{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AVU9","uniProtkbId":"R1AVU9_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":64,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01318.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"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":"EOD01318.1"}],"value":"L21TH_0672"}]}],"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":"EOD01318.1"}],"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":99,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"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":117,"modifier":"EXACT"},"end":{"value":117,"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":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":160,"modifier":"EXACT"},"end":{"value":161,"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":192,"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":215,"modifier":"EXACT"},"end":{"value":217,"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":291,"modifier":"EXACT"},"end":{"value":291,"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":"UP000013378"}],"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-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01318.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01318.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000066","properties":[{"key":"ProteinId","value":"EOD01318.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006308916.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000066.1"}]},{"database":"AlphaFoldDB","id":"R1AVU9","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_0672","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.661","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0820","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9793973at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR006638","properties":[{"key":"EntryName","value":"Elp3/MiaA/NifB-like_rSAM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00729","properties":[{"key":"EntryName","value":"Elp3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSKIDLKSMSINQLKSLYIELGEKTFRAEQTFKWIHGKMIESIDDITVLSKKLRDKLNEKGKITNLKIVKRLDSKLDGTKKYLFALEDGNIIESVMMEYQHGISVCVSTQVGCKMGCTFCASTKDGLVRNLTAGEILDQIYQIQKDMDIKVSNIVLMGSGEPLDNYDNVLKFLEIIHHKHGQNVGYRHITLSTCGIVPKIYELAEENLPITLSISLHSPFQHSREEIMPIARKYSIKEIVDACKYYIEKTNRRITFEYTLIEGVNDSKKEALELSHILEGLLCHVNLIPLNPIKETQLSSTKISYVEEFKRILEKNKISVTVRRKMGGDINAACGQLRRDYLKNE","length":345,"molWeight":39420,"crc64":"A0B1AE525A61912C","md5":"D2B3EDF2035455734415EA84C6AC383D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI00032E7141"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AX44","uniProtkbId":"R1AX44_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":63,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01783.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"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":"EOD01783.1"}],"value":"L21TH_0138"}]}],"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":"EOD01783.1"}],"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":4,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":303,"modifier":"EXACT"},"end":{"value":527,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":508,"modifier":"EXACT"},"end":{"value":508,"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":510,"modifier":"EXACT"},"end":{"value":510,"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":14,"modifier":"EXACT"},"end":{"value":14,"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":14,"modifier":"EXACT"},"end":{"value":14,"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":15,"modifier":"EXACT"},"end":{"value":20,"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":55,"modifier":"EXACT"},"end":{"value":55,"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":72,"modifier":"EXACT"},"end":{"value":72,"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":72,"modifier":"EXACT"},"end":{"value":72,"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":142,"modifier":"EXACT"},"end":{"value":142,"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":149,"modifier":"EXACT"},"end":{"value":151,"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":189,"modifier":"EXACT"},"end":{"value":194,"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":189,"modifier":"EXACT"},"end":{"value":194,"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":225,"modifier":"EXACT"},"end":{"value":225,"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":225,"modifier":"EXACT"},"end":{"value":225,"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":243,"modifier":"EXACT"},"end":{"value":243,"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":355,"modifier":"EXACT"},"end":{"value":355,"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":383,"modifier":"EXACT"},"end":{"value":386,"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":406,"modifier":"EXACT"},"end":{"value":406,"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":463,"modifier":"EXACT"},"end":{"value":463,"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":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01783.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01783.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000020","properties":[{"key":"ProteinId","value":"EOD01783.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006306236.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000020.1"}]},{"database":"AlphaFoldDB","id":"R1AX44","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_0138","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.136","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0504","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9801107at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00159","properties":[{"key":"RectionId","value":"UER00277"}]},{"database":"Proteomes","id":"UP000013378","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":"MPTKYIFITGGVVSSLGKGITAASLGQLLKARGLKVTIQKFDPYINVDPGTMSPYQHGEVFVTDDGAETDLDLGHYERFIDINLSKNSNVTTGKIYWSVINKERKGAYLGGTVQVIPHITNEIKDRVFRVAKEKEVDVVITEIGGTVGDIESLPFLEAIRQIKYDVGKENVMYLHVTLVPYLTKAGELKTKPTQHSVKELRSIGIQPDLVVCRAEHPLNKELKEKIALFCDLDYSDVVQNLDADTLYEVPLLLEDEGLPQKVMNHLKLKCNDPDLTEWKEIVDKLKNPKGKVKIALVGKYVELKDAYISVAEALRHAGIANEVDIDIDWVHSEKLNESNCEELLKEADGILVPGGFGDRGIEGKICAIKYARENKIPFLGICLGMQLAVVEFAKNVLGLEGAHSSELDPKTEYPVIDLMPEQMDIEEMGGTMRLGLYPCKIAEGTKAKEAYDEELIYERHRHRYEFNNEFRDRLIEKGLVVSGISPDERLVEIVELKEHPWFVASQFHPEFKSRPTRSHPLFRDFVKAAKGNS","length":533,"molWeight":59888,"crc64":"6CED6EF0C083A1F1","md5":"079D4B6A4E7938C7F4CC3F70F36168F3"},"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":17},"uniParcId":"UPI00033047BE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AX55","uniProtkbId":"R1AX55_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-06-26","entryVersion":68,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01257.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"6.3.2.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-A2pm-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Meso-diaminopimelate-adding enzyme"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-L-Ala-D-Glu:meso-diaminopimelate ligase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-MurNAc-tripeptide synthetase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"UDP-N-acetylmuramyl-tripeptide synthetase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"murE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01257.1"}],"value":"L21TH_0611"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004752"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01257.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":23,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":458,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":30,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":110,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":152,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:83900"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate","id":"ChEBI:CHEBI:83900"}},{"type":"Binding site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":404,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":456,"modifier":"EXACT"},"end":{"value":456,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Modified residue","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"N6-carboxylysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0131","category":"Biological process","name":"Cell cycle"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022618"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0132","category":"Biological process","name":"Cell division"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01257.1"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01257.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01257.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000066","properties":[{"key":"ProteinId","value":"EOD01257.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006308827.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000066.1"}]},{"database":"AlphaFoldDB","id":"R1AX55","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_0611","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.600","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0769","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9800958at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008765","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylmuramoylalanyl-D-glutamate-2,6-diaminopimelate ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051301","properties":[{"key":"GoTerm","value":"P:cell division"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008360","properties":[{"key":"GoTerm","value":"P:regulation of cell shape"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.90.190.20","properties":[{"key":"EntryName","value":"Mur ligase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.10","properties":[{"key":"EntryName","value":"Mur-like, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1390.10","properties":[{"key":"EntryName","value":"MurE/MurF, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00208","properties":[{"key":"EntryName","value":"MurE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036565","properties":[{"key":"EntryName","value":"Mur-like_cat_sf"}]},{"database":"InterPro","id":"IPR004101","properties":[{"key":"EntryName","value":"Mur_ligase_C"}]},{"database":"InterPro","id":"IPR036615","properties":[{"key":"EntryName","value":"Mur_ligase_C_dom_sf"}]},{"database":"InterPro","id":"IPR013221","properties":[{"key":"EntryName","value":"Mur_ligase_cen"}]},{"database":"InterPro","id":"IPR000713","properties":[{"key":"EntryName","value":"Mur_ligase_N"}]},{"database":"InterPro","id":"IPR035911","properties":[{"key":"EntryName","value":"MurE/MurF_N"}]},{"database":"InterPro","id":"IPR005761","properties":[{"key":"EntryName","value":"UDP-N-AcMur-Glu-dNH2Pim_ligase"}]},{"database":"NCBIfam","id":"TIGR01085","properties":[{"key":"EntryName","value":"murE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001124","properties":[{"key":"EntryName","value":"PRK00139.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001126","properties":[{"key":"EntryName","value":"PRK00139.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135","properties":[{"key":"EntryName","value":"MUR LIGASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23135:SF4","properties":[{"key":"EntryName","value":"UDP-N-ACETYLMURAMOYL-L-ALANYL-D-GLUTAMATE--2,6-DIAMINOPIMELATE LIGASE MURE HOMOLOG, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01225","properties":[{"key":"EntryName","value":"Mur_ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02875","properties":[{"key":"EntryName","value":"Mur_ligase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08245","properties":[{"key":"EntryName","value":"Mur_ligase_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53623","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53244","properties":[{"key":"EntryName","value":"MurD-like peptide ligases, peptide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF63418","properties":[{"key":"EntryName","value":"MurE/MurF N-terminal domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MVLKDLIRKLELIDVIGDLTKDITDITYDSREVVNGSLFVAIVGFKTDGHKYINDAIEKGAKAVIVERDVQLDKNITVIKVNNSRKALAKVSSTFYDRPSSKINVIGVTGTNGKTSVTYLIKSIFDACKRKTGIIGTIGSVIENKVTSTNNTTPESLDLQSILNDMVNTGLDTCIMEVSSHSLELDRVAFCDFNVGIFTNLSVDHLDFHKSIENYLNAKAKLFYKTKNFNIINIDDKYGKKISSKIRKLDVPLLTYGTDSNADIIADNIVYSAEGVSFELITPKGEIDIKMNIPGLFSVYNGLAAAACGYAYNIELENIKEGLESVKGVKGRFEVVPTDKDFTVIIDYAHTPDGLEKVMETISQFAKGRKIIVFGAGGDRPRTRRPLMGEVAAKYSDLSIVTSDNPRTEEPNKIIEDIIEGIERLDGKYVAITDRKEAIRYALKNSQPNDVILLAGKGHEMYQIIGNKRIPFNEKEIVLEILKEIN","length":486,"molWeight":53895,"crc64":"411A73EF2367BE02","md5":"9D3900E82DD59E28624472E49CB9C267"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":10,"Modified residue":1},"uniParcId":"UPI00032F2555"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CBA7","uniProtkbId":"R1CBA7_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":65,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99594.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"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":"EOC99594.1"}],"value":"L21TH_2367"}]}],"comments":[{"texts":[{"evidences":[{"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":"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":"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":"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":"EOC99594.