF:000001","properties":[{"key":"EntryName","value":"Peptidyl-tRNA hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1470","properties":[{"key":"EntryName","value":"Peptidyl-tRNA hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00083","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001328","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro"}]},{"database":"InterPro","id":"IPR018171","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro_CS"}]},{"database":"InterPro","id":"IPR036416","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro_sf"}]},{"database":"NCBIfam","id":"TIGR00447","properties":[{"key":"EntryName","value":"pth"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR17224","properties":[{"key":"EntryName","value":"PEPTIDYL-TRNA HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR17224:SF1","properties":[{"key":"EntryName","value":"PEPTIDYL-TRNA HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01195","properties":[{"key":"EntryName","value":"Pept_tRNA_hydro"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53178","properties":[{"key":"EntryName","value":"Peptidyl-tRNA hydrolase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01196","properties":[{"key":"EntryName","value":"PEPT_TRNA_HYDROL_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSQTWLVMGLGNPGTQYERTRHNVGQMVIGNLAERMGGTLKRHKAGAMVMEGRAGIGGPRVVLARSTGYMNTSGGPTAGLASFYGIDPEHVIAVHDEIDIPFDAIRLKRGGGEGGHNGLRDITKALGTKEYLRVRVGVGRPPGRMDAADYVLKPFTAAEAKQLPVLVEDAADAVVSLMVHGLTDTQQQYHSRG","length":193,"molWeight":20618,"crc64":"1D5CF08C579B2DB9","md5":"4FCF66FE1B33B6585EA0A8F0B945A031"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":1,"Binding site":4,"Site":2},"uniParcId":"UPI0006EB9CE3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2Y0C6","uniProtkbId":"A0A0Q2Y0C6_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2016-01-20","entryVersion":37,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52996.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Phosphoribosylglycinamide formyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"2.1.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"5'-phosphoribosylglycinamide transformylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"GAR transformylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"GART"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"purN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52996.1"}],"value":"AN277_0200280"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Catalyzes the transfer of a formyl group from 10-formyltetrahydrofolate to 5-phospho-ribosyl-glycinamide (GAR), producing 5-phospho-ribosyl-N-formylglycinamide (FGAR) and tetrahydrofolate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(1)-(5-phospho-beta-D-ribosyl)glycinamide + (6R)-10-formyltetrahydrofolate = N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + (6S)-5,6,7,8-tetrahydrofolate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15053"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:143788"},{"database":"ChEBI","id":"CHEBI:147286"},{"database":"ChEBI","id":"CHEBI:195366"}],"ecNumber":"2.1.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005054"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5-phospho-D-ribosyl)glycinamide (10-formyl THF route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"value":"Belongs to the GART family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52996.1"}],"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":175,"modifier":"EXACT"}},"description":"Formyl transferase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00551"}]},{"type":"Active site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":102,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}]},{"type":"Binding site","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:143788"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"N(1)-(5-phospho-beta-D-ribosyl)glycinamide","id":"ChEBI:CHEBI:143788"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:195366"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"(6R)-10-formyltetrahydrofolate","id":"ChEBI:CHEBI:195366"}},{"type":"Binding site","location":{"start":{"value":83,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:195366"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"(6R)-10-formyltetrahydrofolate","id":"ChEBI:CHEBI:195366"}},{"type":"Binding site","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:195366"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"ligand":{"name":"(6R)-10-formyltetrahydrofolate","id":"ChEBI:CHEBI:195366"}},{"type":"Site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Raises pKa of active site His","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01930"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"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_01930"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52996.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52996.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52996.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A0Q2Y0C6","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.1686","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00126"}]},{"database":"Proteomes","id":"UP000053171","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:0004644","properties":[{"key":"GoTerm","value":"F:phosphoribosylglycinamide formyltransferase 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":"CDD","id":"cd08645","properties":[{"key":"EntryName","value":"FMT_core_GART"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.170:FF:000008","properties":[{"key":"EntryName","value":"Phosphoribosylglycinamide formyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.170","properties":[{"key":"EntryName","value":"Formyl transferase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01930","properties":[{"key":"EntryName","value":"PurN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002376","properties":[{"key":"EntryName","value":"Formyl_transf_N"}]},{"database":"InterPro","id":"IPR036477","properties":[{"key":"EntryName","value":"Formyl_transf_N_sf"}]},{"database":"InterPro","id":"IPR004607","properties":[{"key":"EntryName","value":"GART"}]},{"database":"NCBIfam","id":"TIGR00639","properties":[{"key":"EntryName","value":"PurN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43369","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43369:SF2","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLGLYCINAMIDE FORMYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00551","properties":[{"key":"EntryName","value":"Formyl_trans_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53328","properties":[{"key":"EntryName","value":"Formyltransferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVSGSGTNLQSVLDAVARGELPVQVAAVGADQECRGLERAREAGIETFVLAPRDFPDRPAWNRALEEKLASYAPDLLLFAGFMRIVDAQLVARFERRIVNTHPALLPSFPGAHGVRDALAHGVKITGVTVHLVDSGVDTGPILAQAAVPVLEGDTEQSLHERIKEQERPLLVRTLRELAARA","length":182,"molWeight":19653,"crc64":"B7945F38C50B8277","md5":"6D2A3DFF05840C41B885D49A6F89DA5C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":4,"Site":1},"uniParcId":"UPI0006EBBE13"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2YUE4","uniProtkbId":"A0A0Q2YUE4_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2016-01-20","entryVersion":52,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52686.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}],"value":"Inosine-5'-monophosphate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"IMP dehydrogenase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"IMPD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"IMPDH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}],"value":"1.1.1.205"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"guaB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52686.1"}],"value":"AN277_0201660"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + NAD(+) + H2O = XMP + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11708"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58053"}],"ecNumber":"1.1.1.205","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048028"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Mycophenolic acid (MPA) is a non-competitive inhibitor that prevents formation of the closed enzyme conformation by binding to the same site as the amobile flap. In contrast, mizoribine monophosphate (MZP) is a competitive inhibitor that induces the closed conformation. MPA is a potent inhibitor of mammalian IMPDHs but a poor inhibitor of the bacterial enzymes. MZP is a more potent inhibitor of bacterial IMPDH"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003928"}],"value":"Purine metabolism; XMP biosynthesis via de novo pathway; XMP from IMP: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005502"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003927"}],"value":"Belongs to the IMPDH/GMPR family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52686.1"}],"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":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Thioimidate intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-1"}]},{"type":"Active site","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-1"}]},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-4"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-4"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":315,"modifier":"EXACT"},"end":{"value":315,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-4"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":350,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":397,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":434,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58053"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000130-2"}],"ligand":{"name":"IMP","id":"ChEBI:CHEBI:58053"}},{"type":"Binding site","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":488,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":489,"modifier":"EXACT"},"end":{"value":489,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}},{"type":"Binding site","location":{"start":{"value":490,"modifier":"EXACT"},"end":{"value":490,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103","note":"ligand shared between two tetrameric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023122"}],"id":"KW-0129","category":"Domain","name":"CBS domain"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0332","category":"Biological process","name":"GMP biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01964"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52686.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52686.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000002","properties":[{"key":"ProteinId","value":"OAX52686.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684533.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP113782.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2YUE4","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.903","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00601","properties":[{"key":"RectionId","value":"UER00295"}]},{"database":"Proteomes","id":"UP000053171","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003938","properties":[{"key":"GoTerm","value":"F:IMP dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000166","properties":[{"key":"GoTerm","value":"F:nucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006177","properties":[{"key":"GoTerm","value":"P:GMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006183","properties":[{"key":"GoTerm","value":"P:GTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04601","properties":[{"key":"EntryName","value":"CBS_pair_IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00381","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000003","properties":[{"key":"EntryName","value":"GMP reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01964","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR000644","properties":[{"key":"EntryName","value":"CBS_dom"}]},{"database":"InterPro","id":"IPR046342","properties":[{"key":"EntryName","value":"CBS_dom_sf"}]},{"database":"InterPro","id":"IPR005990","properties":[{"key":"EntryName","value":"IMP_DH"}]},{"database":"InterPro","id":"IPR015875","properties":[{"key":"EntryName","value":"IMP_DH/GMP_Rdtase_CS"}]},{"database":"InterPro","id":"IPR001093","properties":[{"key":"EntryName","value":"IMP_DH_GMPRt"}]},{"database":"NCBIfam","id":"TIGR01302","properties":[{"key":"EntryName","value":"IMP_dehydrog"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11911:SF111","properties":[{"key":"EntryName","value":"INOSINE-5'-MONOPHOSPHATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11911","properties":[{"key":"EntryName","value":"INOSINE-5-MONOPHOSPHATE