{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q05308","uniProtkbId":"SP1_RARFA","entryAudit":{"firstPublicDate":"1995-02-01","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"1995-02-01","entryVersion":103,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"value":"Serine protease 1"},"ecNumbers":[{"value":"3.4.21.-"}]},"alternativeNames":[{"fullName":{"value":"Serine protease I"},"shortNames":[{"value":"RPI"}]}],"flag":"Precursor"},"comments":[{"texts":[{"value":"Major serine protease exhibiting lytic activity toward living yeast cells. Similar to elastase in its substrate specificity and has a lectin-like affinity for mannose. Mannoproteins may be the native substrate for RPI"}],"commentType":"FUNCTION"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the peptidase S1 family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Propeptide","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}],"featureId":"PRO_0000026919"},{"type":"Chain","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Serine protease 1","featureId":"PRO_0000026920"},{"type":"Domain","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Ricin B-type lectin","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00174"}]},{"type":"Region","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Essential for the lytic activity, but not for protease function"},{"type":"Active site","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Active site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000250"}]},{"type":"Disulfide bond","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00174"}]},{"type":"Disulfide bond","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00174"}]},{"type":"Disulfide bond","location":{"start":{"value":346,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00174"}]},{"type":"Disulfide bond","location":{"start":{"value":412,"modifier":"EXACT"},"end":{"value":431,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00174"}]},{"type":"Disulfide bond","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00174"}]},{"type":"Disulfide bond","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":514,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00174"}]}],"keywords":[{"id":"KW-0903","category":"Technical term","name":"Direct protein sequencing"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"id":"KW-0430","category":"Ligand","name":"Lectin"},{"id":"KW-0465","category":"Ligand","name":"Mannose-binding"},{"id":"KW-0645","category":"Molecular function","name":"Protease"},{"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"1339445","citationType":"journal article","authors":["Shimoi H.","Iimura Y.","Obata T.","Tadenuma M."],"citationCrossReferences":[{"database":"PubMed","id":"1339445"},{"database":"DOI","id":"10.1016/s0021-9258(19)74023-x"}],"title":"Molecular structure of Rarobacter faecitabidus protease I. A yeast-lytic serine protease having mannose-binding activity.","publicationDate":"1992","journal":"J. Biol. Chem.","firstPage":"25189","lastPage":"25195","volume":"267"},"referencePositions":["NUCLEOTIDE SEQUENCE [GENOMIC DNA]","PROTEIN SEQUENCE OF 212-222; 224-238 AND 240-244"],"referenceComments":[{"value":"YLM-50","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"1778983","citationType":"journal article","authors":["Shimoi H.","Tadenuma M."],"citationCrossReferences":[{"database":"PubMed","id":"1778983"},{"database":"DOI","id":"10.1093/oxfordjournals.jbchem.a123628"}],"title":"Characterization of Rarobacter faecitabidus protease I, a yeast-lytic serine protease having mannose-binding activity.","publicationDate":"1991","journal":"J. Biochem.","firstPage":"608","lastPage":"613","volume":"110"},"referencePositions":["PROTEIN SEQUENCE OF 212-247"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"D10753","properties":[{"key":"ProteinId","value":"BAA01585.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"PIR","id":"A45053","properties":[{"key":"EntryName","value":"A45053"}]},{"database":"RefSeq","id":"WP_170222524.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"Q05308","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q05308","properties":[{"key":"Description","value":"-"}]},{"database":"CAZy","id":"CBM13","properties":[{"key":"FamilyName","value":"Carbohydrate-Binding Module Family 13"}]},{"database":"MEROPS","id":"S01.276","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd21112","properties":[{"key":"EntryName","value":"alphaLP-like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd23452","properties":[{"key":"EntryName","value":"beta-trefoil_Ricin_RPI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.80.10.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.50","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.40.10.10","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR004236","properties":[{"key":"EntryName","value":"Pept_S1_alpha_lytic"}]},{"database":"InterPro","id":"IPR001316","properties":[{"key":"EntryName","value":"Pept_S1A_streptogrisin"}]},{"database":"InterPro","id":"IPR009003","properties":[{"key":"EntryName","value":"Peptidase_S1_PA"}]},{"database":"InterPro","id":"IPR063705","properties":[{"key":"EntryName","value":"Pro_N"}]},{"database":"InterPro","id":"IPR035992","properties":[{"key":"EntryName","value":"Ricin_B-like_lectins"}]},{"database":"InterPro","id":"IPR000772","properties":[{"key":"EntryName","value":"Ricin_B_lectin"}]},{"database":"InterPro","id":"IPR035070","properties":[{"key":"EntryName","value":"Streptogrisin_prodomain"}]},{"database":"Pfam","id":"PF02983","properties":[{"key":"EntryName","value":"Pro_Al_protease"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF28778","properties":[{"key":"EntryName","value":"Pro_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00652","properties":[{"key":"EntryName","value":"Ricin_B_lectin"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00861","properties":[{"key":"EntryName","value":"ALYTICPTASE"}]},{"database":"SMART","id":"SM00458","properties":[{"key":"EntryName","value":"RICIN"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50370","properties":[{"key":"EntryName","value":"Ricin B-like lectins"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50494","properties":[{"key":"EntryName","value":"Trypsin-like serine proteases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50231","properties":[{"key":"EntryName","value":"RICIN_B_LECTIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00134","properties":[{"key":"EntryName","value":"TRYPSIN_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00135","properties":[{"key":"EntryName","value":"TRYPSIN_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKCKKPSALFSALALVGALGAASVLGAASANSASPVAAATVQASSGSAKTSVAATSKSQDGDVLAAIVRDLKITKTQAKKRIKLEEKARQLEPRLQKKLGKKFAGLWISKNGKKIVVGVTTKKAAKVVKKAGATPKIVKSNLTTLKKRATKISKNAPSDIKNVNSWWVDPATNKVVIEARSKKAAKAAATAAGLTAGTYEITVSDDVIVPVRDYWGGDALSGCTLAFPVYGGFLTAGHCAVEGKGHILKTEMTGGQIGTVEASQFGDGIDAAWAKNYGDWNGRGRVTHWNGGGGVDIKGSNEAAVGAHMCKSGRTTKWTCGYLLRKDVSVNYGNGHIVTLNETSACALGGDSGGAYVWNDQAQGITSGSNMDTNNCRSFYQPVNTVLNKWKLSLVTSTDVTTSYVQGYQNNCIDVPNSDFTDGKQLQVWNCNGTNAQKVSFHPDGTLRINGKCLDARWAWTHNGTEVQLMNCNGHIAQKFTLNGAGDLVNVHANKCVDVKDWGGQGGKLQLWECSGGANQKWWRR","length":525,"molWeight":55654,"crc64":"DA2BCF7D330EBB61","md5":"7EC819C0CDA1232B81EDFCBE98C0E02C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Propeptide":1,"Chain":1,"Domain":1,"Region":1,"Active site":3,"Disulfide bond":6},"uniParcId":"UPI0000135D4F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZTW6","uniProtkbId":"A0A542ZTW6_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL63803.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL63803.1"}],"value":"FB461_0281"}]}],"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":"TQL63803.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":172,"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":261,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":499,"modifier":"EXACT"},"end":{"value":508,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":518,"modifier":"EXACT"},"end":{"value":527,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":556,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"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":170,"modifier":"EXACT"},"end":{"value":170,"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":186,"modifier":"EXACT"},"end":{"value":186,"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":201,"modifier":"EXACT"},"end":{"value":201,"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":259,"modifier":"EXACT"},"end":{"value":259,"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":259,"modifier":"EXACT"},"end":{"value":259,"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":364,"modifier":"EXACT"},"end":{"value":364,"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":382,"modifier":"EXACT"},"end":{"value":382,"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: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":408,"modifier":"EXACT"},"end":{"value":408,"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":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":418,"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":454,"modifier":"EXACT"},"end":{"value":454,"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":"UP000315389"}],"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-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL63803.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL63803.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL63803.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142118241.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZTW6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9775031at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00113","properties":[{"key":"RectionId","value":"UER00532"}]},{"database":"UniPathway","id":"UPA00973","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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":"MAYAAPAAVIVLAAGAGTRMVSDTPKVLHRIGGRSLLGHAIHAAQGLDPQRIAVVVRHQRDQVAEHAVEINPDVLIADQDDVPGTGRAVQCGLSTLDASVQARLAGQHGAPIDSEGTVSDAYIDGAVVVIAGDVPLLDADTLGELVSAHAADANAVTILTTEVANPAGYGRILRDPETGQVTGIVEERDASDQQRLIAEINSSVYVFDAALLRAALGQVTTHNVQGEIYLTDVVAIAHQQGLPVRAVKSDDPMVVEGVNDRAQLAILGAELNRRVLNDWMQRGVTVVDPATTWIDVDVDLAQDVTLLPGVQLHGATSVAKGATIGPDTTLTDVEVGENATIIRTHGSLAVIGAGATVGPFAYLRPGTELGEAGKIGTFVEVKNGKIGKGTKVPHLSYVGDATIGEGTNIGAGTIFVNYDGVNKHHTTVGDGARTGANNIFIAPVTIGDGAYTAGGTVVRYEVPAGALAVSAGRQRNIDGWVERRRPGTAAADIARKARGGQGTDGGGLSRQAREEQARAQQRGSQAPPATPVDGAGFGYRIQTPPFGTPVGGVEGDNSNNEGGAGQ","length":566,"molWeight":58245,"crc64":"0572AA262AD1234E","md5":"F51855C0D5679F258FD01CAF68D26EF8"},"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":3,"Active site":1,"Binding site":17},"uniParcId":"UPI0011536D1B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZUU8","uniProtkbId":"A0A542ZUU8_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64138.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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":"TQL64138.1"}],"value":"FB461_0629"}]}],"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":"TQL64138.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":338,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":28,"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":90,"modifier":"EXACT"},"end":{"value":91,"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":149,"modifier":"EXACT"},"end":{"value":151,"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":186,"modifier":"EXACT"},"end":{"value":186,"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":193,"modifier":"EXACT"},"end":{"value":195,"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":246,"modifier":"EXACT"},"end":{"value":246,"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":307,"modifier":"EXACT"},"end":{"value":307,"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":313,"modifier":"EXACT"},"end":{"value":316,"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":128,"modifier":"EXACT"},"end":{"value":128,"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":"UP000315389"}],"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-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64138.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64138.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL64138.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A542ZUU8","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000315389","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":"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":"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"}]}],"sequence":{"value":"MTAWTAMGHAKEGGEMSAKKVGILTAGGDSPGLNAAIRGFGKTAVGHYHMDLIGYRDGITGLVQDRHEPLTGSTLSGILTVGGTILGTSRDKVHRFATPDGVVDMVPTVVENYQREGLDALIMLGGGGTAKNAKRLVDAGLNVIHLPKTIDNDIAETDTTFGFATAMEIATDAIDRVHSTAHSHHRIILTEIMGHRAGWLTLGAGIAGGADIILIPEIPYTVESVAATIRERTKRGSSFSVVAVAEGARDIHDTADYEAARLLVKAAKTPEQQRAAKVHLRNVEDLQREHTFKLARELEAATGLEARVTILGYVQRGGSPSAADRMLATRLGAAAADLVADGEFGVMVASHGEEAVPVPLDRVAGKTKLVPPDHAWVQAARKVGTGLGD","length":389,"molWeight":40953,"crc64":"8C062DDB7E8370C6","md5":"FDF04D8C8AECCFEB8A48305D54211723"},"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":8,"Site":1},"uniParcId":"UPI0011685256"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZV25","uniProtkbId":"A0A542ZV25_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64215.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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":"TQL64215.1"}],"value":"FB461_0709"}]}],"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":"TQL64215.1"}],"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":82,"modifier":"EXACT"},"end":{"value":82,"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":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"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":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":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":52,"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":111,"modifier":"EXACT"},"end":{"value":111,"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":140,"modifier":"EXACT"},"end":{"value":141,"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":"UP000315389"}],"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-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64215.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64215.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL64215.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A542ZV25","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00245","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRVALTIGVLALQGDFREHLATLDACGVRTRAVKSAAQLSQCDALVLPGGESTTIDKLARAFDLRDPIVSAIAGGMPVYGSCAGMILLADEVADGTADQQTFGGIDMTVRRNAFGRQVDSFEEDLTIAGVAGPPLRAVFIRAPAVERVGSGVEVLATTSAEQSPDRIVAVRSGNLLATSFHPEVTGDHRIHELFIRIATKEQ","length":202,"molWeight":21341,"crc64":"D050E8CD5DB2A4E3","md5":"EC7EDAC18A3550C25831AF6E0980DC8D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI00116BE26A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZVP2","uniProtkbId":"A0A542ZVP2_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":24,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64433.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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":"TQL64433.1"}],"value":"FB461_0936"}]}],"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":"TQL64433.1"}],"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":170,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":395,"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":184,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"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":283,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":304,"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":321,"modifier":"EXACT"},"end":{"value":321,"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":343,"modifier":"EXACT"},"end":{"value":343,"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":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64433.