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":327,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":674,"modifier":"EXACT"},"end":{"value":864,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":933,"modifier":"EXACT"},"end":{"value":1067,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":401,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":550,"modifier":"EXACT"},"end":{"value":932,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":933,"modifier":"EXACT"},"end":{"value":1067,"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":284,"modifier":"EXACT"},"end":{"value":284,"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":284,"modifier":"EXACT"},"end":{"value":284,"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":284,"modifier":"EXACT"},"end":{"value":284,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":298,"modifier":"EXACT"},"end":{"value":298,"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":300,"modifier":"EXACT"},"end":{"value":300,"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":300,"modifier":"EXACT"},"end":{"value":300,"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":710,"modifier":"EXACT"},"end":{"value":710,"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":749,"modifier":"EXACT"},"end":{"value":749,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":751,"modifier":"EXACT"},"end":{"value":751,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":755,"modifier":"EXACT"},"end":{"value":755,"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":780,"modifier":"EXACT"},"end":{"value":780,"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":781,"modifier":"EXACT"},"end":{"value":781,"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":782,"modifier":"EXACT"},"end":{"value":782,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":783,"modifier":"EXACT"},"end":{"value":783,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":823,"modifier":"EXACT"},"end":{"value":823,"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":823,"modifier":"EXACT"},"end":{"value":823,"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":823,"modifier":"EXACT"},"end":{"value":823,"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":835,"modifier":"EXACT"},"end":{"value":835,"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":835,"modifier":"EXACT"},"end":{"value":835,"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":835,"modifier":"EXACT"},"end":{"value":835,"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":835,"modifier":"EXACT"},"end":{"value":835,"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":835,"modifier":"EXACT"},"end":{"value":835,"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":837,"modifier":"EXACT"},"end":{"value":837,"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":837,"modifier":"EXACT"},"end":{"value":837,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99594.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99594.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000262","properties":[{"key":"ProteinId","value":"EOC99594.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006316696.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000262.1"}]},{"database":"AlphaFoldDB","id":"R1CBA7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2367","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2321","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0458","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"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":"UP000013378","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:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000026","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_A","properties":[{"key":"EntryName","value":"CPSase_L_chain_A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKNNDIKKVLVIGSGPIIIGQAAEFDYSGTQACQALKEEGVEVVLINSNPATIMTDKEIADKVYIEPLTVEFVEKVIEKERPDSLLAGMGGQTGLNLAVELSDKGILDKYDVKVIGTSIESIKKGEDRESFRVLMEEINQPTIESKIVTDLEIGIDFAEKIGYPVVVRPAYTLGGTGGGIAENEDELKEILSQGLSLSRVGQVLLEKSIKGWKEIEYEVMRDSYGNCITVCNMENIDPVGVHTGDSIVVAPSQTLSDKEYQMLRTAAVDIINAIGIEGGCNVQFALDPDSFNYVVIEVNPRVSRSSALASKATGYPIAKVAAKIALGYGLDEIKNAVTQKTYACFEPSLDYVVVKIPKWPFDKFRQAKRYLGTKMMATGEIMAIGNNFEAAFLKGIRSLEIGKYSLVHEEAAKRSLKELKERVMVPDDERIFDLAEMLRRDYSIQKVSEITGIDRFFISKIKWIVDQEEKLRNSKVEDLNKEWLYLLKKKGFSDKGIADLLRVSPMYIYEKRKMWGIESVYKMVDTCAGEFEAMTPYYYSTYDEFDEVEVNDKKKIMVIGSGPIRIGQGIEFDYCSVHSVLALKKLGIETIIVNNNPETVSTDFDIADKLYFEPLTEEDVLNIIEKERPDGVILQFGGQTAIKLANFLKEMDIPVLGTKPDKIDAAEDRKKFDELLERLNIKRPKGKAIWSIEEGLNEAKRLGYPILVRPSYVLGGMGMEITYNKEELTQYLKEALKRDSKNPVLIDKYLLGKEIEVDAICDGEDILIPGIMEHLERAGVHSGDSITIYPSQNISENTKKKILEYTKKIALGLDVIAMVNIQFIEYEKELYIIEVNPRSSRTVPYISKVSGVPIVELATRVMLGEKLKKLQYGIGLYKESDLIAVKVPVFSTQKLPQVEVSLGPEMRSTGEVLGVGTTLEQALYKGLIAAGMNLDKKNKTILVTLNNHDKERFIPTAKELEKLGYKFMATEGTAKLLRSQGIEVTETKKIREGVPNILDIIRSGMIDFVINTPTKGNDSKRDGFVIRRIAVETSIDVFTSLDTVEALVDILKDKITNGELDVYEIK","length":1067,"molWeight":119294,"crc64":"1094927FD766FAAA","md5":"8340798B9AD6052C3C1FAC48FE48F41A"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":3,"Binding site":38},"uniParcId":"UPI00032F61BA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CDD6","uniProtkbId":"R1CDD6_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":53,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00305.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Asp/Glu-ADT subunit B"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"6.3.5.6"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"6.3.5.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Glutamyl-tRNA(Gln) amidotransferase subunit B"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Glu-ADT subunit B"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"gatB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00305.1"}],"value":"L21TH_1656"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097267"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Catalytic subunit of the Asp/Glu-tRNA(Asn/Gln) amidotransferase complex GatCAB. GatCAB allows the formation of correctly charged Asn-tRNA(Asn) or Gln-tRNA(Gln) through the multi-step transamidation of misacylated Asp-tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction takes place in the presence of glutamine and ATP through an activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln). This subunit specifically recognizes tRNA(Gln) and tRNA(Asn), and mediates the transamidation of misloaded Glu and Asp respectively by catalyzing formation of the activated gamma-phospho-intermediate and its subsequent aminolysis using ammonia produced by the gatA subunit. Recognizes the first base pair and the D-loop of its specific tRNA substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-phospho-L-aspartyl-tRNA(Asn) + NH4(+) = L-asparaginyl-tRNA(Asn) + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57920"},{"database":"Rhea","id":"RHEA-COMP:9674"},{"database":"Rhea","id":"RHEA-COMP:15033"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:78515"},{"database":"ChEBI","id":"CHEBI:142450"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"5-phospho-L-glutamyl-tRNA(Gln) + NH4(+) = L-glutaminyl-tRNA(Gln) + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57912"},{"database":"Rhea","id":"RHEA-COMP:9681"},{"database":"Rhea","id":"RHEA-COMP:15032"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:78521"},{"database":"ChEBI","id":"CHEBI:142449"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-tRNA(Asn) + ATP = 4-phospho-L-aspartyl-tRNA(Asn) + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57916"},{"database":"Rhea","id":"RHEA-COMP:9677"},{"database":"Rhea","id":"RHEA-COMP:15033"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:78516"},{"database":"ChEBI","id":"CHEBI:142450"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartyl-tRNA(Asn) + L-glutamine + ATP + H2O = L-asparaginyl-tRNA(Asn) + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14513"},{"database":"Rhea","id":"RHEA-COMP:9674"},{"database":"Rhea","id":"RHEA-COMP:9677"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:78515"},{"database":"ChEBI","id":"CHEBI:78516"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097075"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamyl-tRNA(Gln) + ATP = 5-phospho-L-glutamyl-tRNA(Gln) + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57908"},{"database":"Rhea","id":"RHEA-COMP:9684"},{"database":"Rhea","id":"RHEA-COMP:15032"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:78520"},{"database":"ChEBI","id":"CHEBI:142449"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamyl-tRNA(Gln) + L-glutamine + ATP + H2O = L-glutaminyl-tRNA(Gln) + L-glutamate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17521"},{"database":"Rhea","id":"RHEA-COMP:9681"},{"database":"Rhea","id":"RHEA-COMP:9684"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:78520"},{"database":"ChEBI","id":"CHEBI:78521"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047407"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Binds 2 Mg(2+) ions, a primary Mg(2+) ion involved in positioning of the gamma-carbonyl group of the amino acid in Glu-tRNA(Gln), and a secondary transient Mg(2+) ion that participates in phosphoryl transfer by polarizing the gamma-phosphate group of ATP."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00097528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Component of the heterotrimeric GatCAB glutamyl-tRNA(Gln) amidotransferase complex composed of GatA, GatB and GatC"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"The C-terminal tail domain, an anti-parallel amphiphilic helix bundle, is involved in discriminating and binding specific tRNAs. Probably recognizes the tRNA(Gln)-specific D-loop structure"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"The N-terminal cradle domain recognizes the first base of the acceptor tRNA stem"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005306"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Belongs to the GatB/GatE family. GatB subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00305.1"}],"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":326,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Asn/Gln amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00845"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"Cradle","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Region","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":474,"modifier":"EXACT"}},"description":"Tail","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00121"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00305.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00305.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00305.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000188","properties":[{"key":"ProteinId","value":"EOD00305.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006313956.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000188.1"}]},{"database":"AlphaFoldDB","id":"R1CDD6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_1656","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.1625","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0064","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9804078at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050566","properties":[{"key":"GoTerm","value":"F:asparaginyl-tRNA synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0050567","properties":[{"key":"GoTerm","value":"F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070681","properties":[{"key":"GoTerm","value":"P:glutaminyl-tRNAGln biosynthesis via transamidation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006412","properties":[{"key":"GoTerm","value":"P:translation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.10.410:FF:000001","properties":[{"key":"EntryName","value":"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.150.380:FF:000001","properties":[{"key":"EntryName","value":"Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.410","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.380","properties":[{"key":"EntryName","value":"GatB domain, N-terminal subdomain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00121","properties":[{"key":"EntryName","value":"GatB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017959","properties":[{"key":"EntryName","value":"Asn/Gln-tRNA_amidoTrfase_suB/E"}]},{"database":"InterPro","id":"IPR006075","properties":[{"key":"EntryName","value":"Asn/Gln-tRNA_Trfase_suB/E_cat"}]},{"database":"InterPro","id":"IPR018027","properties":[{"key":"EntryName","value":"Asn/Gln_amidotransferase"}]},{"database":"InterPro","id":"IPR003789","properties":[{"key":"EntryName","value":"Asn/Gln_tRNA_amidoTrase-B-like"}]},{"database":"InterPro","id":"IPR004413","properties":[{"key":"EntryName","value":"GatB"}]},{"database":"InterPro","id":"IPR042114","properties":[{"key":"EntryName","value":"GatB_C_1"}]},{"database":"InterPro","id":"IPR023168","properties":[{"key":"EntryName","value":"GatB_Yqey_C_2"}]},{"database":"InterPro","id":"IPR017958","properties":[{"key":"EntryName","value":"Gln-tRNA_amidoTrfase_suB_CS"}]},{"database":"InterPro","id":"IPR014746","properties":[{"key":"EntryName","value":"Gln_synth/guanido_kin_cat_dom"}]},{"database":"NCBIfam","id":"NF004012","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004014","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00133","properties":[{"key":"EntryName","value":"gatB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11659","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA GLN AMIDOTRANSFERASE SUBUNIT B MITOCHONDRIAL AND PROKARYOTIC PET112-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11659:SF0","properties":[{"key":"EntryName","value":"GLUTAMYL-TRNA(GLN) AMIDOTRANSFERASE SUBUNIT B, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02934","properties":[{"key":"EntryName","value":"GatB_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02637","properties":[{"key":"EntryName","value":"GatB_Yqey"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00845","properties":[{"key":"EntryName","value":"GatB_Yqey"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF89095","properties":[{"key":"EntryName","value":"GatB/YqeY motif"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55931","properties":[{"key":"EntryName","value":"Glutamine synthetase/guanido kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01234","properties":[{"key":"EntryName","value":"GATB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPYKTIIGLEIHSELLTDSKIFCDCSTEFGGDVNTHTCPVCLGLPGALPVLNKKVVEYGIKAGLAFNCEISERTKMDRKNYFYPDLVKGYQISQYDMPLCQNGYVEIETEDGVKKIRLRRIHIEEDTGKSIHSEDGGSLLDYNRSGVPLIEIVTEPDMNSPEEAKLFLEKLKSILQYIEVSDCKMEEGSLRCDVNINIVDEETGKRSTITELKNLNSFKAAVKAMEYEEERHKKLLEEGKDTRRETRRWDELKNETIVMRVKEEVSDYRYFPEPDIVEMEIDREWVEEIRKELPELPHVKKERFIEQYDLPEYDAEVLTSSKALADFFEETIRYFDDSKQVSNWIMGDISRRLNMENIGIEDVSFTAKDLADLLKLIDEGKISNKIGKKVLRAMFEEGKDPNTIVKEKGLIQISDEGELKKIVDKVLSENQQSVEDYKNGKDRALGFLVGQVMKATRGKANPQLANKLIRESIQ","length":474,"molWeight":54495,"crc64":"0F2FF21D9D340C77","md5":"9D967F1F5547A41E0783E689AE56FF89"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":8},"uniParcId":"UPI00032F2912"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CFA9","uniProtkbId":"R1CFA9_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":74,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00970.