DEHYDROGENASE RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00571","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00478","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000130","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00116","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM01240","properties":[{"key":"EntryName","value":"IMPDH"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54631","properties":[{"key":"EntryName","value":"CBS-domain pair"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51412","properties":[{"key":"EntryName","value":"Inosine monophosphate dehydrogenase (IMPDH)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51371","properties":[{"key":"EntryName","value":"CBS"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00487","properties":[{"key":"EntryName","value":"IMP_DH_GMP_RED"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQPTALSEDPFGLTGLTYDDVLLLPGNTSVIPSEADTRTRLSRRITLKTPIISAAMDTVTDSRMAIAMARLGGMGVIHRNLSIQDQAEHVDRVKRSESGMITKPVTVGPEATLEELDQLCGHYKVSGLPVVDEDGTLVGIITNRDTRYLPESEFPVRTVREVMTPMPLVTGHEGMSKDEAFALLSSHKIEKLPLVDDAGKLTGLITVKDFTKTEQYPHATKDEEDRLRVGAAVGFFGDGYDRAMALIEAGVDALFIDTANGHSQGVLDMIARLKKDPAADHVDIIGGQAATREGAQAIVDAGADAVKVGVGPGSICTTRIIAGVGVPQITAINESAKATIPAGVPLIADGGLQHSGEIGKALVAGADSVMLGSMLAGCDESPGDLIFVNGKQFKAYRGMGSLGAMQTRGKNVSYSKDRYFQADVKGEDKLIPEGIEGQVAYRGPLAAVLHQLEGGLRQTMFYVGSHDIDELKHKGRFVRITPAGLKESHPHDIMMTVEAPNYRR","length":505,"molWeight":53948,"crc64":"5945873014121EF6","md5":"B1218D44887818D05A48FC38B71AC108"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Active site":2,"Binding site":14},"uniParcId":"UPI0006EBC392"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2YV08","uniProtkbId":"A0A0Q2YV08_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2016-01-20","entryVersion":57,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52963.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Homoserine O-acetyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"HAT"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"2.3.1.31"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Homoserine transacetylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"HTA"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"metXA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52963.1"}],"value":"AN277_0200980"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Transfers an acetyl group from acetyl-CoA to L-homoserine, forming acetyl-L-homoserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-homoserine + acetyl-CoA = O-acetyl-L-homoserine + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13701"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57476"},{"database":"ChEBI","id":"CHEBI:57716"}],"ecNumber":"2.3.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; O-acetyl-L-homoserine from L-homoserine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Belongs to the AB hydrolase superfamily. MetX family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52963.1"}],"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":52,"modifier":"EXACT"},"end":{"value":366,"modifier":"EXACT"}},"description":"AB hydrolase-1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00561"}]},{"type":"Active site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000443-1"}]},{"type":"Active site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000443-1"}]},{"type":"Active site","location":{"start":{"value":361,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000443-1"}]},{"type":"Binding site","location":{"start":{"value":234,"modifier":"EXACT"},"end":{"value":234,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00296"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"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_00296"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52963.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX52963.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX52963.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_055684387.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_CP065738.1"}]},{"database":"AlphaFoldDB","id":"A0A0Q2YV08","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"37923.BK826_03780","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"61263136","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"rkr:I6G21_07040","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.998","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"UniPathway","id":"UPA00051","properties":[{"key":"RectionId","value":"UER00074"}]},{"database":"Proteomes","id":"UP000053171","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:0004414","properties":[{"key":"GoTerm","value":"F:homoserine O-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009092","properties":[{"key":"GoTerm","value":"P:L-homoserine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"Gene3D","id":"3.40.50.1820","properties":[{"key":"EntryName","value":"alpha/beta hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00296","properties":[{"key":"EntryName","value":"MetX_acyltransf"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000073","properties":[{"key":"EntryName","value":"AB_hydrolase_1"}]},{"database":"InterPro","id":"IPR029058","properties":[{"key":"EntryName","value":"AB_hydrolase_fold"}]},{"database":"InterPro","id":"IPR008220","properties":[{"key":"EntryName","value":"HAT_MetX-like"}]},{"database":"NCBIfam","id":"NF001209","properties":[{"key":"EntryName","value":"metX"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32268","properties":[{"key":"EntryName","value":"HOMOSERINE O-ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32268:SF11","properties":[{"key":"EntryName","value":"HOMOSERINE