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64433.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL64433.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142119379.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000003.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZVP2","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802554at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000315389","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":"MRIIVGVSGGIAAYKAVLVVRALMERGHEVRVIPTSSALKFVGAPTWEALTGKPATHEVFDSVTEVEHVALGRWADLVAVIPATADLLARAAGGRADDLLTTTLLTTTGPVLMAPAMHTEMWQHPATVANVAVLKERGILVVEPADGRLTGADSGPGRLPEPVDLVDAIEAADPTANRPLAGLRVAISIGGTREPLDPVRFIGNRSSGRQGFALATEASRRGADVVAIVGSIESHPPRGLNSIRVGTALELRDAMLSEAQRADIIIMAAAVADFRPAVAGEHKLKKTGPDQGETVELVQNPDILAELAGSRRDSAQVVVGFAAETGDASASAIEHARDKARRKGADVLVFNDVATNDVFGAANNSVVFLDGRGAELGAATGTKADVAAALLDVVQTLRSAR","length":401,"molWeight":41660,"crc64":"3F298ACCF852CD3B","md5":"7683E7A5DFCB6D1BC854B733C44A680B"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI001150F079"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZVP9","uniProtkbId":"A0A542ZVP9_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":29,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64438.1"}],"value":"FB461_0941"}]}],"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":"TQL64438.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1104,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5051056868"},{"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":681,"modifier":"EXACT"},"end":{"value":877,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":959,"modifier":"EXACT"},"end":{"value":1104,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":959,"modifier":"EXACT"},"end":{"value":1104,"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":717,"modifier":"EXACT"},"end":{"value":717,"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":763,"modifier":"EXACT"},"end":{"value":763,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":768,"modifier":"EXACT"},"end":{"value":768,"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":793,"modifier":"EXACT"},"end":{"value":793,"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":794,"modifier":"EXACT"},"end":{"value":794,"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":795,"modifier":"EXACT"},"end":{"value":795,"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":796,"modifier":"EXACT"},"end":{"value":796,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":836,"modifier":"EXACT"},"end":{"value":836,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":836,"modifier":"EXACT"},"end":{"value":836,"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":836,"modifier":"EXACT"},"end":{"value":836,"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":848,"modifier":"EXACT"},"end":{"value":848,"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":848,"modifier":"EXACT"},"end":{"value":848,"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":848,"modifier":"EXACT"},"end":{"value":848,"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":848,"modifier":"EXACT"},"end":{"value":848,"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":848,"modifier":"EXACT"},"end":{"value":848,"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":850,"modifier":"EXACT"},"end":{"value":850,"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":850,"modifier":"EXACT"},"end":{"value":850,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL64438.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142119389.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000003.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZVP9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804197at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00068","properties":[{"key":"RectionId","value":"UER00171"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00115"}]},{"database":"Proteomes","id":"UP000315389","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"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPRRDDIQSVMVIGSGPIVIGQACEFDYSGTQACRVLKEEGLRVILVNSNPATIMTDPEFADATYVEPITTEVLTSIIAKERPDALLPTLGGQTALNAAIGLAEAGVLDRYGVELIGANIAAIEKGEDREQFKQVVEVAGGESARSAIIHTLDEALEAVIDLKYPVVVRPSFTMGGLGSGIAYDEADLRQIVGQGLHYSPTTEVLLEESILGWKEYELELMRDKHDNVVVVCSIENVDPVGVHTGDSITVAPALTLTDREFQRLRDIGIAVIREVGVDTGGCNIQFAVHPDTGRIIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDITESTPASFEPTLDYIVVKVPRFAFEKFPAADDTLTTTMKSVGEAMALGRNFTEALGKAMRSIDKAGSTFHWDGEAPSGAELTELLELIKRPTEQRIIQVQQALRGGASVDEVYAATGIDPWFLDQIALINDVANAVRSADALDADLLRFAKRHGLSDKQIASLRGIHGRGAATVFEIRKALGIRPVFKTVDTCAAEFEARTPYHYSSYDEETEVRPREREAVIILGSGPNRIGQGIEFDYSCVHATLALSDQYETIMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEVYEAELAAGPIKGVIVQLGGQTPLSLAQGLADYGVPILGTSPSAIDAAEDRGEFGRVLEEAGLPAPAFGTATSVQQAITVAERIGYPVLVRPSYVLGGRGMEIVYGREQLTSYVQRALDAAIATGGHLAPILIDRFLDDAIEIDVDAIYDGEDLYLGGVMEHIEEAGIHSGDSACVLPPVTLSRQEIDRIRRSTVALAKGIGVRGLMNVQYALVSDVLYVLEANPRASRTVPFVSKATGVPLAKAAARVMAGATIAELRADGSLPADGDGGSINPNAPLAVKEAVLPFKRFRTRAGVAVDTVLGPEMRSTGEVMGFDADFPTAFAKSQAAAFGGLPTKGRVFVSVADRDKRLAVLPVKRLAELGFELLATEGTALVLKRNGISSVQVRKQSDGRGPNGEPTIVDLISTGEVDMVINTPNSQGSRADGYEIRAATTAADKAIITTVQQLSAAVQAIEAQLHGGAFDVHPLQTYVVKPGA","length":1104,"molWeight":117929,"crc64":"1140E3E716638A94","md5":"25A73D4855D2083CA42F3C7AFA908055"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Chain":1,"Domain":3,"Region":2,"Binding site":38,"Lipidation":2},"uniParcId":"UPI00114E748C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZW23","uniProtkbId":"A0A542ZW23_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":25,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64564.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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":"TQL64564.1"}],"value":"FB461_1070"}]}],"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":"TQL64564.1"}],"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":40,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":417,"modifier":"EXACT"},"end":{"value":417,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":549,"modifier":"EXACT"},"end":{"value":549,"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":551,"modifier":"EXACT"},"end":{"value":551,"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":49,"modifier":"EXACT"},"end":{"value":49,"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":49,"modifier":"EXACT"},"end":{"value":49,"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":50,"modifier":"EXACT"},"end":{"value":55,"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":107,"modifier":"EXACT"},"end":{"value":107,"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":107,"modifier":"EXACT"},"end":{"value":107,"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":176,"modifier":"EXACT"},"end":{"value":176,"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":183,"modifier":"EXACT"},"end":{"value":185,"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":223,"modifier":"EXACT"},"end":{"value":228,"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":223,"modifier":"EXACT"},"end":{"value":228,"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":259,"modifier":"EXACT"},"end":{"value":259,"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":259,"modifier":"EXACT"},"end":{"value":259,"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":275,"modifier":"EXACT"},"end":{"value":277,"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":390,"modifier":"EXACT"},"end":{"value":390,"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":418,"modifier":"EXACT"},"end":{"value":421,"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":441,"modifier":"EXACT"},"end":{"value":441,"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":502,"modifier":"EXACT"},"end":{"value":502,"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":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64564.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64564.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL64564.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A542ZW23","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000315389","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":"MADDQNPGEKSRLDDILGLSPVKNQRLISSLGRGDHITRQVFVTGGVASSLGKGLTASSLGRLLRSRGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDIGHYERFLDENLGALANVTTGQVYSNVIAKERRGEYLGDTVQVIPHITDAIKERMRAQSGTNVDVIITEIGGTVGDIESQPFLEAARQVRHELGRDNVFFLHVSLVPYIGPSGELKTKPTQHSVAALRSIGIQPDAIVLRADRDVPEATKNKIALMCDVDTEAVVTAKDAPSIYDIPRVLHSEGLDAYVVRRLDLPFHDVDWDGWRQLLERVHYPERTVTVALVGKYIDLPDAYLSVTEALRAGGFAANAKVNIRWVASDQCESPEGAQQVLGGVDAVLIPGGFGVRGVDGKIGAARWARENKVPTLGICLGMQVMVMEYARNILGLAGASSSEFDPETKHPVVATMAEQLAFVDGEGDLGGTMRLGAYDAELKAGSVLAETYGSTSVSERHRHRYEVNNAYRDALEDAGLSIAGTSPDGSLVEFIELPRETHPYYVATQAHPEFKSRPTRAHPLFAGLIRAALDGQGLLLEDEEVDRAVADELA","length":592,"molWeight":64245,"crc64":"618B09CDD41D444B","md5":"C116E51E7930C1F7D1C7C3FE0A82C9B9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":1,"Active site":4,"Binding site":16},"uniParcId":"UPI00116A7862"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZW39","uniProtkbId":"A0A542ZW39_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64519.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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":"TQL64519.1"}],"value":"FB461_1024"}]}],"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"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"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":"TQL64519.1"}],"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":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI: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":102,"modifier":"EXACT"},"end":{"value":105,"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":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":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":104,"modifier":"EXACT"},"end":{"value":104,"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":"UP000315389"}],"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-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64519.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64519.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL64519.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142119525.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000007.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZW39","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9802503at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000315389","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":"FunFam","id":"3.40.50.460:FF:000002","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"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":"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":"MQIGLLTGGGDCPGLNAAIRAVVKRGLGEYGHSIMGFRNGWKGVVDGDILPLTRDKIRNTLPLGGTLLGTARYHPTKENGGIDAVLQVLEQERIEALICIGGDGTLHAASEVAAAGVKIVAIPKTIDNDVWGTDQSIGYHTAVNIATEAIDRIHTTAESHNRVMVIEVMGRTAGWIAVNAGIAGGAEIVLAPEEPFDMDKVVRFLTHRHRSHASFSIVVVAEGAQAVPGSSFEYTSATGKYGEIIGGAVGAAVSQEIAQRTGFDTRLTVLGHVQRGGSPTPTDRILGSRFGVAAVDAINADKSDVMTALIGEHVELVSLQEIAGKVKTVPAELLQVARALA","length":341,"molWeight":35686,"crc64":"0685F22C3481A632","md5":"F2F72E23F0C84773B81EB3016756B462"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":10,"Site":1},"uniParcId":"UPI0011535D17"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZWF9","uniProtkbId":"A0A542ZWF9_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":23,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64687.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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":"TQL64687.1"}],"value":"FB461_1196"}]}],"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":"TQL64687.1"}],"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":122,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":192,"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":225,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":250,"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":327,"modifier":"EXACT"},"end":{"value":327,"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":"UP000315389"}],"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-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64687.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL64687.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL64687.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142119805.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000001.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZWF9","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAVRPQSLGMPLDFSARTKGRRGKPPRHFVDFSQDEVSEFLAEVGQPKFRGKQLATHYFEHFSNDSSEMTDLPAAIRERIQETLFPALLTEVRELTADGGTTVKTLWNLFDDAKVESVLMRYPSRSTLCISSQAGCGMACPFCATGQLGLTRNLTTAEIVEQVRAAQRALHEGRIPGGPTSLNNIVFMGMGEPLANYKAIMGTVRALVAPRPWGMGMSARNVTVSTVGLVPAMRKLADEGIPVTLALSLHAPDDDLRSELVPINTRWSVGEALDAARHYFEVTGRRVSIEYALIKDMNDHAWRADLLAKKLNARGKGWVHVNPIPLNPTPGSIWTAPDKDVEREFVDRLRAAGIPTTIRDTRGSDIDGACGQLAAAKEEKSA","length":382,"molWeight":41818,"crc64":"7DA47661A3575138","md5":"9CC659A7FC3576FD2DC4E5B2CB66E25F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Active site":2,"Binding site":7},"uniParcId":"UPI00115339B0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZXG6","uniProtkbId":"A0A542ZXG6_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":28,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL65051.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"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":"TQL65051.1"}],"value":"FB461_1584"}]}],"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":"TQL65051.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":64,"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":61,"modifier":"EXACT"},"end":{"value":61,"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":148,"modifier":"EXACT"},"end":{"value":148,"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":197,"modifier":"EXACT"},"end":{"value":197,"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":200,"modifier":"EXACT"},"end":{"value":200,"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":302,"modifier":"EXACT"},"end":{"value":302,"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":352,"modifier":"EXACT"},"end":{"value":352,"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":428,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":471,"modifier":"EXACT"},"end":{"value":475,"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":498,"modifier":"EXACT"},"end":{"value":498,"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":499,"modifier":"EXACT"},"end":{"value":499,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL65051.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL65051.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL65051.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL65051.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000001","properties":[{"key":"ProteinId","value":"TQL65051.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142120469.