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Riboflavin biosynthesis protein RibBA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"4.1.99.12"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase II"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"ribBA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00970.1"}],"value":"L21TH_0974"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043932"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049295"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004853"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00970.1"}],"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":207,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"DHBP synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":403,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"Proton acceptor; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":317,"modifier":"EXACT"},"end":{"value":317,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022619"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00970.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00970.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000096","properties":[{"key":"ProteinId","value":"EOD00970.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006310771.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000096.1"}]},{"database":"AlphaFoldDB","id":"R1CFA9","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_0974","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.957","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0108","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"eggNOG","id":"COG0807","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9793111at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00275","properties":[{"key":"RectionId","value":"UER00399"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01283","properties":[{"key":"EntryName","value":"RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"InterPro","id":"IPR016299","properties":[{"key":"EntryName","value":"Riboflavin_synth_RibBA"}]},{"database":"NCBIfam","id":"NF006803","properties":[{"key":"EntryName","value":"PRK09311.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFKFNTIEEAIEDIKKGKVIVVVDDEDRENEGDLVMAAEKVTPEAINFMAKYGRGLICVPMVKDRLEELDIYPMVSNNTDPKETAFTVSVDAKNTTTGISAYERAETILKLVDKNSTKEDFNRPGHIFPLEARDGGVLKRAGHTEASVDLTKLAGLYPAGVICEIMNEDGTMARVPQLMEFTKKHNLKIITIADLIAYRRKNESLIERVSEASMPIKYGEFKIIGYVNKLNGEHHVALVKGEINNEMPVLVRVHSECLTGDAFGSLRCDCGEQLQSALSAIEEEGKGILLYMRQEGRGIGLINKIKAYALQDKGMDTVEANLALGFPEDMRDYGIGAQILADLGAKKIRLMTNNPKKLSGLSGYGIKVVERVPLQIQYNKTNEFYLKTKQHKMGHLLNFEEVE","length":403,"molWeight":44933,"crc64":"9DC850EAFA9B2E12","md5":"26DCDE97531EBD5FD0D1BC43BC094C5F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Active site":2,"Binding site":16,"Site":2},"uniParcId":"UPI00032FD148"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CLH4","uniProtkbId":"R1CLH4_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-06-26","entryVersion":73,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99530.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Multifunctional fusion protein"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Holo-[acyl-carrier-protein] synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Holo-ACP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"2.7.8.7"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"4'-phosphopantetheinyl transferase AcpS"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"acpS"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99530.1"}],"value":"L21TH_2442"}]}],"comments":[{"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_00101"}],"value":"Transfers the 4'-phosphopantetheine moiety from coenzyme A to a Ser of acyl-carrier-protein"}],"commentType":"FUNCTION"},{"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":"HAMAP-Rule","id":"MF_01965"}]}},{"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":"HAMAP-Rule","id":"MF_01965"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"apo-[ACP] + CoA = holo-[ACP] + adenosine 3',5'-bisphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12068"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9690"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29999"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:58343"},{"database":"ChEBI","id":"CHEBI:64479"}],"ecNumber":"2.7.8.7","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"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_00101"}],"value":"Belongs to the P-Pant transferase superfamily. AcpS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99530.1"}],"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":148,"modifier":"EXACT"},"end":{"value":431,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"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":254,"modifier":"EXACT"},"end":{"value":254,"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":305,"modifier":"EXACT"},"end":{"value":305,"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":342,"modifier":"EXACT"},"end":{"value":346,"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":371,"modifier":"EXACT"},"end":{"value":371,"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":372,"modifier":"EXACT"},"end":{"value":372,"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":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"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":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00101"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"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:0000313","source":"Proteomes","id":"UP000013378"}],"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_00101"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99530.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99530.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000268","properties":[{"key":"ProteinId","value":"EOC99530.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006316959.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000268.1"}]},{"database":"AlphaFoldDB","id":"R1CLH4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2442","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2396","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0063","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"eggNOG","id":"COG0736","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9806925at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008897","properties":[{"key":"GoTerm","value":"F:holo-[acyl-carrier-protein] synthase 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:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006633","properties":[{"key":"GoTerm","value":"P:fatty acid biosynthetic process"},{"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":"3.90.470.20","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00101","properties":[{"key":"EntryName","value":"AcpS"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008278","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom"}]},{"database":"InterPro","id":"IPR037143","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom_sf"}]},{"database":"InterPro","id":"IPR002582","properties":[{"key":"EntryName","value":"ACPS"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR004568","properties":[{"key":"EntryName","value":"Ppantetheine-prot_Trfase_dom"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"NCBIfam","id":"TIGR00516","properties":[{"key":"EntryName","value":"acpS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00556","properties":[{"key":"EntryName","value":"pantethn_trn"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01648","properties":[{"key":"EntryName","value":"ACPS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56214","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01049","properties":[{"key":"EntryName","value":"YJEF_C_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01050","properties":[{"key":"EntryName","value":"YJEF_C_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIIGNGIDIIETDRIKKILKRQKSFINRIYSDKEKKYIKSRKENIHTIAGMFAAKEAVSKSLGSGIRDFKWKDIEILHDSFGKPYVELNGNAKKLAEEKGIENIHISITHIEKYALAFAICDNNKVINKHNQIKQEDKNKFFNLKPIDDRLVKSIIPERKNQSHKGTYGRVSVLAGCKGMLGASYLTSMASLRSGSGLVYTLVPNSLYEIMEIKATETIIKPVEDLNKGYFNSASFDEIQDVASIADVIALGPGLGVDEERIKLVNKLLASFNKPIVLDADGINCVSKMTQVLEKRKYPTIITPHPGELSRLLNISIQEIQDNRVKYARLTSKKYGVITVLKGANTIVASKEGEIFINMTGNPGMATAGSGDVLTGVISSFIGQGIEPLKAAIAGVYIHGLAGDLASYEKGQYGIIATDILEKIPYSIKKLVGK","length":434,"molWeight":47774,"crc64":"064497B1DF06EAC4","md5":"7BBD09EAD6288F832BD2E58FB27D3862"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":8},"uniParcId":"UPI000330C805"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CNR3","uniProtkbId":"R1CNR3_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":65,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00341.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"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":"EOD00341.1"}],"value":"L21TH_1640"}]}],"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":"ARBA","id":"ARBA00005166"},{"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":"ARBA","id":"ARBA00005208"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00341.1"}],"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":4,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"Nucleotidyl transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00483"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":463,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":10,"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":21,"modifier":"EXACT"},"end":{"value":21,"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":81,"modifier":"EXACT"},"end":{"value":82,"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":103,"modifier":"EXACT"},"end":{"value":105,"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":105,"modifier":"EXACT"},"end":{"value":105,"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":142,"modifier":"EXACT"},"end":{"value":142,"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":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":230,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":335,"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":353,"modifier":"EXACT"},"end":{"value":353,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":389,"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":407,"modifier":"EXACT"},"end":{"value":407,"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":425,"modifier":"EXACT"},"end":{"value":425,"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":442,"modifier":"EXACT"},"end":{"value":442,"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":"UP000013378"}],"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-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00341.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00341.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000186","properties":[{"key":"ProteinId","value":"EOD00341.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006313883.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000186.1"}]},{"database":"AlphaFoldDB","id":"R1CNR3","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_1640","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.1609","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG1207","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"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":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0019134","properties":[{"key":"GoTerm","value":"F:glucosamine-1-phosphate N-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003977","properties":[{"key":"GoTerm","value":"F:UDP-N-acetylglucosamine diphosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000902","properties":[{"key":"GoTerm","value":"P:cell morphogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009245","properties":[{"key":"GoTerm","value":"P:lipid A biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006048","properties":[{"key":"GoTerm","value":"P:UDP-N-acetylglucosamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR005835","properties":[{"key":"EntryName","value":"NTP_transferase_dom"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010934","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00483","properties":[{"key":"EntryName","value":"NTP_transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLTSIILAAGEGTRMKSKLPKVLHKICNKPMVNYVIEAAHKANLNKNILIVGHGGDKVREAVKNENVEIVKQPIGEEFPYGTGYAVMQAKDHIKENSYVIILYGDTPLITSETLTKLIEFHKSGGYNATVLTAEFEDPTGYGRIIRDENGNVTEIVEHKDATDKQKEIREINSGIYCFDGKYLKSVLDKLDNNNAQGEYYITDAIKILNEEGCKIGGYKIEDKVEIAGVNSKVQLAEAEAVMRRRINEKLLMNGAIMIDPSSTYIDSDVKIGKDTVIYPGVIIEGNTEIGEECVIGHNSRIVDSKIGDRVNIQSSTIIESEVDNDTNIGPYAYLRPNSKIGKSVKIGDFVEVKNSTIGDKSKASHLAYIGDAEVGKNVNIGCGVVFVNYDGKVKHKTIVEDNAFVGSNSNLVAPVIVRENGYVAAGSTITEEVKSGALSIARARQFNKEGWVEKKNLQREEKK","length":463,"molWeight":50889,"crc64":"B57F057532848989","md5":"C31B332D562CA82E9EBBA9E4E31C7AEF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":3,"Active site":1,"Binding site":18},"uniParcId":"UPI00032D890D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CRL1","uniProtkbId":"R1CRL1_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-06-26","entryVersion":44,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01311.