O-ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00561","properties":[{"key":"EntryName","value":"Abhydrolase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000443","properties":[{"key":"EntryName","value":"Homoser_Ac_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53474","properties":[{"key":"EntryName","value":"alpha/beta-Hydrolases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAVAAPVGTRAEGVVRTLGLGPLALESGQVLPAASLAYETWGELAPDASNAVLVLHALTGDTHAAAGRVGPEAPEQTRLAASRPGWWEGLIGPGRAIDTDRYFVVCPNMLGGCDGSTGPCSPGPDGRIWGSRFPRASLRDAVAAEALLADALGIDRWHLVVGGSLGGCRAAEWAVSFPERVRACAVVAAGPAATAEQIAWGHAQALAIRQDPEFRDGDYPLGAGPVRGLELARRIAHITYRSPAELDRRFGRRGQEGTEEDRAVHGRGRYRVESYLDHQGRQLARRFDANAYLGLTEALLGHDLGRGRGGLRAGLARTTCRWTVAAVDSDRLFHPEQSELLAASLPRPVRVRRIASTRGHDGFLTETQQLGRILTETVL","length":380,"molWeight":40540,"crc64":"7FBAB6C155ACDBC6","md5":"2E1896EC6F789D461C40F5FB5D1601D1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":3,"Binding site":2},"uniParcId":"UPI0006EBDA93"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A0Q2YV41","uniProtkbId":"A0A0Q2YV41_9MICC","entryAudit":{"firstPublicDate":"2016-01-20","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-01-20","entryVersion":38,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rothia kristinae","taxonId":37923,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX53002.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Micrococcaceae","Rothia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00018266"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"Cytidine deaminase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012783"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"3.5.4.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032005"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"Cytidine aminohydrolase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX53002.1"}],"value":"AN277_0200390"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003949"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2'-deoxycytidine + H2O + H(+) = 2'-deoxyuridine + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13433"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15698"},{"database":"ChEBI","id":"CHEBI:16450"},{"database":"ChEBI","id":"CHEBI:28938"}],"ecNumber":"3.5.4.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049252"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine + H2O + H(+) = uridine + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16069"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16704"},{"database":"ChEBI","id":"CHEBI:17562"},{"database":"ChEBI","id":"CHEBI:28938"}],"ecNumber":"3.5.4.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049558"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006576"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"value":"Belongs to the cytidine and deoxycytidylate deaminase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX53002.1"}],"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":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-1"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":97,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364006"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000053171"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606262-3"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-3MISLP1OPEHI9","citationType":"submission","authors":["Waterworth S.C.","Walmsley T.A.","Matongo T.","Davies-Coleman M.T.","Dorrington R.A."],"title":"Identification of putative biosynthetic pathways for the production of bioactive secondary metabolites by the marine actinomycete Kocuria kristinae RUTW2-3.","publicationDate":"JUN-2016","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX53002.1"}],"value":"RUTW2-3","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"OAX53002.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"LJBJ02000001","properties":[{"key":"ProteinId","value":"OAX53002.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A0Q2YV41","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|37923.10.peg.590","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"Proteomes","id":"UP000053171","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:0004126","properties":[{"key":"GoTerm","value":"F:cytidine deaminase 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:1901135","properties":[{"key":"GoTerm","value":"P:carbohydrate derivative metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0055086","properties":[{"key":"GoTerm","value":"P:nucleobase-containing small molecule metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0072527","properties":[{"key":"GoTerm","value":"P:pyrimidine-containing compound metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd01283","properties":[{"key":"EntryName","value":"cytidine_deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.140.10","properties":[{"key":"EntryName","value":"Cytidine Deaminase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002125","properties":[{"key":"EntryName","value":"CMP_dCMP_dom"}]},{"database":"InterPro","id":"IPR050202","properties":[{"key":"EntryName","value":"Cyt/Deoxycyt_deaminase"}]},{"database":"InterPro","id":"IPR006262","properties":[{"key":"EntryName","value":"Cyt_deam_tetra"}]},{"database":"InterPro","id":"IPR016193","properties":[{"key":"EntryName","value":"Cytidine_deaminase-like"}]},{"database":"NCBIfam","id":"TIGR01354","properties":[{"key":"EntryName","value":"cyt_deam_tetra"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004064","properties":[{"key":"EntryName","value":"PRK05578.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11644","properties":[{"key":"EntryName","value":"CYTIDINE DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11644:SF2","properties":[{"key":"EntryName","value":"CYTIDINE DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00383","properties":[{"key":"EntryName","value":"dCMP_cyt_deam_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53927","properties":[{"key":"EntryName","value":"Cytidine deaminase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51747","properties":[{"key":"EntryName","value":"CYT_DCMP_DEAMINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGACVGDDPAWPELLAAARDCLERAYCPYSGFPVGAAARTEDGRLVTGANIENAAYGVTLCAECSLVSELFRTGGGRLVRFACVDRTGTPIMPCGRCRQLLSEHAAPGLVVLTPQGELPMAEVLPQAFGPGNLGS","length":135,"molWeight":14040,"crc64":"117CB8FC6C996DDF","md5":"4F4494801677F95CBF55F73970099E8D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":1,"Binding site":4},"uniParcId":"UPI0006EB382A"}}]}