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZXG6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9806925at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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":"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":"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":"MIEGYLAADVREAERPYLDAGVPLMERAAFGLAMVALRELRQRRGTTAGAHAVILAGKGNNGADAMLAGIHLRRRGVAVTALLVHESGVESTVTALRNAGARVLSLSQALADCTTGMPWPGIADEVGDSHTPLDWLVGRIHMSDLIVDGILGTGTRPGGSSGAGMPDELAELLMRIGGGWLPRRSVEERRPLVIAVDLPSGIDPDTGTVVDRNTVLFADVTVTFQCSKAGLLLAPAAEFVGRIEVIDIGIGEALHGVAPAVARFEPADERLRVYVKAPGWGDHKYTRGVVGVVAGSSQYPGAGLMATASAVRAGAGMARYLGPANVAELIVSQSPEVVHAPGRVQAYVVGSGLPSRDEGQPADIGEQLDRAAAAIEVALGIPTEDGLSLLGLPEGPARKVPVVVDAGGFSVLPDARVRLTSDVVLTPHAGELAGLVSSFGPDEVSREQIEAEPAKYARLAHDLTGATVVLKGPVTVIADEHRLWSQTGPSWLARAGSGDILAGIIGSLLAQSDDRQSRAEIAAAGVLVHATAARIASGQRDDPAAVGRPPTAQAIIDAVPYAIGRIIAASSS","length":572,"molWeight":59040,"crc64":"BA32468BC5F7BEDA","md5":"35D65A2D92953AA88806155947E8F996"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":11},"uniParcId":"UPI00114E5F28"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542Z9Y5","uniProtkbId":"A0A542Z9Y5_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":28,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57157.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00665"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"Replicative DNA helicase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00665"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"5.6.2.3"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57157.1"}],"value":"FB461_2277"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating dsDNA into templates for DNA synthesis. A processive ATP-dependent 5'-3' DNA helicase it has DNA-dependent ATPase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048954"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093875"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008428"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362085"}],"value":"Belongs to the helicase family. DnaB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57157.1"}],"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":192,"modifier":"EXACT"},"end":{"value":457,"modifier":"EXACT"}},"description":"SF4 helicase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51199"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":223,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022705"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0235","category":"Biological process","name":"DNA replication"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022515"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00596"}],"id":"KW-0639","category":"Cellular component","name":"Primosome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57157.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57157.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000005","properties":[{"key":"ProteinId","value":"TQL57157.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142122128.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542Z9Y5","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9773982at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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:1990077","properties":[{"key":"GoTerm","value":"C:primosome complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006269","properties":[{"key":"GoTerm","value":"P:DNA replication, synthesis of primer"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00984","properties":[{"key":"EntryName","value":"DnaB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.860.10:FF:000001","properties":[{"key":"EntryName","value":"Replicative DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000351","properties":[{"key":"EntryName","value":"Replicative DNA helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.860.10","properties":[{"key":"EntryName","value":"DNAb Helicase, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036185","properties":[{"key":"EntryName","value":"DNA_heli_DnaB-like_N_sf"}]},{"database":"InterPro","id":"IPR007692","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB"}]},{"database":"InterPro","id":"IPR007694","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB-like_C"}]},{"database":"InterPro","id":"IPR007693","properties":[{"key":"EntryName","value":"DNA_helicase_DnaB-like_N"}]},{"database":"InterPro","id":"IPR016136","properties":[{"key":"EntryName","value":"DNA_helicase_N/primase_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF004384","properties":[{"key":"EntryName","value":"dnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00665","properties":[{"key":"EntryName","value":"DnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30153:SF2","properties":[{"key":"EntryName","value":"REPLICATIVE DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30153","properties":[{"key":"EntryName","value":"REPLICATIVE DNA HELICASE DNAB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00772","properties":[{"key":"EntryName","value":"DnaB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03796","properties":[{"key":"EntryName","value":"DnaB_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48024","properties":[{"key":"EntryName","value":"N-terminal domain of DnaB helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51199","properties":[{"key":"EntryName","value":"SF4_HELICASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNSEYGEPFDEPSNEGPGRTPPQDVAAEQSVLGSMLISKDAIADVIEAVRDSDFYRPSHEIIYSAITNLYGRGEPADAITVVDELTKRGELGRIGGATYIHDLIAMVPTAANAGYYARIVRERAILRRLVEAGTRIVQIGYAADGGDVDELVNNAQAEVYAVTETRATEDYVVLGPVVDQTFDEIERIAQSGEGMAGVPTGFDDLDSLTNGLHAGQMIVIAARPAIGKSTLGIDIVRSAAIKHNQTAVVFSLEMSRTEIAMRLLSAESELSLQKLRTGRVDANDWSRLANTQKRIADAPLYIDDSPNMSLMEIRAKCRRLKQRHDLKLVVIDYLQLMTSGKRVESRQQEVSEFSRALKLLAKELEVPVIAISQLNRGPEQRTDKRPQMSDLRESGSIEQDADMVILLHREDAYEPESPRAGEADLIVAKHRNGPTATIAVAFQGRYSRFKNMARDASFGG","length":461,"molWeight":50630,"crc64":"6A031AF370557FAB","md5":"44EC91715E3200134083D0DC062FA6A5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Binding site":1},"uniParcId":"UPI0011500A8D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZA69","uniProtkbId":"A0A542ZA69_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":28,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57216.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"5-methyltetrahydropteroyltriglutamate--homocysteine methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"2.1.1.14"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"Cobalamin-independent methionine synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"Methionine synthase, vitamin-B12 independent isozyme"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"metE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57216.1"}],"value":"FB461_2337"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"Catalyzes the transfer of a methyl group from 5-methyltetrahydrofolate to homocysteine resulting in methionine formation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = tetrahydropteroyltri-L-glutamate + L-methionine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21196"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:58140"},{"database":"ChEBI","id":"CHEBI:58199"},{"database":"ChEBI","id":"CHEBI:58207"}],"ecNumber":"2.1.1.14","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"Binds 1 zinc ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004681"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-methionine from L-homocysteine (MetE route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009553"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"value":"Belongs to the vitamin-B12 independent methionine synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57216.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"Cobalamin-independent methionine synthase MetE N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08267"}]},{"type":"Domain","location":{"start":{"value":440,"modifier":"EXACT"},"end":{"value":762,"modifier":"EXACT"}},"description":"Cobalamin-independent methionine synthase MetE C-terminal/archaeal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01717"}]},{"type":"Active site","location":{"start":{"value":708,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-3"}]},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":122,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58199"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-homocysteine","id":"ChEBI:CHEBI:58199"}},{"type":"Binding site","location":{"start":{"value":445,"modifier":"EXACT"},"end":{"value":447,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57844"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-methionine","id":"ChEBI:CHEBI:57844"}},{"type":"Binding site","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58199"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"L-homocysteine","id":"ChEBI:CHEBI:58199"}},{"type":"Binding site","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57844"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-methionine","id":"ChEBI:CHEBI:57844"}},{"type":"Binding site","location":{"start":{"value":529,"modifier":"EXACT"},"end":{"value":530,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":575,"modifier":"EXACT"},"end":{"value":575,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":613,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58199"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-homocysteine","id":"ChEBI:CHEBI:58199"}},{"type":"Binding site","location":{"start":{"value":613,"modifier":"EXACT"},"end":{"value":613,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57844"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-1"}],"ligand":{"name":"L-methionine","id":"ChEBI:CHEBI:57844"}},{"type":"Binding site","location":{"start":{"value":619,"modifier":"EXACT"},"end":{"value":619,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58207"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"5-methyltetrahydropteroyltri-L-glutamate","id":"ChEBI:CHEBI:58207"}},{"type":"Binding site","location":{"start":{"value":655,"modifier":"EXACT"},"end":{"value":655,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":655,"modifier":"EXACT"},"end":{"value":655,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":657,"modifier":"EXACT"},"end":{"value":657,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":657,"modifier":"EXACT"},"end":{"value":657,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":740,"modifier":"EXACT"},"end":{"value":740,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":740,"modifier":"EXACT"},"end":{"value":740,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000382-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1","note":"catalytic"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023167"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"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_00172"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00172"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57216.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57216.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000005","properties":[{"key":"ProteinId","value":"TQL57216.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142122234.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZA69","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"244285at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00051","properties":[{"key":"RectionId","value":"UER00082"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003871","properties":[{"key":"GoTerm","value":"F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008652","properties":[{"key":"GoTerm","value":"P:amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03311","properties":[{"key":"EntryName","value":"CIMS_C_terminal_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03312","properties":[{"key":"EntryName","value":"CIMS_N_terminal_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00172","properties":[{"key":"EntryName","value":"Meth_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013215","properties":[{"key":"EntryName","value":"Cbl-indep_Met_Synth_N"}]},{"database":"InterPro","id":"IPR006276","properties":[{"key":"EntryName","value":"Cobalamin-indep_Met_synthase"}]},{"database":"InterPro","id":"IPR002629","properties":[{"key":"EntryName","value":"Met_Synth_C/arc"}]},{"database":"InterPro","id":"IPR038071","properties":[{"key":"EntryName","value":"UROD/MetE-like_sf"}]},{"database":"NCBIfam","id":"TIGR01371","properties":[{"key":"EntryName","value":"met_syn_B12ind"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003556","properties":[{"key":"EntryName","value":"metE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30519","properties":[{"key":"EntryName","value":"5-METHYLTETRAHYDROPTEROYLTRIGLUTAMATE--HOMOCYSTEINE METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08267","properties":[{"key":"EntryName","value":"Meth_synt_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01717","properties":[{"key":"EntryName","value":"Meth_synt_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000382","properties":[{"key":"EntryName","value":"MeTrfase_B12_ind"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51726","properties":[{"key":"EntryName","value":"UROD/MetE-like"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTTPAFPVATIVGYPRIGRRRELKKAVEAYWAGKSTLAELEETASGLRQATRERLAELGLGRTDASIPETFSFYDQVLDVTAAVGAVPPRFAGFEGLDLYFTLARGIGDIAPLEMTKWFDTNYHYLVPEIGPDTAFSLSSRRIIDQFTQARAGGFVTRPAIVGPVTYLLLSKAADGAPEGFDPLDRLEDILPVYAELLAELAAAGAPWVQLDEPGLVTDNISVEPGVVSAAVTRAYEVLAGGQRPAIFVTSPFGDLRENFPVLAATGVEAIHVDLVHGGVPAAAPGLATKTLVGGVIDGHNIWAADLGAKFEQLEALTELGASAVSAATATSLQHVPHDTADEKWEDAELDANLHAWLAFADQKVVEVVTLSRGLTSGRGAIEDEITASQQALASRAAAAGVRVDAIRARTAALTEADFSRGDYDERAAAQAAKLGLPELPTTTIGSFPQTVEIRRARAAHARGELATEAYEAEMRAEIKRVIELQESIGLDVLVHGEAERNDMVQYFAELLDGFAVTTNGWVQSYGSRCTRPSILWGDVSRPEPMTVRWATYAQSLTPKPVKGMLTGPVTIMAWSFVRDDIPLGETANQLGLALRDEVNDLEAAGIGIIQVDEPALRELLPLRREDQPAYLDWSVGSFRLSTAGVRPETQIHTHLCYSEFGEVIGAIDGLDADVTSIEAARSRMEIVPELAAAGYARGVGPGVYDIHSPRVPSVDEVSELVALAAQGVPGNLLWINPDCGLKTRGYAETVPSLENLVAATRAVRNREVANV","length":772,"molWeight":82697,"crc64":"BA0A4934AB3D4CAD","md5":"AA07ED5050182DFE4709A1704E7B0F32"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":2,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":21},"uniParcId":"UPI001150A0E5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZAA3","uniProtkbId":"A0A542ZAA3_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57245.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine dehydrogenase (decarboxylating)"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"1.4.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine cleavage system P-protein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine decarboxylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Glycine dehydrogenase (aminomethyl-transferring)"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"gcvP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57245.1"}],"value":"FB461_2368"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003788"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-[(R)-lipoyl]-L-lysyl-[glycine-cleavage complex H protein] + glycine + H(+) = N(6)-[(R)-S(8)-aminomethyldihydrolipoyl]-L-lysyl-[glycine-cleavage complex H protein] + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24304"},{"database":"Rhea","id":"RHEA-COMP:10494"},{"database":"Rhea","id":"RHEA-COMP:10495"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:83099"},{"database":"ChEBI","id":"CHEBI:83143"}],"ecNumber":"1.4.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049026"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603437-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011690"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"The glycine cleavage system is composed of four proteins: P, T, L and H"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010756"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"value":"Belongs to the GcvP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57245.