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"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":"EOD01311.1"}],"value":"L21TH_0665"}]}],"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":"EOD01311.1"}],"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":178,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":392,"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":188,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Active site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"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":287,"modifier":"EXACT"},"end":{"value":287,"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":303,"modifier":"EXACT"},"end":{"value":306,"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":335,"modifier":"EXACT"},"end":{"value":335,"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"}}],"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":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01311.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01311.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000066","properties":[{"key":"ProteinId","value":"EOD01311.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006308909.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000066.1"}]},{"database":"AlphaFoldDB","id":"R1CRL1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_0665","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.654","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0452","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9802554at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00241","properties":[{"key":"RectionId","value":"UER00353"}]},{"database":"Proteomes","id":"UP000013378","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":"MLKGKNIVVGVTGGIAAYKAADIVSKLKKLQANVDVIMTESATKFISPLTFQSLSQNFVTVDMFKEPKKWEIEHISLAQKADVFLIAPATANVIGKVANGIADDMLSTTIMATKSKVVFAPAMNTNMYTNPIFQQNMNKLKELGYEFIRPAKGRLACGDYGEGKMADTVDIVSYVTDMLTNKELKGKKVIVTAGPTIEPIDPVRYLTNHSSGKMGYAIAEEAEKMGAEVILISGPTHLKAPDGVEVVRINTTQQMFNEIEKRFNGCDVLIKAAAPLDYKPEEVYNNKIKKGNGKLELSFTRNPDILKYFGNNKKDQIVVGFAAETDNVLENGRKKMKNKNLDFIVVNDVSNKDAGFKKETNVATIIDKEGTEKSYPKMSKRELAKIILDKILDNFS","length":396,"molWeight":43708,"crc64":"63859DA93E9DE703","md5":"C93B2381CC750A6E1174461E57216BAD"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":6},"uniParcId":"UPI00032FE313"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CT03","uniProtkbId":"R1CT03_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-06-26","entryVersion":65,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01781.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00016943"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Ribokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"RK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012035"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"2.7.1.15"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"rbsK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01781.1"}],"value":"L21TH_0136"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Catalyzes the phosphorylation of ribose at O-5 in a reaction requiring ATP and magnesium. The resulting D-ribose-5-phosphate can then be used either for sythesis of nucleotides, histidine, and tryptophan, or as a component of the pentose phosphate pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribose + ATP = D-ribose 5-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13697"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:47013"},{"database":"ChEBI","id":"CHEBI:78346"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.15","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-tagatofuranose 6-phosphate + ATP = D-tagatofuranose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12420"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58694"},{"database":"ChEBI","id":"CHEBI:58695"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.144","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000535"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Requires a divalent cation, most likely magnesium in vivo, as an electrophilic catalyst to aid phosphoryl group transfer. It is the chelate of the metal and the nucleotide that is the actual substrate."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Activated by a monovalent cation that binds near, but not in, the active site. The most likely occupant of the site in vivo is potassium. Ion binding induces a conformational change that may alter substrate affinity"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Carbohydrate metabolism; D-ribose degradation; D-ribose 5-phosphate from beta-D-ribopyranose: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000535"}],"value":"Carbohydrate metabolism; D-tagatose 6-phosphate degradation; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-tagatose 6-phosphate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000535"}],"value":"Belongs to the carbohydrate kinase PfkB family. LacC subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Belongs to the carbohydrate kinase PfkB family. Ribokinase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005380"}],"value":"Belongs to the carbohydrate kinase pfkB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01781.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Active site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":39,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":225,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000535"}],"id":"KW-0423","category":"Biological process","name":"Lactose metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01987"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"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_01987"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01781.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD01781.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000020","properties":[{"key":"ProteinId","value":"EOD01781.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006306232.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000020.1"}]},{"database":"AlphaFoldDB","id":"R1CT03","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_0136","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.134","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0524","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9775849at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00704","properties":[{"key":"RectionId","value":"UER00715"}]},{"database":"UniPathway","id":"UPA00916","properties":[{"key":"RectionId","value":"UER00889"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004747","properties":[{"key":"GoTerm","value":"F:ribokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009024","properties":[{"key":"GoTerm","value":"F:tagatose-6-phosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046835","properties":[{"key":"GoTerm","value":"P:carbohydrate phosphorylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019303","properties":[{"key":"GoTerm","value":"P:D-ribose catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:2001059","properties":[{"key":"GoTerm","value":"P:D-tagatose 6-phosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"CDD","id":"cd01174","properties":[{"key":"EntryName","value":"ribokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01987","properties":[{"key":"EntryName","value":"Ribokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002173","properties":[{"key":"EntryName","value":"Carboh/pur_kinase_PfkB_CS"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR002139","properties":[{"key":"EntryName","value":"Ribo/fructo_kinase"}]},{"database":"InterPro","id":"IPR011877","properties":[{"key":"EntryName","value":"Ribokinase"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR017583","properties":[{"key":"EntryName","value":"Tagatose/fructose_Pkinase"}]},{"database":"NCBIfam","id":"TIGR02152","properties":[{"key":"EntryName","value":"D_ribokin_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10584:SF166","properties":[{"key":"EntryName","value":"RIBOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10584","properties":[{"key":"EntryName","value":"SUGAR KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000535","properties":[{"key":"EntryName","value":"1PFK/6PFK/LacC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00990","properties":[{"key":"EntryName","value":"RIBOKINASE"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00584","properties":[{"key":"EntryName","value":"PFKB_KINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSDITVIGSLNMDLVATVKNMPKVGETLIGKELKQIPGGKGANQAVAAARLGAKVSMIGKVGDDGFGKNLMDSMNSDGIDTKYIKREENTSTGVALITVNDEGDNSIVVIPGANFKVTKEDIDKATEAIEGSKIVLLQLEIPIDVVKYSLKKAKTLGKYTILNPAPAQNLDDEIIENVDLLIPNETELEILSGIEIKQEEDILNASRKLIKKGVKELIVTMGGKGCLYINKDIVKKYKAHKVQVVDTTAAGDSFTAAVSVQLSKKESIDKAIEFAMKVGALTVTKEGAQSSLPYLKDVLDFKGE","length":304,"molWeight":32623,"crc64":"299F91DC60CD0843","md5":"1796D0CCC673D45EDA825BED623635F2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":13},"uniParcId":"UPI00032F71C1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1CW42","uniProtkbId":"R1CW42_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":65,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00854.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"pfkA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00854.1"}],"value":"L21TH_1092"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"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":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Allosterically activated by ADP and other diphosphonucleosides, and allosterically inhibited by phosphoenolpyruvate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"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_00339"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Prokaryotic clade 'B1' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00854.1"}],"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":4,"modifier":"EXACT"},"end":{"value":275,"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_00339"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"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_00339"}],"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_00339"}],"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_00339"}],"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_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; 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_00339"}],"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_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":185,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":213,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"ADP","id":"ChEBI:CHEBI:456216","note":"allosteric activator; 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_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00339"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"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_00339"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00854.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00854.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000110","properties":[{"key":"ProteinId","value":"EOD00854.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006311194.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000110.1"}]},{"database":"AlphaFoldDB","id":"R1CW42","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_1092","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.1069","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0205","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9802503at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00109","properties":[{"key":"RectionId","value":"UER00182"}]},{"database":"Proteomes","id":"UP000013378","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:UniProtKB-UniRule"}]},{"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:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.50.450:FF:000001","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_00339","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_B1"},{"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":"IPR012828","properties":[{"key":"EntryName","value":"PFKA_ATP_prok"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02482","properties":[{"key":"EntryName","value":"PFKA_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"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":"MKTIGVLTSGGDAPGMNAAIRAVVRTGIYNEIKIMGIKQGYNGLINGDIEEMELSSVADIIHRGGTVLRSARCEEFKTEEGRNKALTVLKVFGIEGLVVIGGDGSFMGAKKLSEAGIPTIGIPGTIDNDLGYTDYTIGFDTAVNTVLDAISKIRDTSTSHGRANIIEVMGRDCGDIALYAGLAGGAESVIVPEEDFDVDEVCKRLIQGKNRGKLHSIIMLAEGVGNAYELGKTIQEKTGIETRCTVLGHIQRGGSPSAFDRLLASRMGARAVELLLEGKSGRVIGAKKNELFDMDIDEALDVKKEFDKKAYELTKILSI","length":319,"molWeight":34098,"crc64":"84D263E0954B5385","md5":"2B3D1CB951F2A82924ADAFF91675F310"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":15},"uniParcId":"UPI00032E5E59"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AQM7","uniProtkbId":"R1AQM7_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":62,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"tRNA modification GTPase MnmE"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"3.6.