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":453,"modifier":"EXACT"}},"description":"Glycine cleavage system P-protein N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02347"}]},{"type":"Domain","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":770,"modifier":"EXACT"}},"description":"Glycine cleavage system P-protein N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02347"}]},{"type":"Domain","location":{"start":{"value":838,"modifier":"EXACT"},"end":{"value":958,"modifier":"EXACT"}},"description":"Glycine dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF21478"}]},{"type":"Modified residue","location":{"start":{"value":742,"modifier":"EXACT"},"end":{"value":742,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR603437-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00711"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57245.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57245.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000005","properties":[{"key":"ProteinId","value":"TQL57245.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142122282.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZAA3","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9801272at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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:0005960","properties":[{"key":"GoTerm","value":"C:glycine cleavage complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016594","properties":[{"key":"GoTerm","value":"F:glycine binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004375","properties":[{"key":"GoTerm","value":"F:glycine dehydrogenase (decarboxylating) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019464","properties":[{"key":"GoTerm","value":"P:glycine decarboxylation via glycine cleavage system"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.640.10:FF:000007","properties":[{"key":"EntryName","value":"glycine dehydrogenase (Decarboxylating), mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00711","properties":[{"key":"EntryName","value":"GcvP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003437","properties":[{"key":"EntryName","value":"GcvP"}]},{"database":"InterPro","id":"IPR049316","properties":[{"key":"EntryName","value":"GDC-P_C"}]},{"database":"InterPro","id":"IPR049315","properties":[{"key":"EntryName","value":"GDC-P_N"}]},{"database":"InterPro","id":"IPR020581","properties":[{"key":"EntryName","value":"GDC_P"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR00461","properties":[{"key":"EntryName","value":"gcvP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003346","properties":[{"key":"EntryName","value":"gcvPB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11773:SF1","properties":[{"key":"EntryName","value":"GLYCINE DEHYDROGENASE (DECARBOXYLATING), MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11773","properties":[{"key":"EntryName","value":"GLYCINE DEHYDROGENASE, DECARBOXYLATING"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21478","properties":[{"key":"EntryName","value":"GcvP2_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02347","properties":[{"key":"EntryName","value":"GDC-P"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTTPAPANFTFTDRHIGPDDSHLATMLDSVGYASLDALTDAAVPKSIALTEPLGLPEPLSEPEVLADLRRIAGRNRVLTSMIGQGYYDTITPAVIRRGVLENPAWYTAYTPYQPEISQGRLEALLNFQTLVSDLTGLPVAGASLLDEATAVAEAVALMFRSRGRKLDLATDVVVIDADVLPTTIAVVTARAEAAGQRVIVADLHTGEATGWDAASLAAAGASIVGLVLAHPGASGAVRDLKGVIADAKAAGALVTFTTDLLALTLLVSPGELGADIAVGSSQRLGVPMFYGGPHAAFIATSHGLERQLPGRLVGVSVDADGAVAYRLALQTREQHIRRERATSNICTAQALLAITASMYAVYHGPQGLRSIAERVQALAGGLAAALRALELPGIAVADHALFDTVRISAPGLTERIRQGAAQRGINVYVADSDHVQIAFDEVSTAEHVATVLESVVAAVAERTLTWFACDVRGESLEFAVDGGETTRATWSASGASLPSWALRGTDYLTHPTFNSYRSETAMMRYLRRLADKDLALDRTMIPLGSCTMKLNAAVEMEAISWPEFAQIHPLAPADQTEGYAELIEKLTSWLSEITGYAGVSVQPNAGSQGEFAGLLAIRKYHEGRGEPGRSVCLIPASAHGTNAASAAMAGLSVVVIATAEDGSIDLADLRAKVAENADRLAAIMLTYPSTHGVYEEHVREVCDLVHEAGGQVYIDGANLNALVGLAKPGQFGGDVSHLNLHKTFAIPHGGGGPGVGPVAVAEHLLPYLPGDPSGARGGDATAAADVAASATAAAPDEAPSPISAQAPPVSAAQFGSAGVLPISYAYIALMGADLRRSSQVAVLSANYLARRLEQAFPVLYTGPNGLVAHECILDLRAITAATKITAEDVAKRLIDYGFHAPTLSFPVAGTLMVEPTESEDLAELDRFIDAMLAIRAEIAQVEAGEVTAEDSVLRAAPHTAESVTAEVWEHSYTRTEAAYPVPALRQAKYWPPVRRIDGAYGDRNLVCSCPPLSHYAADGDA","length":1021,"molWeight":107028,"crc64":"80792919EF3B542C","md5":"170B45D39F3E8CB83844FC65597E7C18"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Modified residue":1},"uniParcId":"UPI0011506873"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZAU7","uniProtkbId":"A0A542ZAU7_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":18,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57411.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"K(+)-insensitive pyrophosphate-energized proton pump"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"7.1.3.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Membrane-bound proton-translocating pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Pyrophosphate-energized inorganic pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"H(+)-PPase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"hppA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57411.1"}],"value":"FB461_2145"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Proton pump that utilizes the energy of pyrophosphate hydrolysis as the driving force for proton movement across the membrane. Generates a proton motive force"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"diphosphate + H2O + H(+)(in) = 2 phosphate + 2 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13973"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"}],"ecNumber":"7.1.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004141"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Belongs to the H(+)-translocating pyrophosphatase (TC 3.A.10) family. K(+)-insensitive subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57411.1"}],"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":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":874,"modifier":"EXACT"}},"description":"K(+)-insensitive pyrophosphate-energized proton pump","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5022006443"},{"type":"Transmembrane","location":{"start":{"value":65,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":225,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":323,"modifier":"EXACT"},"end":{"value":346,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":478,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":484,"modifier":"EXACT"},"end":{"value":503,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":573,"modifier":"EXACT"},"end":{"value":594,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":606,"modifier":"EXACT"},"end":{"value":625,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":673,"modifier":"EXACT"},"end":{"value":694,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":700,"modifier":"EXACT"},"end":{"value":721,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":768,"modifier":"EXACT"},"end":{"value":787,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Transmembrane","location":{"start":{"value":793,"modifier":"EXACT"},"end":{"value":811,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]},{"type":"Region","location":{"start":{"value":826,"modifier":"EXACT"},"end":{"value":860,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":827,"modifier":"EXACT"},"end":{"value":847,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Site","location":{"start":{"value":567,"modifier":"EXACT"},"end":{"value":567,"modifier":"EXACT"}},"description":"Determinant of potassium independence","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023065"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01129"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57411.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57411.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000004","properties":[{"key":"ProteinId","value":"TQL57411.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_211349906.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZAU7","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0009678","properties":[{"key":"GoTerm","value":"F:diphosphate hydrolysis-driven proton transmembrane transporter activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004427","properties":[{"key":"GoTerm","value":"F:inorganic diphosphate phosphatase 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":"HAMAP","id":"MF_01129","properties":[{"key":"EntryName","value":"PPase_energized_pump"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004131","properties":[{"key":"EntryName","value":"PPase-energised_H-pump"}]},{"database":"NCBIfam","id":"NF001950","properties":[{"key":"EntryName","value":"PRK00733.1-1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31998","properties":[{"key":"EntryName","value":"K(+)-INSENSITIVE PYROPHOSPHATE-ENERGIZED PROTON PUMP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03030","properties":[{"key":"EntryName","value":"H_PPase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001265","properties":[{"key":"EntryName","value":"H+-PPase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIPLHNSKRSGTDQRSKFRRGGLVLAAALLTPLWAAAPAHAAELGGEANLQLPNLGDIKVAGIGGHTLLGIAFGICLLGLVFGVVAYSQLQKLPVHKSMREISELIYSTCKEYLIKQGKFLLVLWAFIAAVILLYFKVLVGFSWGKVAIILAFSLIGMGGSFAVAWYGIRLNTFANSRAAFASLDGKPLAQHRIPMKSGMSIGMVLISVELIIMLSIMLFLPGDIAGSCFIGFAIGESLGAAALRIAGGIFTKIADIGADLMKIVFKIKEDDPRNPGVIADCTGDNAGDSVGPSADGFETYGVTGVALVTFILLGVHDPAIQGTLLIWLFFVRAIMLVASGISYFSNDAFTKAKYASAIRMNFEAPLTVLVWLTSAVSIALTFLTSYILLNGLEAAPGLWWRLSTIITCGTLAGALIPELVKVFTSTKARHTQEVVKSSREGGPSLNILSGLVAGNFSAYWLGMAIVGLMAVALLFANQGLDEIMLAPAVFAFGLVAFGFLGMGPVTIAVDSYGPVTDNAQSVYELSQIEEIENIDEELRTEFGIEPKWHEAKRMLEENDGAGNTFKATAKPVLIGTAVVGATTMIFSIIMTLTSGLTVGLSNLSLLHPPFLLGLISGGAIIYWFTGASTQAVTTGAYRAVEFIKDTIKLDENTPKRASVSDSRKVVAICTQYAQQGMLTIFLAVFFTTLSFAFIEPFFFIGYLVSIAVFGLYQAIFMANAGGAWDNAKKIVEVDLHAKGTALHDASVVGDTVGDPFKDTSSVALNPVIKFTTLFGLLAVELGVSMTDKGQSGLVHVLAAVFFVISACFVYRSFYGMRINTSLDQGDDLRIPEDPSRPDGSEFKDESSVPTADVTGPEDVMRADEALVGKEAGE","length":874,"molWeight":93174,"crc64":"DB1E60F33A0F3C85","md5":"53EABFF00B38A3954BBE9F326FC3A931"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":17,"Region":1,"Compositional bias":1,"Site":1},"uniParcId":"UPI001168B84F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZAV2","uniProtkbId":"A0A542ZAV2_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":30,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57370.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00072146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Uracil phosphoribosyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011894"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"2.4.2.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031082"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"UMP pyrophosphorylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00079807"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"UPRTase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"upp"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57370.1"}],"value":"FB461_2104"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056901"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UMP + diphosphate = 5-phospho-alpha-D-ribose 1-diphosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13017"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57865"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052919"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Binds 1 Mg(2+) ion per subunit. The magnesium is bound as Mg-PRPP."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Allosterically activated by GTP"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005180"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"value":"Belongs to the UPRTase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57370.1"}],"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":205,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14681"}]},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":99,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":134,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17568"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"uracil","id":"ChEBI:CHEBI:17568"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17568"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"uracil","id":"ChEBI:CHEBI:17568"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01218"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"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_01218"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57370.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57370.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000004","properties":[{"key":"ProteinId","value":"TQL57370.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A542ZAV2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00574","properties":[{"key":"RectionId","value":"UER00636"}]},{"database":"Proteomes","id":"UP000315389","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:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004845","properties":[{"key":"GoTerm","value":"F:uracil phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044206","properties":[{"key":"GoTerm","value":"P:UMP salvage"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006223","properties":[{"key":"GoTerm","value":"P:uracil salvage"},{"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:000003","properties":[{"key":"EntryName","value":"Uracil phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01218_B","properties":[{"key":"EntryName","value":"Upp_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"InterPro","id":"IPR034332","properties":[{"key":"EntryName","value":"Upp_B"}]},{"database":"InterPro","id":"IPR005765","properties":[{"key":"EntryName","value":"UPRT"}]},{"database":"InterPro","id":"IPR050054","properties":[{"key":"EntryName","value":"UPRTase/APRTase"}]},{"database":"NCBIfam","id":"NF001097","properties":[{"key":"EntryName","value":"upp"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01091","properties":[{"key":"EntryName","value":"upp"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315","properties":[{"key":"EntryName","value":"ADENINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32315:SF4","properties":[{"key":"EntryName","value":"URACIL PHOSPHORIBOSYLTRANSFERASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14681","properties":[{"key":"EntryName","value":"UPRTase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MADHPLIAHKLTVLRDVNTDSPTFRRLVEELVALLAYEATREVRVETVEVTTPVATTTGTHISTPRPLVVPILRAGLGMLEGMSKLLPTAEVGFLGMLRDETTLEAVTYANRLPQDITGRQTFLLDPMLATGGTLIMAIDYLLELGAKDVTAICLLAAPEGIDAVRQSVGDRAEVKIVVAAVDERLNAKGYIVPGLGDAGDRLYGVVD","length":208,"molWeight":22317,"crc64":"F258EEABD7E6AE80","md5":"E44F98A316BA22FD0073A955821B320D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":6},"uniParcId":"UPI00116B659A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZB36","uniProtkbId":"A0A542ZB36_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2019-10-16","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57501.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Serine--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"6.1.