-.-"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"mnmE"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"trmE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99427.1"}],"value":"L21TH_2545"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Exhibits a very high intrinsic GTPase hydrolysis rate. Involved in the addition of a carboxymethylaminomethyl (cmnm) group at the wobble position (U34) of certain tRNAs, forming tRNA-cmnm(5)s(2)U34"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Homodimer. Heterotetramer of two MnmE and two MnmG subunits"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011043"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003313"}],"value":"Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin-like GTPase superfamily. TrmE GTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99427.1"}],"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":222,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"TrmE-type G","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51709"}]},{"type":"Binding site","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":236,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":259,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":257,"modifier":"EXACT"},"end":{"value":257,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":276,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01046"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57457"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"ligand":{"name":"(6S)-5-formyl-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57457"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00379"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99427.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000274","properties":[{"key":"ProteinId","value":"EOC99427.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006317187.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000274.1"}]},{"database":"AlphaFoldDB","id":"R1AQM7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2545","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2500","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0486","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9805918at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003924","properties":[{"key":"GoTerm","value":"F:GTPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"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:0030955","properties":[{"key":"GoTerm","value":"F:potassium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0002098","properties":[{"key":"GoTerm","value":"P:tRNA wobble uridine modification"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04164","properties":[{"key":"EntryName","value":"trmE"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd14858","properties":[{"key":"EntryName","value":"TrmE_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1360.120:FF:000003","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000494","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1360.120","properties":[{"key":"EntryName","value":"Probable tRNA modification gtpase trme, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.430","properties":[{"key":"EntryName","value":"tRNA modification GTPase MnmE domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00379","properties":[{"key":"EntryName","value":"GTPase_MnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR031168","properties":[{"key":"EntryName","value":"G_TrmE"}]},{"database":"InterPro","id":"IPR006073","properties":[{"key":"EntryName","value":"GTP-bd"}]},{"database":"InterPro","id":"IPR018948","properties":[{"key":"EntryName","value":"GTP-bd_TrmE_N"}]},{"database":"InterPro","id":"IPR004520","properties":[{"key":"EntryName","value":"GTPase_MnmE"}]},{"database":"InterPro","id":"IPR027368","properties":[{"key":"EntryName","value":"MnmE_dom2"}]},{"database":"InterPro","id":"IPR025867","properties":[{"key":"EntryName","value":"MnmE_helical"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR005225","properties":[{"key":"EntryName","value":"Small_GTP-bd"}]},{"database":"InterPro","id":"IPR027266","properties":[{"key":"EntryName","value":"TrmE/GcvT-like"}]},{"database":"NCBIfam","id":"NF003661","properties":[{"key":"EntryName","value":"mnmE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00450","properties":[{"key":"EntryName","value":"mnmE_trmE_thdF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00231","properties":[{"key":"EntryName","value":"small_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42714","properties":[{"key":"EntryName","value":"TRNA MODIFICATION GTPASE GTPBP3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42714:SF2","properties":[{"key":"EntryName","value":"TRNA MODIFICATION GTPASE GTPBP3, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01926","properties":[{"key":"EntryName","value":"MMR_HSR1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12631","properties":[{"key":"EntryName","value":"MnmE_helical"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10396","properties":[{"key":"EntryName","value":"TrmE_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00449","properties":[{"key":"EntryName","value":"RASTRNSFRMNG"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF116878","properties":[{"key":"EntryName","value":"TrmE connector domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51709","properties":[{"key":"EntryName","value":"G_TRME"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNNDTIAAIATAPGEAGIGIVRISGNNAIDIADKLFKGKRVEKLSEAEQRKLTYGYIIDPKTGDKVDEVLAVYMKAPYTYTTEDVVEINCHGGSIPVRKVLELVLENGARMAERGEFTKRAFLNGRIDLSQAEAVMDLISAKTDTSYDVSLNQLEGKLSKEVREIRNILLNMLAHIEVSIDFPEEDIEQVTYEEIKKQGHEVYDRIKKLLDTVNTGKILREGLKTVILGKPNVGKSSLLNSLLRENRAIVTDVPGTTRDIIEEYINIKGIPLKLVDTAGIRQTEDIVEKIGVERAKELLNTADLVIAVFDASRELTEEDFHVMETIKDKKAIVLLNKTDLPVKTDENVIREKLGDKEIIKSSMVKEKGIDQLEETLRDMFFEGEVKISDNIIVTNVRHRDSLLKARNNIHEALEAIELGMTLDCIEVDVKDCWSNLGEITGDTVSEDIIDKIFKDFCIGK","length":460,"molWeight":51498,"crc64":"E31D57B79EE4DB93","md5":"E8616186EC0A4255031B1F0C6AF26734"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":17},"uniParcId":"UPI00032ED9A8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AQX3","uniProtkbId":"R1AQX3_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":69,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99522.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"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":"EOC99522.1"}],"value":"L21TH_2434"}]}],"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":"EOC99522.1"}],"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":208,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14681"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"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":104,"modifier":"EXACT"},"end":{"value":104,"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":131,"modifier":"EXACT"},"end":{"value":139,"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":194,"modifier":"EXACT"},"end":{"value":194,"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":199,"modifier":"EXACT"},"end":{"value":201,"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":200,"modifier":"EXACT"},"end":{"value":200,"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":"UP000013378"}],"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-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99522.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99522.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000268","properties":[{"key":"ProteinId","value":"EOC99522.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006316947.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000268.1"}]},{"database":"AlphaFoldDB","id":"R1AQX3","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2434","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2388","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0035","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9781675at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00574","properties":[{"key":"RectionId","value":"UER00636"}]},{"database":"Proteomes","id":"UP000013378","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":"MSKVTLIDHPLIQHKLTLLRDKKTGAKDFRELVNEIAMLMGYEVTRDFQLENVEIETPICKATGKMLTGKKVAIVPILRAGLGMVDGMLKLIPAAKVGHIGLYRNEETLKPVEYYCKLPQDIAEREVIITEPMLATGGSSSDAITLLKKRGAKNIRLMCLVCSKQGLEVVTNEHPDVDIYTAAIDEKLNEHGYIVPGLGDAGDRLFGTK","length":209,"molWeight":23058,"crc64":"75C9FD405D317E89","md5":"D2AB22165859A11378ACEB8B76C23784"},"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":"UPI00032E7119"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AQY1","uniProtkbId":"R1AQY1_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2013-06-26","entryVersion":59,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99532.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Alanine racemase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"5.1.1.1"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99532.1"}],"value":"L21TH_2444"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Catalyzes the interconversion of L-alanine and D-alanine. May also act on other amino acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-alanine = D-alanine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20249"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57972"}],"ecNumber":"5.1.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000316"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine from L-alanine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"value":"Belongs to the alanine racemase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99532.1"}],"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":249,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"Alanine racemase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01005"}]},{"type":"Active site","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Proton acceptor; specific for D-alanine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}]},{"type":"Active site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Proton acceptor; specific for L-alanine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}]},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-52"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-52"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":41,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600821-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01201"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99532.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99532.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000268","properties":[{"key":"ProteinId","value":"EOC99532.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006316962.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000268.1"}]},{"database":"AlphaFoldDB","id":"R1AQY1","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2444","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2398","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0787","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9813814at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00042","properties":[{"key":"RectionId","value":"UER00497"}]},{"database":"Proteomes","id":"UP000013378","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:0008784","properties":[{"key":"GoTerm","value":"F:alanine racemase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030632","properties":[{"key":"GoTerm","value":"P:D-alanine 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:TreeGrafter"}]},{"database":"CDD","id":"cd00430","properties":[{"key":"EntryName","value":"PLPDE_III_AR"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.37.10:FF:000006","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.10:FF:000002","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.10","properties":[{"key":"EntryName","value":"Alanine racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.37.10","properties":[{"key":"EntryName","value":"Lyase, Ornithine Decarboxylase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01201","properties":[{"key":"EntryName","value":"Ala_racemase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000821","properties":[{"key":"EntryName","value":"Ala_racemase"}]},{"database":"InterPro","id":"IPR009006","properties":[{"key":"EntryName","value":"Ala_racemase/Decarboxylase_C"}]},{"database":"InterPro","id":"IPR011079","properties":[{"key":"EntryName","value":"Ala_racemase_C"}]},{"database":"InterPro","id":"IPR001608","properties":[{"key":"EntryName","value":"Ala_racemase_N"}]},{"database":"InterPro","id":"IPR020622","properties":[{"key":"EntryName","value":"Ala_racemase_pyridoxalP-BS"}]},{"database":"InterPro","id":"IPR029066","properties":[{"key":"EntryName","value":"PLP-binding_barrel"}]},{"database":"NCBIfam","id":"TIGR00492","properties":[{"key":"EntryName","value":"alr"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30511","properties":[{"key":"EntryName","value":"ALANINE RACEMASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30511:SF0","properties":[{"key":"EntryName","value":"ALANINE RACEMASE, CATABOLIC-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00842","properties":[{"key":"EntryName","value":"Ala_racemase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01168","properties":[{"key":"EntryName","value":"Ala_racemase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00992","properties":[{"key":"EntryName","value":"ALARACEMASE"}]},{"database":"SMART","id":"SM01005","properties":[{"key":"EntryName","value":"Ala_racemase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50621","properties":[{"key":"EntryName","value":"Alanine racemase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51419","properties":[{"key":"EntryName","value":"PLP-binding barrel"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00395","properties":[{"key":"EntryName","value":"ALANINE_RACEMASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKSLQNIRPVWAEINLDNLAHNIREVRRVTKEDTLITAVVKADGYGHGAAIAAKTFLNNGADRLAVATLSEALELRKEGINAPILILGYTPDSQFEKVIENDITQTIYTYEQGINISKAAHKVGKVGKIHVKIDTGMSRLGFVPNKSSVEDIVKIAKLSGIKIEGIFSHFAKADERDKSATNEQYKKFKWIIQELESKNINIPIKHISNSAAIIDLPQYNLDMVRAGIMLYGLYPSNEVNKKAVRLKPAMTLKAKISHIKEVEKGTGISYGHVYITEKESKIGTLPIGYADGYTRILTNKAEVGIKGYKVPVIGRICMDQCMIDVSSIKDIKVGDEVILFGDGYNNSPHIDEVAEKLETINYEIVCMVSRRVPRVYIKQGDIVHIKDYLEE","length":391,"molWeight":43597,"crc64":"1393E6285E5C7663","md5":"36ED224453E609B9F2C1C7529EAFD75B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":2,"Modified residue":1},"uniParcId":"UPI00032EDB21"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ARE2","uniProtkbId":"R1ARE2_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":57,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99727.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"Protein-glutamate methylesterase/protein-glutamine glutaminase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"3.1.1.61"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"3.5.1.44"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"cheB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99727.1"}],"value":"L21TH_2257"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"Involved in chemotaxis. Part of a chemotaxis signal transduction system that modulates chemotaxis in response to various stimuli. Catalyzes the demethylation of specific methylglutamate residues introduced into the chemoreceptors (methyl-accepting chemotaxis proteins or MCP) by CheR. Also mediates the irreversible deamidation of specific glutamine residues to glutamic acid"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutaminyl-[protein] + H2O = L-glutamyl-[protein] + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16441"},{"database":"Rhea","id":"RHEA-COMP:10207"},{"database":"Rhea","id":"RHEA-COMP:10208"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29973"},{"database":"ChEBI","id":"CHEBI:30011"}],"ecNumber":"3.5.1.44","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[protein]-L-glutamate 5-O-methyl ester + H2O = L-glutamyl-[protein] + methanol + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23236"},{"database":"Rhea","id":"RHEA-COMP:10208"},{"database":"Rhea","id":"RHEA-COMP:10311"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17790"},{"database":"ChEBI","id":"CHEBI:29973"},{"database":"ChEBI","id":"CHEBI:82795"}],"ecNumber":"3.1.1.61","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048267"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"Contains a C-terminal catalytic domain, and an N-terminal region which modulates catalytic activity"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"Phosphorylated by CheA. Phosphorylation of the N-terminal regulatory domain activates the methylesterase activity"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"value":"Belongs to the CheB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99727.1"}],"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":4,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"Response regulatory","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50110"}]},{"type":"Domain","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"CheB-type methylesterase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50122"}]},{"type":"Active site","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00050"}]},{"type":"Active site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00050"}]},{"type":"Active site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00050"}]},{"type":"Modified residue","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"4-aspartylphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00169"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00050"}],"id":"KW-0145","category":"Biological process","name":"Chemotaxis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00099"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00169"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99727.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99727.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000250","properties":[{"key":"ProteinId","value":"EOC99727.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006316266.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000250.1"}]},{"database":"AlphaFoldDB","id":"R1ARE2","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2257","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2208","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG2201","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9793421at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0000156","properties":[{"key":"GoTerm","value":"F:phosphorelay response regulator activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008984","properties":[{"key":"GoTerm","value":"F:protein-glutamate methylesterase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050568","properties":[{"key":"GoTerm","value":"F:protein-glutamine glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006935","properties":[{"key":"GoTerm","value":"P:chemotaxis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd16432","properties":[{"key":"EntryName","value":"CheB_Rec"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd17541","properties":[{"key":"EntryName","value":"REC_CheB-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2300","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.180","properties":[{"key":"EntryName","value":"Methylesterase CheB, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00099","properties":[{"key":"EntryName","value":"CheB_chemtxs"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008248","properties":[{"key":"EntryName","value":"CheB-like"}]},{"database":"InterPro","id":"IPR035909","properties":[{"key":"EntryName","value":"CheB_C"}]},{"database":"InterPro","id":"IPR011006","properties":[{"key":"EntryName","value":"CheY-like_sf"}]},{"database":"InterPro","id":"IPR000673","properties":[{"key":"EntryName","value":"Sig_transdc_resp-reg_Me-estase"}]},{"database":"InterPro","id":"IPR001789","properties":[{"key":"EntryName","value":"Sig_transdc_resp-reg_receiver"}]},{"database":"NCBIfam","id":"NF001965","properties":[{"key":"EntryName","value":"cheB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009206","properties":[{"key":"EntryName","value":"cheB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42872","properties":[{"key":"EntryName","value":"PROTEIN-GLUTAMATE METHYLESTERASE/PROTEIN-GLUTAMINE GLUTAMINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42872:SF3","properties":[{"key":"EntryName","value":"PROTEIN-GLUTAMATE METHYLESTERASE_PROTEIN-GLUTAMINE GLUTAMINASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01339","properties":[{"key":"EntryName","value":"CheB_methylest"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00072","properties":[{"key":"EntryName","value":"Response_reg"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000876","properties":[{"key":"EntryName","value":"RR_chemtxs_CheB"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00448","properties":[{"key":"EntryName","value":"REC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52172","properties":[{"key":"EntryName","value":"CheY-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52738","properties":[{"key":"EntryName","value":"Methylesterase CheB, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50122","properties":[{"key":"EntryName","value":"CHEB"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50110","properties":[{"key":"EntryName","value":"RESPONSE_REGULATORY"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSIKVFVVDDSAFMRKIISDILEQDKDIEILDTARNGKDALEKLKALKPDIITLDIEMPIMNGIECLESIMKEHKVPVVMLSSLTTSGAEATIKALELGAVDFITKPDSVFDMSNNEKKQELTKKIKTAAKVKRPKTVFNNIGESYSMNTVTKKNYSYSTLVAIGTSTGGPKALQAIIPYIHKDINGSILVVQHMPPGFTKSLAKRLNSLSKINVKEAEDGEKVLKGYCYIAPGGFHMEVKEKRSGDLYIELNKNEPVTGHRPSVDVMMDSVSKISTMNKMGIILTGMGADGATGIKKIKENRGYTIAQDENSCVVFGMPKSAIKNNAIDNILPLNKIATEIVNKVGC","length":348,"molWeight":38086,"crc64":"E65EF3C3C380B198","md5":"EA3180A3FAA3E2E40D557EA889C761CF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":3,"Modified residue":1},"uniParcId":"UPI00032EFB92"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ARG0","uniProtkbId":"R1ARG0_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":62,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99742.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"Peptidase T"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"3.4.11.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"Aminotripeptidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"Tripeptidase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"Tripeptide aminopeptidase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"pepT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99742.1"}],"value":"L21TH_2220"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"Cleaves the N-terminal amino acid of tripeptides"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of the N-terminal residue from a tripeptide.","ecNumber":"3.4.11.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000870"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"value":"Belongs to the peptidase M20B family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99742.1"}],"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":208,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"Peptidase M20 dimerisation","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07687"}]},{"type":"Active site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-1"}]},{"type":"Active site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-1"}]},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"1"}},{"type":"Binding site","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":381,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037215-2"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022438"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"id":"KW-0031","category":"Molecular function","name":"Aminopeptidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023049"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"id":"KW-0482","category":"Molecular function","name":"Metalloprotease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00550"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99742.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99742.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000245","properties":[{"key":"ProteinId","value":"EOC99742.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"R1ARG0","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2220","properties":[{"key":"Description","value":"-"}]},{"database":"MEROPS","id":"M20.003","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2174","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG2195","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"Proteomes","id":"UP000013378","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:0045148","properties":[{"key":"GoTerm","value":"F:tripeptide aminopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043171","properties":[{"key":"GoTerm","value":"P:peptide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd03892","properties":[{"key":"EntryName","value":"M20_peptT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.360:FF:000002","properties":[{"key":"EntryName","value":"Peptidase T"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.360","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.10","properties":[{"key":"EntryName","value":"Zn peptidases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00550","properties":[{"key":"EntryName","value":"Aminopeptidase_M20"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001261","properties":[{"key":"EntryName","value":"ArgE/DapE_CS"}]},{"database":"InterPro","id":"IPR036264","properties":[{"key":"EntryName","value":"Bact_exopeptidase_dim_dom"}]},{"database":"InterPro","id":"IPR002933","properties":[{"key":"EntryName","value":"Peptidase_M20"}]},{"database":"InterPro","id":"IPR011650","properties":[{"key":"EntryName","value":"Peptidase_M20_dimer"}]},{"database":"InterPro","id":"IPR010161","properties":[{"key":"EntryName","value":"Peptidase_M20B"}]},{"database":"NCBIfam","id":"NF003976","properties":[{"key":"EntryName","value":"pepT"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01882","properties":[{"key":"EntryName","value":"peptidase-T"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009920","properties":[{"key":"EntryName","value":"PRK13381.