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Seryl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"SerRS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Seryl-tRNA(Ser/Sec) synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"serS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57501.1"}],"value":"FB461_2242"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Catalyzes the attachment of serine to tRNA(Ser). Is also able to aminoacylate tRNA(Sec) with serine, to form the misacylated tRNA L-seryl-tRNA(Sec), which will be further converted into selenocysteinyl-tRNA(Sec)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Sec) + L-serine + ATP = L-seryl-tRNA(Sec) + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42580"},{"database":"Rhea","id":"RHEA-COMP:9742"},{"database":"Rhea","id":"RHEA-COMP:10128"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78533"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Ser) + L-serine + ATP = L-seryl-tRNA(Ser) + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12292"},{"database":"Rhea","id":"RHEA-COMP:9669"},{"database":"Rhea","id":"RHEA-COMP:9703"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78533"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Homodimer. The tRNA molecule binds across the dimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Consists of two distinct domains, a catalytic core and a N-terminal extension that is involved in tRNA binding"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"value":"Belongs to the class-II aminoacyl-tRNA synthetase family. Type-1 seryl-tRNA synthetase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57501.1"}],"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":138,"modifier":"EXACT"},"end":{"value":406,"modifier":"EXACT"}},"description":"Aminoacyl-transfer RNA synthetases class-II family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50862"}]},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":283,"modifier":"EXACT"},"end":{"value":283,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-2"}],"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:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:33384"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"ligand":{"name":"L-serine","id":"ChEBI:CHEBI:33384"}},{"type":"Site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Important for serine binding","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001529-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00176"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57501.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL57501.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000004","properties":[{"key":"ProteinId","value":"TQL57501.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142122039.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZB36","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804647at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00906","properties":[{"key":"RectionId","value":"UER00895"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004828","properties":[{"key":"GoTerm","value":"F:serine-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016260","properties":[{"key":"GoTerm","value":"P:L-selenocysteine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006434","properties":[{"key":"GoTerm","value":"P:seryl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00770","properties":[{"key":"EntryName","value":"SerRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.40","properties":[{"key":"EntryName","value":"Serine-tRNA synthetase, tRNA binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00176","properties":[{"key":"EntryName","value":"Ser_tRNA_synth_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002314","properties":[{"key":"EntryName","value":"aa-tRNA-synt_IIb"}]},{"database":"InterPro","id":"IPR006195","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR002317","properties":[{"key":"EntryName","value":"Ser-tRNA-ligase_type_1"}]},{"database":"InterPro","id":"IPR015866","properties":[{"key":"EntryName","value":"Ser-tRNA-synth_1_N"}]},{"database":"InterPro","id":"IPR042103","properties":[{"key":"EntryName","value":"SerRS_1_N_sf"}]},{"database":"InterPro","id":"IPR033729","properties":[{"key":"EntryName","value":"SerRS_core"}]},{"database":"InterPro","id":"IPR010978","properties":[{"key":"EntryName","value":"tRNA-bd_arm"}]},{"database":"NCBIfam","id":"TIGR00414","properties":[{"key":"EntryName","value":"serS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11778","properties":[{"key":"EntryName","value":"SERYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02403","properties":[{"key":"EntryName","value":"Seryl_tRNA_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00587","properties":[{"key":"EntryName","value":"tRNA-synt_2b"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001529","properties":[{"key":"EntryName","value":"Ser-tRNA-synth_IIa"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00981","properties":[{"key":"EntryName","value":"TRNASYNTHSER"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46589","properties":[{"key":"EntryName","value":"tRNA-binding arm"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50862","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_II"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIDLNLLRDEPELVRESQRLRGEDPELVDRIIDADARRRSSLAAFEGARAEQKSMGKQVATASADERPALLAKTKELAERVKAFQADATQAGNEFDELLRQIQNVVEGAPPGGEDDYIVVREVGQARDFTAEGFQPADHLAIGEGLRAIDTARGAKVSGSRFYYLTGIGARLELALLNAAVDCALRAGFTPVITPTLVKPEVMAGTGFLGRHSDEIYHLGTDDLYLVGTSEVALAGYHSDEIIDLSDGPLRYAGWSACYRREAGSHGKDVRGIIRVHQFHKVEMFSYTTVEDAAAEHQRLLALEEEMLALVDLPYRVIDTAAGDLGSSAARKFDCEAWLPSQQRYLELTSTSNCTTYQARRLSVRERTESGATRAVATLNGTLATTRWIVAILENHQQADGSVTVPEGLRPYLGGLEVLIPKA","length":423,"molWeight":46226,"crc64":"0C4267B944DFEE58","md5":"0F723A092DC9682FBF21BA52BB875D4E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":10,"Site":1},"uniParcId":"UPI00114E6566"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZDR8","uniProtkbId":"A0A542ZDR8_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58493.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"Probable tRNA (cytidine(34)/5-carboxymethylaminomethyluridine(34)-2'-O)-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"2.1.1.207"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"tRNA (cytidine(34)-2'-O)-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"tRNA (cytidine/uridine-2'-O-)-methyltransferase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58493.1"}],"value":"FB461_1907"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"S-adenosyl-L-methionine-dependent methyltransferase that probably methylates the ribose at the nucleotide 34 wobble position in the two leucyl isoacceptors tRNA(Leu)(CAA) and tRNA(Leu)(UAA). It leads to the formation of 2'-O-methylcytidine (Cm34) in tRNA(Leu)(CAA) and 5-carboxymethylaminomethyl-2'-O-methyluridine (cmnm5Um34) in tRNA(Leu)(UAA)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-carboxymethylaminomethyluridine(34) in tRNA(Leu) + S-adenosyl-L-methionine = 5-carboxymethylaminomethyl-2'-O-methyluridine(34) in tRNA(Leu) + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43088"},{"database":"Rhea","id":"RHEA-COMP:10333"},{"database":"Rhea","id":"RHEA-COMP:10334"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74508"},{"database":"ChEBI","id":"CHEBI:74511"}],"ecNumber":"2.1.1.207","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"cytidine(34) in tRNA + S-adenosyl-L-methionine = 2'-O-methylcytidine(34) in tRNA + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43084"},{"database":"Rhea","id":"RHEA-COMP:10331"},{"database":"Rhea","id":"RHEA-COMP:10332"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74495"},{"database":"ChEBI","id":"CHEBI:82748"}],"ecNumber":"2.1.1.207","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"Belongs to the class IV-like SAM-binding methyltransferase superfamily. RNA methyltransferase TrmH family. TrmL subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58493.1"}],"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":19,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"tRNA/rRNA methyltransferase SpoU type","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00588"}]},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR029256-1"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR029256-1"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR029256-1"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"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_01885"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"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_01885"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01885"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58493.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58493.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58493.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A542ZDR8","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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:0003723","properties":[{"key":"GoTerm","value":"F:RNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0141102","properties":[{"key":"GoTerm","value":"F:tRNA (5-carboxymethylaminomethyluridine(34)-2'-O-ribose)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0141098","properties":[{"key":"GoTerm","value":"F:tRNA (cytidine(34)-2'-O-ribose)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0002130","properties":[{"key":"GoTerm","value":"P:wobble position ribose methylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd18094","properties":[{"key":"EntryName","value":"SpoU-like_TrmL"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1280.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01885","properties":[{"key":"EntryName","value":"tRNA_methyltr_TrmL"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029028","properties":[{"key":"EntryName","value":"Alpha/beta_knot_MTases"}]},{"database":"InterPro","id":"IPR001537","properties":[{"key":"EntryName","value":"SpoU_MeTrfase"}]},{"database":"InterPro","id":"IPR016914","properties":[{"key":"EntryName","value":"TrmL"}]},{"database":"InterPro","id":"IPR029026","properties":[{"key":"EntryName","value":"tRNA_m1G_MTases_N"}]},{"database":"PANTHER","id":"PTHR42971","properties":[{"key":"EntryName","value":"TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42971:SF1","properties":[{"key":"EntryName","value":"TRNA (CYTIDINE(34)-2'-O)-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00588","properties":[{"key":"EntryName","value":"SpoU_methylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF029256","properties":[{"key":"EntryName","value":"SpoU_TrmH_prd"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75217","properties":[{"key":"EntryName","value":"alpha/beta knot"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MCLSLIQSSDNGVVSQLPRIAFYEPRIPQNTGNAIRLSAVTGAALDLIEPLGFDLSEPKLKRAGLDYHDLASVTVYPDLDALLDAFPRARVLAFTTRASTRYTDIHYEPGDILLFGPEPTGLPPEVLAHERITAEVRIPMLAGRRSLNLTSSASIAIYEAWRQSDFASGA","length":170,"molWeight":18539,"crc64":"26B2635C22373842","md5":"9F4AA35266E43320B5FB74D51C7B4E5D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":4},"uniParcId":"UPI00116D4DD8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZDW6","uniProtkbId":"A0A542ZDW6_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":25,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58507.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acetyl-coenzyme A synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"AcCoA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acs"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"6.2.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acetate--CoA ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acyl-activating enzyme"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"acsA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58507.1"}],"value":"FB461_1921"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Catalyzes the conversion of acetate into acetyl-CoA (AcCoA), an essential intermediate at the junction of anabolic and catabolic pathways. AcsA undergoes a two-step reaction. In the first half reaction, AcsA combines acetate with ATP to form acetyl-adenylate (AcAMP) intermediate. In the second half reaction, it can then transfer the acetyl group from AcAMP to the sulfhydryl group of CoA, forming the product AcCoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23176"},{"database":"ChEBI","id":"CHEBI:30089"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.2.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Acetylated. Deacetylation by the SIR2-homolog deacetylase activates the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Belongs to the ATP-dependent AMP-binding enzyme family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58507.1"}],"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":90,"modifier":"EXACT"}},"description":"Acetyl-coenzyme A synthetase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16177"}]},{"type":"Domain","location":{"start":{"value":97,"modifier":"EXACT"},"end":{"value":491,"modifier":"EXACT"}},"description":"AMP-dependent synthetase/ligase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00501"}]},{"type":"Domain","location":{"start":{"value":544,"modifier":"EXACT"},"end":{"value":629,"modifier":"EXACT"}},"description":"AMP-binding enzyme C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13193"}]},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":324,"modifier":"EXACT"},"end":{"value":324,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":400,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":424,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":425,"modifier":"EXACT"},"end":{"value":425,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":428,"modifier":"EXACT"},"end":{"value":428,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":429,"modifier":"EXACT"},"end":{"value":429,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":528,"modifier":"EXACT"},"end":{"value":528,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":536,"modifier":"EXACT"},"end":{"value":536,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57287"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"CoA","id":"ChEBI:CHEBI:57287"}},{"type":"Binding site","location":{"start":{"value":539,"modifier":"EXACT"},"end":{"value":539,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":550,"modifier":"EXACT"},"end":{"value":550,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":552,"modifier":"EXACT"},"end":{"value":552,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":555,"modifier":"EXACT"},"end":{"value":555,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Modified residue","location":{"start":{"value":629,"modifier":"EXACT"},"end":{"value":629,"modifier":"EXACT"}},"description":"N6-acetyllysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01123"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58507.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58507.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58507.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142121466.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZDW6","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9803968at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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:0003987","properties":[{"key":"GoTerm","value":"F:acetyl-CoA synthetase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006085","properties":[{"key":"GoTerm","value":"P:acetyl-CoA biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd05966","properties":[{"key":"EntryName","value":"ACS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.12780:FF:000001","properties":[{"key":"EntryName","value":"Acetyl-coenzyme A synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.300.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12780","properties":[{"key":"EntryName","value":"N-terminal domain of ligase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01123","properties":[{"key":"EntryName","value":"Ac_CoA_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011904","properties":[{"key":"EntryName","value":"Ac_CoA_lig"}]},{"database":"InterPro","id":"IPR032387","properties":[{"key":"EntryName","value":"ACAS_N"}]},{"database":"InterPro","id":"IPR045851","properties":[{"key":"EntryName","value":"AMP-b_sf"}]},{"database":"InterPro","id":"IPR025110","properties":[{"key":"EntryName","value":"AMP-bd_C"}]},{"database":"InterPro","id":"IPR020845","properties":[{"key":"EntryName","value":"AMP-binding_CS"}]},{"database":"InterPro","id":"IPR000873","properties":[{"key":"EntryName","value":"AMP-dep_synth/lig_dom"}]},{"database":"InterPro","id":"IPR042099","properties":[{"key":"EntryName","value":"ANL_N_sf"}]},{"database":"NCBIfam","id":"TIGR02188","properties":[{"key":"EntryName","value":"Ac_CoA_lig_AcsA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001208","properties":[{"key":"EntryName","value":"PRK00174.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24095","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24095:SF14","properties":[{"key":"EntryName","value":"ACETYL-COENZYME A SYNTHETASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16177","properties":[{"key":"EntryName","value":"ACAS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00501","properties":[{"key":"EntryName","value":"AMP-binding"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13193","properties":[{"key":"EntryName","value":"AMP-binding_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56801","properties":[{"key":"EntryName","value":"Acetyl-CoA synthetase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00455","properties":[{"key":"EntryName","value":"AMP_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNTTENSSPALSNLLSEARSFPPSEEFAAQANATAALAREADERGEEFWADQARKMLSWHTPFTQTLDWSRAPVARWFADGTLNAAYNALDRHVKAGRGKRVAIHFEGEPGDTRTVTYDDLLTEVSRAANALQALGVQTGDRVIIYLPMLVESVVAMLACARIGAPHSVVFGGFSAEALRSRIEDAGARVIITADGGYRRGAPFALKPAVDEAIATLNPDNHPGISHVLVVQRTGQEVEWHDERDLWWHEAMESADIRHEPTFVEAEHPLFILYTSGTTGRPKGILHTTGGYLTQAAFTHWAVFDLKAETDVYWCTADIGWITGHSYVVYGPLINGATQVIYEGTPDTPHRGRWWEIVQKYKVSILYTAPTAIRTYMKWGEEVPDQFDLTSLRLLGSVGEPINPEAWMWYRRVIGGGSTPVVDTWWQTETGAIMISPLPGVTAAKPGSAQSPLPGIAVDVVDDDANSVPAGGGGYLVVSKPWPAMLRGIWGDLDRFKETYWSRFKNIYFAGDGAKRDDDGDIWLLGRVDDVMNVSGHRLSTTEIESSLVAHDAVAEAAVVGAADETTGQAVVAFVILRGEFAAAAQDDEGAAAIQEQLRTHVARQIGPIAKPRRILIVPELPKTRSGKIMRRLLRDVAENRTVGDATTLADSSVMALIKGKLG","length":664,"molWeight":72489,"crc64":"EE5E77315BF2F1A4","md5":"9F9F6E3046358F94D7B63251540E2699"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Binding site":15,"Modified residue":1},"uniParcId":"UPI001152F600"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZDW9","uniProtkbId":"A0A542ZDW9_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58479.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012729"}],"value":"chitinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012729"}],"value":"3.2.1.14"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58479.1"}],"value":"FB461_1892"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.","ecNumber":"3.2.1.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000822"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10053"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"value":"Belongs to the glycosyl hydrolase 18 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58479.1"}],"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":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":623,"modifier":"EXACT"}},"description":"chitinase","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5021949256"},{"type":"Domain","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"GH18","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51910"}]},{"type":"Region","location":{"start":{"value":464,"modifier":"EXACT"},"end":{"value":515,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":556,"modifier":"EXACT"},"end":{"value":576,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":556,"modifier":"EXACT"},"end":{"value":573,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10053"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023024"}],"id":"KW-0146","category":"Biological process","name":"Chitin degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023295"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01258"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023024"}],"id":"KW-0624","category":"Biological process","name":"Polysaccharide degradation"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58479.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58479.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58479.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_211349887.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZDW9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030246","properties":[{"key":"GoTerm","value":"F:carbohydrate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008061","properties":[{"key":"GoTerm","value":"F:chitin binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008843","properties":[{"key":"GoTerm","value":"F:endochitinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd12215","properties":[{"key":"EntryName","value":"ChiC_BD"},{"key":"MatchStatus","value":"2"}]},{"database":"CDD","id":"cd06548","properties":[{"key":"EntryName","value":"GH18_chitinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.50.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.10.10.20","properties":[{"key":"EntryName","value":"Carbohydrate-binding module superfamily 5/12"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003610","properties":[{"key":"EntryName","value":"CBM5/12"}]},{"database":"InterPro","id":"IPR036573","properties":[{"key":"EntryName","value":"CBM_sf_5/12"}]},{"database":"InterPro","id":"IPR011583","properties":[{"key":"EntryName","value":"Chitinase_II/V-like_cat"}]},{"database":"InterPro","id":"IPR029070","properties":[{"key":"EntryName","value":"Chitinase_insertion_sf"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR001223","properties":[{"key":"EntryName","value":"Glyco_hydro18_cat"}]},{"database":"InterPro","id":"IPR001579","properties":[{"key":"EntryName","value":"Glyco_hydro_18_chit_AS"}]},{"database":"InterPro","id":"IPR050314","properties":[{"key":"EntryName","value":"Glycosyl_Hydrlase_18"}]},{"database":"PANTHER","id":"PTHR11177","properties":[{"key":"EntryName","value":"CHITINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11177:SF317","properties":[{"key":"EntryName","value":"CHITINASE 12-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02839","properties":[{"key":"EntryName","value":"CBM_5_12"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF00704","properties":[{"key":"EntryName","value":"Glyco_hydro_18"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00495","properties":[{"key":"EntryName","value":"ChtBD3"},{"key":"MatchStatus","value":"2"}]},{"database":"SMART","id":"SM00636","properties":[{"key":"EntryName","value":"Glyco_18"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51055","properties":[{"key":"EntryName","value":"Carbohydrate binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF54556","properties":[{"key":"EntryName","value":"Chitinase insertion domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01095","properties":[{"key":"EntryName","value":"GH18_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51910","properties":[{"key":"EntryName","value":"GH18_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKIKQSRGAWRTAIGALGAAAVGLTTVLLATASPAVPDVPAGDSAINGYRNVGYFAQWGVYGRDFHVKNLDTSGAASQLTHINYSFANIDHNTNKCFIANKAAQEGFPEGSGDAYADYGKTYTAANSVSGEADKWDQPLAGSFNQLKQLKAKYPHIKVMISIGGWTYSKYFSQAAKTDASRKALVSSCIDLYLKGNVPVIDGFGGPGTAAGIFDGIDIDWEWPGSPNGQANNLVDPVNDRGNFKLLLKEFRAQLNALQSQTGKHYLLSGFLPANQVDIDAGGWNDPELFNYFDFGNIQGYDLWGAWDLTKTGHQANLYDDPADTRTADKRFSVDKAVKLYTSKGINPAKLGIGLAAYGRGWTNVSTNTPWASGNLRAATGTYEAGNDDYWRIKNVGTGYYDPVAGAAWRYDGSTWWSYDNPQSIQAKADYIVAKGLGGGMWWELSGDRNNELISTLNAKLVAAPQGPVDANNPTDPTDPTDPTDPTDPTDPTDPTDPTDPTDPNDPGTYPAWNASTVYNGGDRVVHNGVVYQAGWWTQGETPGTTGEWGVWRVVPGGGTTDPGNPGNPGGPGDPGTTYPAWSSSAVYVGGDVVTHNGVNYRAAWWTQGETPGTTGEWGVWRVV","length":623,"molWeight":66776,"crc64":"F2EEEA612512A45D","md5":"C9356AA5C24BE75E46FCD7615A45EEFE"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":1,"Region":2,"Compositional bias":1,"Active site":1},"uniParcId":"UPI00116FD279"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZDZ7","uniProtkbId":"A0A542ZDZ7_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":24,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"Polyphosphate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"2.7.4.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"value":"ATP-polyphosphate phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"value":"Polyphosphoric acid kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"value":"ppk"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58509.1"}],"value":"FB461_1923"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"Catalyzes the reversible transfer of the terminal phosphate of ATP to form a long-chain polyphosphate (polyP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[phosphate](n) + ATP = [phosphate](n+1) + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19573"},{"database":"Rhea","id":"RHEA-COMP:9859"},{"database":"Rhea","id":"RHEA-COMP:14280"},{"database":"ChEBI","id":"CHEBI:16838"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"An intermediate of this reaction is the autophosphorylated ppk in which a phosphate is covalently linked to a histidine residue through a N-P bond"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003800"}],"value":"Belongs to the polyphosphate kinase 1 (PPK1) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58509.1"}],"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":65,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"Polyphosphate kinase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13089"}]},{"type":"Domain","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"Polyphosphate kinase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02503"}]},{"type":"Domain","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":566,"modifier":"EXACT"}},"description":"Polyphosphate kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF17941"}]},{"type":"Domain","location":{"start":{"value":574,"modifier":"EXACT"},"end":{"value":745,"modifier":"EXACT"}},"description":"Polyphosphate kinase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13090"}]},{"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":"Active site","location":{"start":{"value":506,"modifier":"EXACT"},"end":{"value":506,"modifier":"EXACT"}},"description":"Phosphohistidine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}]},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":446,"modifier":"EXACT"},"end":{"value":446,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":476,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":539,"modifier":"EXACT"},"end":{"value":539,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":635,"modifier":"EXACT"},"end":{"value":635,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":663,"modifier":"EXACT"},"end":{"value":663,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00347"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58509.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58509.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A542ZDZ7","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9761456at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009358","properties":[{"key":"GoTerm","value":"C:polyphosphate kinase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008976","properties":[{"key":"GoTerm","value":"F:polyphosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006799","properties":[{"key":"GoTerm","value":"P:polyphosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd09165","properties":[{"key":"EntryName","value":"PLDc_PaPPK1_C1_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd09168","properties":[{"key":"EntryName","value":"PLDc_PaPPK1_C2_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.870.10:FF:000001","properties":[{"key":"EntryName","value":"Polyphosphate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.870.10","properties":[{"key":"EntryName","value":"Endonuclease Chain A"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1840.10","properties":[{"key":"EntryName","value":"Polyphosphate kinase middle domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.310","properties":[{"key":"EntryName","value":"Polyphosphate kinase N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00347","properties":[{"key":"EntryName","value":"Polyphosphate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003414","properties":[{"key":"EntryName","value":"PP_kinase"}]},{"database":"InterPro","id":"IPR041108","properties":[{"key":"EntryName","value":"PP_kinase_C_1"}]},{"database":"InterPro","id":"IPR024953","properties":[{"key":"EntryName","value":"PP_kinase_middle"}]},{"database":"InterPro","id":"IPR036830","properties":[{"key":"EntryName","value":"PP_kinase_middle_dom_sf"}]},{"database":"InterPro","id":"IPR025200","properties":[{"key":"EntryName","value":"PPK_C_dom2"}]},{"database":"InterPro","id":"IPR025198","properties":[{"key":"EntryName","value":"PPK_N_dom"}]},{"database":"InterPro","id":"IPR036832","properties":[{"key":"EntryName","value":"PPK_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR03705","properties":[{"key":"EntryName","value":"poly_P_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003917","properties":[{"key":"EntryName","value":"PRK05443.1-1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003918","properties":[{"key":"EntryName","value":"PRK05443.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003921","properties":[{"key":"EntryName","value":"PRK05443.2-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003922","properties":[{"key":"EntryName","value":"PRK05443.2-3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30218","properties":[{"key":"EntryName","value":"POLYPHOSPHATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30218:SF0","properties":[{"key":"EntryName","value":"POLYPHOSPHATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02503","properties":[{"key":"EntryName","value":"PP_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13090","properties":[{"key":"EntryName","value":"PP_kinase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17941","properties":[{"key":"EntryName","value":"PP_kinase_C_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13089","properties":[{"key":"EntryName","value":"PP_kinase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF015589","properties":[{"key":"EntryName","value":"PP_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56024","properties":[{"key":"EntryName","value":"Phospholipase D/nuclease"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF143724","properties":[{"key":"EntryName","value":"PHP14-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF140356","properties":[{"key":"EntryName","value":"PPK N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTEKSQPETNSVIGESSLAVDPTMEPSLAEHIAEHIADKARGKAAATLPALDVPEELEPLPADRFLDREISWLAFNKRVLELAEDESVPLLERARFLAIFASNLDEFFMVRVAGLKRRIATGIAVTAASGLSPHRVLEEISIRASRLMDRHARVFADEVRPALLAEGISIVHWGELGADEQERLRKYFRRQIFPVLTPLAVDPAHPFPYISGLSLNLAVVVRNPATGKEHFARVKVPPLLPRFIAVDDKGRPSPADSQVANPDTVSFVPIEEVIAEHLDVLFPGMEISEHHTFRVTRNEDVEVEEDDAENLLKAMEKELLRRRFGPPVRLEVAEGITERVASILTRELGVKASEVYTLPAPLDLTGLNSIADIERPNLQFPKFVPTTNHQLAEVERATPTNIFSVIRQRDVLLHHPYDSFSTSVQTFLEQAAADPNVLAIKQTLYRTSGDSPIVDALIDAADAGKQVLALVEIKARFDEQANISWARKLEHAGVHVVYGIVGLKTHCKLSLVVRQEADGLRRYVHVGTGNYHPKTARLYTDLGLLTCDPTVGQDVTRLFNQLSGYAPQTKFSRLLVAPRTVRVGLIARIERERRAALAGRKAWIKIKVNSVVDEQTIDALYRASQAGVEIDIVVRGICSIRPGVPGLSETIRVRSILGRYLEHSRVFAFANSGGPAIGDGPEAGPEVYIGSADLMHRNLDRRVEALVRIDDPGHIDYLLWLLDESTSDHTSSWHLDESGRWDRVNLGEDGPLIDLQSELIARQRRQLSSGR","length":771,"molWeight":85593,"crc64":"79614D24D431F1DF","md5":"50F8E3BE680B62CA455E50B17BE1E684"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":4,"Region":1,"Active site":1,"Binding site":6},"uniParcId":"UPI001153039D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZE29","uniProtkbId":"A0A542ZE29_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Phosphoribosylformylglycinamidine synthase subunit PurL"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"FGAM synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"6.3.5.