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42994","properties":[{"key":"EntryName","value":"PEPTIDASE T"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42994:SF1","properties":[{"key":"EntryName","value":"PEPTIDASE T"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07687","properties":[{"key":"EntryName","value":"M20_dimer"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01546","properties":[{"key":"EntryName","value":"Peptidase_M20"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF037215","properties":[{"key":"EntryName","value":"Peptidase_M20B"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55031","properties":[{"key":"EntryName","value":"Bacterial exopeptidase dimerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53187","properties":[{"key":"EntryName","value":"Zn-dependent exopeptidases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00758","properties":[{"key":"EntryName","value":"ARGE_DAPE_CPG2_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00759","properties":[{"key":"EntryName","value":"ARGE_DAPE_CPG2_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MMSKVVERFISYAKIDTKSDPNSNTCPSTEKQFNLANVLVKELKEIGLEDVSVDDNGYVMATLPANTNKDIPTIGFIAHMDTSPDMSGKNVNPKFVEDYDGEDIILNESDNVILSPKDFPELKNYIGTTLITTDGTTLLGADDKAGIAEIVTAMEYLINHPEIEHGTIKVCFTPDEEIGRGADLFDVEKFNADFAYTVDGGPIGELEYENFNAASAKITVNGRNVHPGSAKDKMVNSMELAMELNSMLPENQKPQYTEKYEGFFHLININGSVEQTTVQYIIRDHNKEKFETKKELMKNTVDFLNKKYGDNTVVLEMKDQYYNMKEKIEPVMHIVETAKKAMEEVGVTPDVKPIRGGTDGARLSYMGLPCPNLFTGGHNFHGKYEYIPTFAMEKAVEVILKIVELYAK","length":408,"molWeight":45638,"crc64":"7EA1802860FDCD88","md5":"CA88011DBC28103681E93A137B6CBBC7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":6},"uniParcId":"UPI00032E5200"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ARG6","uniProtkbId":"R1ARG6_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2025-06-18","lastSequenceUpdateDate":"2013-06-26","entryVersion":50,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99747.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Aspartate carbamoyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"2.1.3.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Aspartate transcarbamylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"ATCase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"pyrB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99747.1"}],"value":"L21TH_2225"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Catalyzes the condensation of carbamoyl phosphate and aspartate to form carbamoyl aspartate and inorganic phosphate, the committed step in the de novo pyrimidine nucleotide biosynthesis pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20013"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:32814"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048859"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004852"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Heterododecamer (2C3:3R2) of six catalytic PyrB chains organized as two trimers (C3), and six regulatory PyrI chains organized as three dimers (R2)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008896"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"value":"Belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99747.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Aspartate/ornithine carbamoyltransferase carbamoyl-P binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02729"}]},{"type":"Domain","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Aspartate/ornithine carbamoyltransferase Asp/Orn-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00185"}]},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":56,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":136,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29991"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"L-aspartate","id":"ChEBI:CHEBI:29991"}},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}},{"type":"Binding site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58228"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"ligand":{"name":"carbamoyl phosphate","id":"ChEBI:CHEBI:58228"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00001"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"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_00001"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99747.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99747.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000245","properties":[{"key":"ProteinId","value":"EOC99747.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006316107.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000245.1"}]},{"database":"AlphaFoldDB","id":"R1ARG6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2225","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2179","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0540","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9774690at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00070","properties":[{"key":"RectionId","value":"UER00116"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004070","properties":[{"key":"GoTerm","value":"F:aspartate carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"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:0006520","properties":[{"key":"GoTerm","value":"P:amino acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000001","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000002","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00001","properties":[{"key":"EntryName","value":"Asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR002082","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753:SF6","properties":[{"key":"EntryName","value":"ASPARTATE CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45753","properties":[{"key":"EntryName","value":"ORNITHINE CARBAMOYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00101","properties":[{"key":"EntryName","value":"ATCASE"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNLKGKHLIDPNDFTLEELDQIFKVAQDMEKHPKKYSEICKSKILATLFYEPSTRTRLSFESAMLRMGGNILGFADATTSSVSKGESVADTVRVVSGYADIIVMRHPKEGAPLLSSEYSSVPVINGGDGGHQHPTQTLTDLLTIKNLKGKIDDNKVALCGDLKYGRTVHSLIKTLARYKNMSFYLVSPPQLKLPTYIKEFVKNEYNAEIFETSYLEEVINEVDILYMTRIQRERFFNEEDYLKLKNSYILTRDKIKDAKEDMLIMHPLPRVNEIDYSVDDDKRAVYFKQAQYGVYVRMSLMAHLLGVV","length":308,"molWeight":35199,"crc64":"83E8ABCDC96DA6D0","md5":"BA3462CFF4D3581624B62BBACEBF9374"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":10},"uniParcId":"UPI00032FA9BE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ARJ6","uniProtkbId":"R1ARJ6_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":58,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99306.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024442"}],"value":"Type 3 secretion system ATPase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024382"}],"value":"7.4.2.8"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99306.1"}],"value":"L21TH_2655"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57720"},{"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":"7.1.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10106"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + cellular proteinSide 1 = ADP + phosphate + cellular proteinSide 2.","ecNumber":"7.4.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034006"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024342"}],"value":"Belongs to the ATPase alpha/beta chains family. T3SS ATPase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99306.1"}],"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":159,"modifier":"EXACT"},"end":{"value":340,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023065"}],"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022927"}],"id":"KW-0653","category":"Biological process","name":"Protein transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023026"}],"id":"KW-0843","category":"Biological process","name":"Virulence"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99306.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99306.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000280","properties":[{"key":"ProteinId","value":"EOC99306.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006317419.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000280.1"}]},{"database":"AlphaFoldDB","id":"R1ARJ6","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2655","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2609","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG1157","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9802718at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0030257","properties":[{"key":"GoTerm","value":"C:type III protein secretion system complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008564","properties":[{"key":"GoTerm","value":"F:protein-exporting ATPase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046961","properties":[{"key":"GoTerm","value":"F:proton-transporting ATPase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044780","properties":[{"key":"GoTerm","value":"P:bacterial-type flagellum assembly"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0071973","properties":[{"key":"GoTerm","value":"P:bacterial-type flagellum-dependent cell motility"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030254","properties":[{"key":"GoTerm","value":"P:protein secretion by the type III secretion system"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18117","properties":[{"key":"EntryName","value":"ATP-synt_flagellum-secretory_path_III_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01136","properties":[{"key":"EntryName","value":"ATPase_flagellum-secretory_path_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.12240:FF:000002","properties":[{"key":"EntryName","value":"Flagellum-specific ATP synthase FliI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12240","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR020003","properties":[{"key":"EntryName","value":"ATPase_a/bsu_AS"}]},{"database":"InterPro","id":"IPR050053","properties":[{"key":"EntryName","value":"ATPase_alpha/beta_chains"}]},{"database":"InterPro","id":"IPR004100","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR005714","properties":[{"key":"EntryName","value":"ATPase_T3SS_FliI/YscN"}]},{"database":"InterPro","id":"IPR013380","properties":[{"key":"EntryName","value":"ATPase_T3SS_SctN"}]},{"database":"InterPro","id":"IPR022425","properties":[{"key":"EntryName","value":"FliI_clade2"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR040627","properties":[{"key":"EntryName","value":"T3SS_ATPase_C"}]},{"database":"NCBIfam","id":"TIGR03497","properties":[{"key":"EntryName","value":"FliI_clade2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01026","properties":[{"key":"EntryName","value":"fliI_yscN"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02546","properties":[{"key":"EntryName","value":"III_secr_ATP"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184","properties":[{"key":"EntryName","value":"ATP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184:SF9","properties":[{"key":"EntryName","value":"SPI-1 TYPE 3 SECRETION SYSTEM ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02874","properties":[{"key":"EntryName","value":"ATP-synt_ab_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18269","properties":[{"key":"EntryName","value":"T3SS_ATPase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"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":"PS00152","properties":[{"key":"EntryName","value":"ATPASE_ALPHA_BETA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYEINIKKYLKETKAIEYIKYRGKVTKVTGLTIESSGPLAKIGELCYIYPFNQERPILAEVVGFKEEKILLMPLGDMEGIGPDSTVVASGHSLRVKVGENLIGRVLDGLGNPIDGKGPLKTTNYYSVFNNPPNPLKRKKIKEVLSLGIKSIDGLLTCGKGQRIGIFAGSGVGKSTLMGMIARNAQADINVIGLIGERGREVREFIEKDLKEEGLKKSVLVVATSDQPALVRMKGALLTTAIAEYFRDKGKNVMLLMDSLTRFAMAQREVGLAIGEPPVTRGYTPSVFAVLPRLLERAGTSDKGTITALYTVLVDGDDLNEPITDTVRGILDGHIVLSRKLANQNHYPAIDILASVSRVMPNIAQNEHIEISNKIKDMLATYKESEDLISIGAYKKGTNQKLDKAIDVIDLINEKLLKQGIMESYGFNDTLKIMKTINDKI","length":440,"molWeight":48279,"crc64":"71CC9B2ED6C098C8","md5":"8BE944661DC0DD751C6E0819BA603A03"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Site":1},"uniParcId":"UPI0003308E26"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ARM8","uniProtkbId":"R1ARM8_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":44,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99802.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012448"}],"value":"serine-type D-Ala-D-Ala carboxypeptidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012448"}],"value":"3.4.16.4"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99802.1"}],"value":"L21TH_2107"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003217"}],"value":"Removes C-terminal D-alanyl residues from sugar-peptide cell wall precursors"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Preferential cleavage: (Ac)2-L-Lys-D-Ala-|-D-Ala. Also transpeptidation of peptidyl-alanyl moieties that are N-acyl substituents of D-alanine.","ecNumber":"3.4.16.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034000"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004752"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007164"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004016"}],"value":"Belongs to the peptidase S11 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99802.1"}],"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":23,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":437,"modifier":"EXACT"}},"description":"serine-type D-Ala-D-Ala carboxypeptidase","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5055616340"},{"type":"Transmembrane","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":416,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"Peptidase S11 D-Ala-D-Ala carboxypeptidase A C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00936"}]},{"type":"Active site","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"Acyl-ester intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR618044-1"}]},{"type":"Active site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR618044-1"}]},{"type":"Active site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR618044-1"}]},{"type":"Binding site","location":{"start":{"value":238,"modifier":"EXACT"},"end":{"value":238,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR618044-2"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022645"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99802.1"}],"id":"KW-0121","category":"Molecular function","name":"Carboxypeptidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022960"}],"id":"KW-0133","category":"Biological process","name":"Cell shape"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023316"}],"id":"KW-0961","category":"Biological process","name":"Cell wall biogenesis/degradation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99802.1"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022984"}],"id":"KW-0573","category":"Biological process","name":"Peptidoglycan synthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022729"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99802.