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Formylglycinamide ribonucleotide amidotransferase subunit II"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"FGAR amidotransferase II"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"FGAR-AT II"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Glutamine amidotransferase PurL"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Phosphoribosylformylglycinamidine synthase subunit II"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"purL"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58605.1"}],"value":"FB461_2023"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Part of the phosphoribosylformylglycinamidine synthase complex involved in the purines biosynthetic pathway. Catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to yield formylglycinamidine ribonucleotide (FGAM) and glutamate. The FGAM synthase complex is composed of three subunits. PurQ produces an ammonia molecule by converting glutamine to glutamate. PurL transfers the ammonia molecule to FGAR to form FGAM in an ATP-dependent manner. PurS interacts with PurQ and PurL and is thought to assist in the transfer of the ammonia molecule from PurQ to PurL"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(2)-formyl-N(1)-(5-phospho-beta-D-ribosyl)glycinamide + L-glutamine + ATP + H2O = 2-formamido-N(1)-(5-O-phospho-beta-D-ribosyl)acetamidine + L-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17129"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:147286"},{"database":"ChEBI","id":"CHEBI:147287"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Purine metabolism; IMP biosynthesis via de novo pathway; 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Monomer. Part of the FGAM synthase complex composed of 1 PurL, 1 PurQ and 2 PurS subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Belongs to the FGAMS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58605.1"}],"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":26,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"Phosphoribosylformylglycinamidine synthase linker","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18072"}]},{"type":"Domain","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"PurM-like N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00586"}]},{"type":"Domain","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"PurM-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02769"}]},{"type":"Domain","location":{"start":{"value":470,"modifier":"EXACT"},"end":{"value":593,"modifier":"EXACT"}},"description":"PurM-like N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00586"}]},{"type":"Domain","location":{"start":{"value":607,"modifier":"EXACT"},"end":{"value":754,"modifier":"EXACT"}},"description":"PurM-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02769"}]},{"type":"Active site","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}]},{"type":"Active site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":115,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}]},{"type":"Binding site","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":67,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":289,"modifier":"EXACT"},"end":{"value":289,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":527,"modifier":"EXACT"},"end":{"value":527,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":564,"modifier":"EXACT"},"end":{"value":564,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":565,"modifier":"EXACT"},"end":{"value":565,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":567,"modifier":"EXACT"},"end":{"value":567,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022755"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00420"}],"id":"KW-0658","category":"Biological process","name":"Purine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58605.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58605.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142121643.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZE29","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9804441at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00074","properties":[{"key":"RectionId","value":"UER00128"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004642","properties":[{"key":"GoTerm","value":"F:phosphoribosylformylglycinamidine synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006189","properties":[{"key":"GoTerm","value":"P:'de novo' IMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02203","properties":[{"key":"EntryName","value":"PurL_repeat1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02204","properties":[{"key":"EntryName","value":"PurL_repeat2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1330.10:FF:000004","properties":[{"key":"EntryName","value":"Phosphoribosylformylglycinamidine synthase subunit PurL"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.650.10","properties":[{"key":"EntryName","value":"PurM-like C-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1330.10","properties":[{"key":"EntryName","value":"PurM-like, N-terminal domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00420","properties":[{"key":"EntryName","value":"PurL_2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010074","properties":[{"key":"EntryName","value":"PRibForGlyAmidine_synth_PurL"}]},{"database":"InterPro","id":"IPR041609","properties":[{"key":"EntryName","value":"PurL_linker"}]},{"database":"InterPro","id":"IPR010918","properties":[{"key":"EntryName","value":"PurM-like_C_dom"}]},{"database":"InterPro","id":"IPR036676","properties":[{"key":"EntryName","value":"PurM-like_C_sf"}]},{"database":"InterPro","id":"IPR016188","properties":[{"key":"EntryName","value":"PurM-like_N"}]},{"database":"InterPro","id":"IPR036921","properties":[{"key":"EntryName","value":"PurM-like_N_sf"}]},{"database":"NCBIfam","id":"TIGR01736","properties":[{"key":"EntryName","value":"FGAM_synth_II"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002290","properties":[{"key":"EntryName","value":"purL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43555","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43555:SF1","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYLFORMYLGLYCINAMIDINE SYNTHASE SUBUNIT PURL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00586","properties":[{"key":"EntryName","value":"AIRS"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02769","properties":[{"key":"EntryName","value":"AIRS_C"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF18072","properties":[{"key":"EntryName","value":"FGAR-AT_linker"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001587","properties":[{"key":"EntryName","value":"FGAM_synthase_II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56042","properties":[{"key":"EntryName","value":"PurM C-terminal domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF55326","properties":[{"key":"EntryName","value":"PurM N-terminal domain-like"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSETANHQAPILDTVERAAATPDEPQPYAELGLKADEYDRIRELLGRRPTAAELAMYSVMWSEHCSYKSSKVHLRKFGDATTEEMKKHLLVGMGENAGVVDIGDGWAVTFKVESHNHPSFVEPYQGAATGVGGIVRDIISMGARPVAVMDQLRFGAVDHPDTARVVHGVVAGVGGYGNSLGLPNIGGELVFDSSYQGNPLVNALCLGVLRHEDIHLANASGVGNKVVLFGARTGGDGIGGASILASETFEDGVPAKRPSVQVGDPFMEKVLIECCLELYKAGVVEGIQDLGAAGISCATSELASNGEGGMHVWLDDVLLRDPTLNAGEILMSESQERMMAVVTPEKLDEFLAITSKWDVESSVVGEVNDSGRLTIDHHGQRIVDVDPRTVAHEGPVYDRPYARPQWQDALNRDSVSTAEGRINYARPSTGDELRATAMRLLGSPNLASPAWVTNQYDRFVQGNTALAQPDDSGVIRVDESTGLGVALATDANGRYAKLDPRTGAQLALAEAYRNVATVGARPLAVTDCLNFGTPEHPATMWQLVEAIEGLAEACKELGVPVTGGNVSLYNTTGDPDESDSSIHPTPVVGVLGVLDDVRAAIPMGWSEAGLAVMLLGRTRGELDGSAWADVVHGQLGGVPPIVDFDAERSLAELLQAARSAGVVAGAHDLSEGGLSQGLFEAALRHGYGVTVNLDAIRERDGINQFEALFSESTARVLVAVPSEKVAAFTSLAENHGVPAAVIGTTTSREDATVNVAGSFEVPLAEARELFEGTLPKLFG","length":779,"molWeight":82357,"crc64":"DD5E5E53E3A4BE83","md5":"958EBFC769A4F3C280FA490DE7F172AC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":5,"Active site":2,"Binding site":13},"uniParcId":"UPI00115201CE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZE43","uniProtkbId":"A0A542ZE43_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":22,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58614.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00020771"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000515"}],"value":"Delta-aminolevulinic acid dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012053"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000515"}],"value":"4.2.1.24"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58614.1"}],"value":"FB461_2032"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025628"}],"value":"Catalyzes an early step in the biosynthesis of tetrapyrroles. Binds two molecules of 5-aminolevulinate per subunit, each at a distinct site, and catalyzes their condensation to form porphobilinogen"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 5-aminolevulinate = porphobilinogen + 2 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58126"},{"database":"ChEBI","id":"CHEBI:356416"}],"ecNumber":"4.2.1.24","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047651"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000515"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004694"}],"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011823"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000515"}],"value":"Homooctamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008055"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004161"}],"value":"Belongs to the ALAD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58614.1"}],"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":335,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001415-1"}]},{"type":"Active site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001415-1"}]},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:356416"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001415-2"}],"ligand":{"name":"5-aminolevulinate","id":"ChEBI:CHEBI:356416","label":"1"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:356416"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001415-2"}],"ligand":{"name":"5-aminolevulinate","id":"ChEBI:CHEBI:356416","label":"1"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:356416"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001415-2"}],"ligand":{"name":"5-aminolevulinate","id":"ChEBI:CHEBI:356416","label":"2"}},{"type":"Binding site","location":{"start":{"value":312,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:356416"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001415-2"}],"ligand":{"name":"5-aminolevulinate","id":"ChEBI:CHEBI:356416","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023133"}],"id":"KW-0350","category":"Biological process","name":"Heme biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000515"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000515"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58614.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58614.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58614.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142121667.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZE43","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9805001at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00251","properties":[{"key":"RectionId","value":"UER00318"}]},{"database":"Proteomes","id":"UP000315389","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:0004655","properties":[{"key":"GoTerm","value":"F:porphobilinogen synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.20.20.70:FF:000019","properties":[{"key":"EntryName","value":"Delta-aminolevulinic acid dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001731","properties":[{"key":"EntryName","value":"ALAD"}]},{"database":"InterPro","id":"IPR030656","properties":[{"key":"EntryName","value":"ALAD_AS"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"NCBIfam","id":"NF006762","properties":[{"key":"EntryName","value":"hemB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11458","properties":[{"key":"EntryName","value":"DELTA-AMINOLEVULINIC ACID DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11458:SF0","properties":[{"key":"EntryName","value":"DELTA-AMINOLEVULINIC ACID DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00490","properties":[{"key":"EntryName","value":"ALAD"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001415","properties":[{"key":"EntryName","value":"Porphbilin_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00144","properties":[{"key":"EntryName","value":"DALDHYDRTASE"}]},{"database":"SMART","id":"SM01004","properties":[{"key":"EntryName","value":"ALAD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00169","properties":[{"key":"EntryName","value":"D_ALA_DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPHLRPRRARRTPAIRELLTQTRLHPRDLVLPVFVKEGLQEPAEIRSMPGVYQHTIASVRDLTEQARDAGLGGIMVFAVPQSRDALGSGATDPDGFFAAAIRAVAQAAEGALVVMSDICLDEFTDHGHCGVLRPDGTIDNDATIDRYAQMAVIHADAGADVVGLSGMMDGQTAEVRAALDDAGLIDTLILSYTAKYASAFYGPFRDAVESTLEGDRRTYQMDPANRREALRALDIEEASGADIVMVKPAGSYLDVLADLAAASSVPVAAYQVSGEYAMIEAASANGWIDRERVIVESLIAIRRAGADVILTYYALEAAAWLAGSRRDALPVNPPVASGSAGRVADAGAGSGRLDEFPAGPIPRADEVGR","length":369,"molWeight":39126,"crc64":"1D607F918E866C0F","md5":"CB43347089F50F675115D0F4AB4CFE9E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Active site":2,"Binding site":4},"uniParcId":"UPI0011525F26"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZE44","uniProtkbId":"A0A542ZE44_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2019-10-16","entryVersion":21,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58612.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"Glutamyl-tRNA reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"GluTR"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"1.2.1.70"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"hemA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58612.1"}],"value":"FB461_2030"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"Catalyzes the NADPH-dependent reduction of glutamyl-tRNA(Glu) to glutamate 1-semialdehyde (GSA)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-4-amino-5-oxopentanoate + tRNA(Glu) + NADP(+) = L-glutamyl-tRNA(Glu) + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12344"},{"database":"Rhea","id":"RHEA-COMP:9663"},{"database":"Rhea","id":"RHEA-COMP:9680"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57501"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78520"}],"ecNumber":"1.2.1.70","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"Possesses an unusual extended V-shaped dimeric structure with each monomer consisting of three distinct domains arranged along a curved 'spinal' alpha-helix. The N-terminal catalytic domain specifically recognizes the glutamate moiety of the substrate. The second domain is the NADPH-binding domain, and the third C-terminal domain is responsible for dimerization"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"During catalysis, the active site Cys acts as a nucleophile attacking the alpha-carbonyl group of tRNA-bound glutamate with the formation of a thioester intermediate between enzyme and glutamate, and the concomitant release of tRNA(Glu). The thioester intermediate is finally reduced by direct hydride transfer from NADPH, to form the product GSA"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"value":"Belongs to the glutamyl-tRNA reductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58612.1"}],"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":153,"modifier":"EXACT"}},"description":"Glutamyl-tRNA reductase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF05201"}]},{"type":"Domain","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":302,"modifier":"EXACT"}},"description":"Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01488"}]},{"type":"Active site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000445-1"}]},{"type":"Binding site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000445-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000445-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000445-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":117,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000445-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000445-3"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Important for activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000445-4"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00087"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58612.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58612.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58612.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_170222706.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZE44","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00251","properties":[{"key":"RectionId","value":"UER00316"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008883","properties":[{"key":"GoTerm","value":"F:glutamyl-tRNA reductase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0033014","properties":[{"key":"GoTerm","value":"P:tetrapyrrole biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.30.460.30","properties":[{"key":"EntryName","value":"Glutamyl-tRNA reductase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00087","properties":[{"key":"EntryName","value":"Glu_tRNA_reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000343","properties":[{"key":"EntryName","value":"4pyrrol_synth_GluRdtase"}]},{"database":"InterPro","id":"IPR015895","properties":[{"key":"EntryName","value":"4pyrrol_synth_GluRdtase_N"}]},{"database":"InterPro","id":"IPR036343","properties":[{"key":"EntryName","value":"GluRdtase_N_sf"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR006151","properties":[{"key":"EntryName","value":"Shikm_DH/Glu-tRNA_Rdtase"}]},{"database":"NCBIfam","id":"NF000750","properties":[{"key":"EntryName","value":"PRK00045.3-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43013","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43013:SF1","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05201","properties":[{"key":"EntryName","value":"GlutR_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01488","properties":[{"key":"EntryName","value":"Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000445","properties":[{"key":"EntryName","value":"4pyrrol_synth_GluRdtase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69742","properties":[{"key":"EntryName","value":"Glutamyl tRNA-reductase catalytic, 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":"MNLVALSASHRSTDLELVACLSHRAAGLDRALAARLGTGVIVLATCNRFEIYLETRGDRMAARSQALGVIAGECLMDEASVAAAFSTFEGQAAVEHLFSVASGLESMVIGEREVTRQVSRALEASRAVGTLSATLDRLFQDAIRVAREVDAETGLREHGRSVATVGLDVAADALPSRPAVPGRGFSGRSVLLIGTGNYAALTYAALRARGCTDIAVYSHTGRARHFARERQVEIVGRSELAATLRRVDVIVSCSGRSGRIVTPETLRGAQAQVLIDLSLERDIDPACAQNPRVRLIDLDTVRTHAPELGEAPVLSARLIIEAGIGRFRARLDERLLASTLADEVARAEQDIARERSALLDAFGEFLDPAEIEYLVRKVRLERKRDLHARITRLKAAAHT","length":399,"molWeight":43070,"crc64":"CE644ECADA6E2199","md5":"FE4A503A5F5FA637AD4CC900FA5125AF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"DOMAIN":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":5,"Site":1},"uniParcId":"UPI0011756D1D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZE52","uniProtkbId":"A0A542ZE52_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2019-10-16","entryVersion":23,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58613.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Porphobilinogen deaminase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"PBG"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"2.5.1.61"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Hydroxymethylbilane synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"HMBS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Pre-uroporphyrinogen synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"hemC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58613.1"}],"value":"FB461_2031"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002869"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Tetrapolymerization of the monopyrrole PBG into the hydroxymethylbilane pre-uroporphyrinogen in several discrete steps"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 porphobilinogen + H2O = hydroxymethylbilane + 4 NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13185"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:57845"},{"database":"ChEBI","id":"CHEBI:58126"}],"ecNumber":"2.5.1.61","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048169"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"dipyrromethane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60342"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Binds 1 dipyrromethane group covalently."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"The porphobilinogen subunits are added to the dipyrromethane group"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005638"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"value":"Belongs to the HMBS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58613.1"}],"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":8,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01379"}]},{"type":"Domain","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Porphobilinogen deaminase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03900"}]},{"type":"Domain","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":609,"modifier":"EXACT"}},"description":"Tetrapyrrole biosynthesis uroporphyrinogen III synthase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02602"}]},{"type":"Region","location":{"start":{"value":620,"modifier":"EXACT"},"end":{"value":639,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":629,"modifier":"EXACT"},"end":{"value":639,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Modified residue","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"S-(dipyrrolylmethanemethyl)cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00260"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"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_00260"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58613.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58613.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58613.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142121665.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZE52","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"9810298at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000315389","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:0004418","properties":[{"key":"GoTerm","value":"F:hydroxymethylbilane synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004852","properties":[{"key":"GoTerm","value":"F:uroporphyrinogen-III synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.40.190.10:FF:000005","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10090","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.190.10","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.160.40","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00260","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036108","properties":[{"key":"EntryName","value":"4pyrrol_syn_uPrphyn_synt_sf"}]},{"database":"InterPro","id":"IPR003754","properties":[{"key":"EntryName","value":"4pyrrol_synth_uPrphyn_synth"}]},{"database":"InterPro","id":"IPR000860","properties":[{"key":"EntryName","value":"HemC"}]},{"database":"InterPro","id":"IPR022419","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_cofac_BS"}]},{"database":"InterPro","id":"IPR022417","properties":[{"key":"EntryName","value":"Porphobilin_deaminase_N"}]},{"database":"InterPro","id":"IPR022418","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C"}]},{"database":"InterPro","id":"IPR036803","properties":[{"key":"EntryName","value":"Porphobilinogen_deaminase_C_sf"}]},{"database":"NCBIfam","id":"TIGR00212","properties":[{"key":"EntryName","value":"hemC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11557:SF0","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN DEAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02602","properties":[{"key":"EntryName","value":"HEM4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01379","properties":[{"key":"EntryName","value":"Porphobil_deam"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03900","properties":[{"key":"EntryName","value":"Porphobil_deamC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00151","properties":[{"key":"EntryName","value":"PORPHBDMNASE"}]},{"database":"SUPFAM","id":"SSF69618","properties":[{"key":"EntryName","value":"HemD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53850","properties":[{"key":"EntryName","value":"Periplasmic binding protein-like II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54782","properties":[{"key":"EntryName","value":"Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00533","properties":[{"key":"EntryName","value":"PORPHOBILINOGEN_DEAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTLPDRPLRLGTRGSALARTQSGLVVSALEALGVRVEIVPIVTSGDRSTAPLTQIGGTGVFVTAVRDALLADRCDLAVHSLKDLPVDGVPGLTLAAVPARADVRDALCARDGYRLADLPPGAVIGTGSHRRALHLTALRPDLRVVGLRGNVDSRVERVRSGELDAVVLAAAGLERLGLLASVTEFFAPLDSPPAPGQGALAIECRSEDEATVALLAALDDRATRHAVIAERAVLARLDAGCTAPVGAWGRIDGDELLVDALIWREGGDEPLRARAAWPIRAAGGSTTESAGADGGSQAVAGTALDAAATRATAGSGSAGSASTASAAATRATASSGAGLTEADAAALGTWVAEDLLRQGADAVEGIGAKPAPTIVVPIPADGSSRWEDCAREAGLVPESIELLSAEYEHDAPAVAALVMDLGRGSYTHLALTSSRALTALKRAGEPLAAVQRVGGFTVAAIGPATAAAAIAAGLSVGLVPAEDHSAHGLAAGLLRTRHAAGSAAIPHSDLADGRLAAELRGAGWRVDEVIAYRIHAALPAVTDWSLRPPDLVFLTSGSAAHAWHQLIAATPAIRGAGAIVLGRGAADAAAALGIPVIATATAADAPSLTRAMRNAREIVNGHNEGGKTRPPPPAPTEGA","length":639,"molWeight":64358,"crc64":"7285651BB339A35A","md5":"E89BB423DC8844459D0FAE9F7D6BF54F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":1,"Compositional bias":1,"Modified residue":1},"uniParcId":"UPI00114F78C2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A542ZE74","uniProtkbId":"A0A542ZE74_RARFA","entryAudit":{"firstPublicDate":"2019-10-16","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2019-10-16","entryVersion":27,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Rarobacter faecitabidus","taxonId":13243,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58644.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Micrococcales","Rarobacteraceae","Rarobacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011971"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Orotate phosphoribosyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"OPRT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"OPRTase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011971"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"2.4.2.10"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"pyrE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58644.1"}],"value":"FB461_2062"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Catalyzes the transfer of a ribosyl phosphate group from 5-phosphoribose 1-diphosphate to orotate, leading to the formation of orotidine monophosphate (OMP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"orotidine 5'-phosphate + diphosphate = orotate + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10380"},{"database":"ChEBI","id":"CHEBI:30839"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57538"},{"database":"ChEBI","id":"CHEBI:58017"}],"ecNumber":"2.4.2.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004889"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from orotate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family. PyrE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58644.1"}],"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":76,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58017"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"5-phospho-alpha-D-ribose 1-diphosphate","id":"ChEBI:CHEBI:58017","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30839"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"orotate","id":"ChEBI:CHEBI:30839"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30839"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"ligand":{"name":"orotate","id":"ChEBI:CHEBI:30839"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01208"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"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_01208"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-EVNPQP3TP7DC4","citationType":"submission","authors":["Klenk H.-P."],"title":"Sequencing the genomes of 1000 actinobacteria strains.","publicationDate":"JUN-2019","submissionDatabase":"EMBL/GenBank/DDBJ databases"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58644.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}],"value":"DSM 4813","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"TQL58644.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000315389"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"VFOS01000003","properties":[{"key":"ProteinId","value":"TQL58644.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_142121719.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAAASV010000002.1"}]},{"database":"AlphaFoldDB","id":"A0A542ZE74","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"1493031at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00119"}]},{"database":"Proteomes","id":"UP000315389","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004588","properties":[{"key":"GoTerm","value":"F:orotate phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.2020:FF:000029","properties":[{"key":"EntryName","value":"Orotate phosphoribosyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01208","properties":[{"key":"EntryName","value":"PyrE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023031","properties":[{"key":"EntryName","value":"OPRT"}]},{"database":"InterPro","id":"IPR004467","properties":[{"key":"EntryName","value":"Or_phspho_trans_dom"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"NCBIfam","id":"TIGR00336","properties":[{"key":"EntryName","value":"pyrE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19278","properties":[{"key":"EntryName","value":"OROTATE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19278:SF9","properties":[{"key":"EntryName","value":"URIDINE 5'-MONOPHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSNETFSPTPREQLRDLIKELAVVHGKVTLASGKEADYYVDLRRVTLHHLAAPLVGHVLLDHLEEAGYSTADVDAVGGLTMGADPVALALLHAAASRGQDLDAFVVRKEGKAHGLQRRIEGPDVAGRNVVAVEDTSTTGGSVLTAVEALREAGANVVAVAVIVDRDTGAREKIEAAGLEYLYLYGLADLGLS","length":192,"molWeight":20233,"crc64":"D98EC613DB9E86B1","md5":"043EDB4E554D618DAE37C58AB589E818"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":7},"uniParcId":"UPI00114FD949"}}]}