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99802.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000236","properties":[{"key":"ProteinId","value":"EOC99802.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006315660.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000236.1"}]},{"database":"AlphaFoldDB","id":"R1ARM8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2107","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2073","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG1686","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9791132at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00219","properties":[{"key":"RectionId","value":"-"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009002","properties":[{"key":"GoTerm","value":"F:serine-type D-Ala-D-Ala carboxypeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009252","properties":[{"key":"GoTerm","value":"P:peptidoglycan biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniPathway"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"2.60.410.10","properties":[{"key":"EntryName","value":"D-Ala-D-Ala carboxypeptidase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.710.10","properties":[{"key":"EntryName","value":"DD-peptidase/beta-lactamase superfamily"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012338","properties":[{"key":"EntryName","value":"Beta-lactam/transpept-like"}]},{"database":"InterPro","id":"IPR015956","properties":[{"key":"EntryName","value":"Peniciliin-bd_prot_C_sf"}]},{"database":"InterPro","id":"IPR018044","properties":[{"key":"EntryName","value":"Peptidase_S11"}]},{"database":"InterPro","id":"IPR012907","properties":[{"key":"EntryName","value":"Peptidase_S11_C"}]},{"database":"InterPro","id":"IPR037167","properties":[{"key":"EntryName","value":"Peptidase_S11_C_sf"}]},{"database":"InterPro","id":"IPR001967","properties":[{"key":"EntryName","value":"Peptidase_S11_N"}]},{"database":"PANTHER","id":"PTHR21581","properties":[{"key":"EntryName","value":"D-ALANYL-D-ALANINE CARBOXYPEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21581:SF33","properties":[{"key":"EntryName","value":"D-ALANYL-D-ALANINE CARBOXYPEPTIDASE DACB"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07943","properties":[{"key":"EntryName","value":"PBP5_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00768","properties":[{"key":"EntryName","value":"Peptidase_S11"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00725","properties":[{"key":"EntryName","value":"DADACBPTASE1"}]},{"database":"SMART","id":"SM00936","properties":[{"key":"EntryName","value":"PBP5_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56601","properties":[{"key":"EntryName","value":"beta-lactamase/transpeptidase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69189","properties":[{"key":"EntryName","value":"Penicillin-binding protein associated domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKNVIVGILSLFLVLNSFNISYADKPSITSHAAILIDANTGQVLFEKNAHKSMYPASTTKIMTAILALEKCNLGNKVTIDNETPYGIEGSHIALEPGEIISMEDLLYALLIESANDAAIAIAKHIGGSVENFAKLMNEKAKSIGAKNTHFTNPNGLPDKNHTTTAYDLAMMAKYAMEIDKFREIVKNYNYKIGATNKKSEPRYLKSANRLIYGTGSGNQIYVDGKWVDIKYEGAEGIKTGYTVAAQNCLVASAVRGNQRLISVVLHAQGTNVYVDTHKLLNYGFDNFNYKQLAFKNEFIENIKVTHGDNKYVPGIINQSIFATIPKGREDEIQKVLDIPEELSAPISIGQVLGTVKFTLDGETLATTNIVSTMEVNQKGIYQVVATTKKDSIWTKWWFWLIVLFILWRFYIAYIRYKRRKRRRSKRITYYNTKYNGY","length":437,"molWeight":49154,"crc64":"B82FD880D3318929","md5":"85887E55E35D1B3188B313CCC9D358A0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Transmembrane":1,"Domain":1,"Active site":3,"Binding site":1},"uniParcId":"UPI0003313BDF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ART8","uniProtkbId":"R1ART8_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-06-26","entryVersion":48,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99862.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00014680"}],"value":"Pyrimidine-nucleoside phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011889"}],"value":"2.4.2.2"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99862.1"}],"value":"L21TH_2086"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003877"}],"value":"Catalyzes phosphorolysis of the pyrimidine nucleosides uridine, thymidine and 2'-deoxyuridine with the formation of the corresponding pyrimidine base and ribose-1-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2'-deoxyuridine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22824"},{"database":"ChEBI","id":"CHEBI:16450"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57259"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001066"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"thymidine + phosphate = 2-deoxy-alpha-D-ribose 1-phosphate + thymine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16037"},{"database":"ChEBI","id":"CHEBI:17748"},{"database":"ChEBI","id":"CHEBI:17821"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57259"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048525"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uridine + phosphate = alpha-D-ribose 1-phosphate + uracil","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24388"},{"database":"ChEBI","id":"CHEBI:16704"},{"database":"ChEBI","id":"CHEBI:17568"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57720"}],"ecNumber":"2.4.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048453"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001958"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006915"}],"value":"Belongs to the thymidine/pyrimidine-nucleoside phosphorylase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99862.1"}],"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":345,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Pyrimidine nucleoside phosphorylase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00941"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99862.1"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99862.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99862.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99862.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000235","properties":[{"key":"ProteinId","value":"EOC99862.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006315629.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000235.1"}]},{"database":"AlphaFoldDB","id":"R1ART8","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2086","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2051","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0213","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9763887at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0004645","properties":[{"key":"GoTerm","value":"F:1,4-alpha-oligoglucan phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0047847","properties":[{"key":"GoTerm","value":"F:deoxyuridine phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0009032","properties":[{"key":"GoTerm","value":"F:thymidine phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004850","properties":[{"key":"GoTerm","value":"F:uridine phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:RHEA"}]},{"database":"GO","id":"GO:0006206","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006213","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleoside metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.20.970.10:FF:000002","properties":[{"key":"EntryName","value":"Pyrimidine-nucleoside phosphorylase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1030.10:FF:000003","properties":[{"key":"EntryName","value":"Pyrimidine-nucleoside phosphorylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1030.10","properties":[{"key":"EntryName","value":"Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1170.30","properties":[{"key":"EntryName","value":"Pyrimidine nucleoside phosphorylase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.970.10","properties":[{"key":"EntryName","value":"Transferase, Pyrimidine Nucleoside Phosphorylase, Chain C"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000312","properties":[{"key":"EntryName","value":"Glycosyl_Trfase_fam3"}]},{"database":"InterPro","id":"IPR017459","properties":[{"key":"EntryName","value":"Glycosyl_Trfase_fam3_N_dom"}]},{"database":"InterPro","id":"IPR036320","properties":[{"key":"EntryName","value":"Glycosyl_Trfase_fam3_N_dom_sf"}]},{"database":"InterPro","id":"IPR035902","properties":[{"key":"EntryName","value":"Nuc_phospho_transferase"}]},{"database":"InterPro","id":"IPR036566","properties":[{"key":"EntryName","value":"PYNP-like_C_sf"}]},{"database":"InterPro","id":"IPR013102","properties":[{"key":"EntryName","value":"PYNP_C"}]},{"database":"InterPro","id":"IPR018090","properties":[{"key":"EntryName","value":"Pyrmidine_PPas_bac/euk"}]},{"database":"InterPro","id":"IPR017872","properties":[{"key":"EntryName","value":"Pyrmidine_PPase_CS"}]},{"database":"InterPro","id":"IPR000053","properties":[{"key":"EntryName","value":"Thymidine/pyrmidine_PPase"}]},{"database":"NCBIfam","id":"NF004490","properties":[{"key":"EntryName","value":"PRK05820.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004747","properties":[{"key":"EntryName","value":"PRK06078.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02644","properties":[{"key":"EntryName","value":"Y_phosphoryl"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10515","properties":[{"key":"EntryName","value":"THYMIDINE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10515:SF0","properties":[{"key":"EntryName","value":"THYMIDINE PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02885","properties":[{"key":"EntryName","value":"Glycos_trans_3N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00591","properties":[{"key":"EntryName","value":"Glycos_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07831","properties":[{"key":"EntryName","value":"PYNP_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000478","properties":[{"key":"EntryName","value":"TP_PyNP"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00941","properties":[{"key":"EntryName","value":"PYNP_C"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52418","properties":[{"key":"EntryName","value":"Nucleoside phosphorylase/phosphoribosyltransferase catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47648","properties":[{"key":"EntryName","value":"Nucleoside phosphorylase/phosphoribosyltransferase N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54680","properties":[{"key":"EntryName","value":"Pyrimidine nucleoside phosphorylase C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00647","properties":[{"key":"EntryName","value":"THYMID_PHOSPHORYLASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRMYDIIMKKRNGGELTTEEINYFIEEYTKGNIPDYQVSALMMAIYFQKMNKRETADLTKAMVNSGVTIDLSDIKGVKVDKHSTGGVGDTTTLILGPIVAAAGVPVAKMSGRGLGHTGGTIDKLESFKGFSVEMTREQFVNNVNDKKIAIGGQTADLAPADKKLYALRDVTATVDNISLIASSIMSKKIAAGADAIVLDVKTGSGAFMKEEEASFELAKEMVDIGNNVGRNTVAVVTDMDQPLGFAVGNALEVKEAIDTLKGEGPVDLTELCLTLGSHMLVLGGQAESVEEARKILEDIISSGKGLAKLRELVEAQGGDPSYVDNPSLLPKASIEQPVIAAKEGYIKSIKADDIGKAALVLGAGRETKESEIDLSVGIVLHKKIGDYVKEGEAIATIHANSEEKQKTAEEMILSAYEIVSEEVKKNKLIKGIVTKDGIKTF","length":441,"molWeight":47145,"crc64":"539C74EB6F4AFB01","md5":"5B1EBD8CF89F0E5193214D5768EA5E2F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI000330F34C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ARU4","uniProtkbId":"R1ARU4_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-06-26","entryVersion":50,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99867.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"Methylated-DNA--protein-cysteine methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"2.1.1.63"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"6-O-methylguanine-DNA methyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"MGMT"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"O-6-methylguanine-DNA-alkyltransferase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99867.1"}],"value":"L21TH_2091"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"Involved in the cellular defense against the biological effects of O6-methylguanine (O6-MeG) and O4-methylthymine (O4-MeT) in DNA. Repairs the methylated nucleobase in DNA by stoichiometrically transferring the methyl group to a cysteine residue in the enzyme. This is a suicide reaction: the enzyme is irreversibly inactivated"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of alkylated DNA, releasing 3-methyladenine, 3-methylguanine, 7-methylguanine and 7-methyladenine.","ecNumber":"3.2.2.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000086"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 4-O-methyl-thymidine in DNA + L-cysteinyl-[protein] = a thymidine in DNA + S-methyl-L-cysteinyl-[protein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53428"},{"database":"Rhea","id":"RHEA-COMP:10131"},{"database":"Rhea","id":"RHEA-COMP:10132"},{"database":"Rhea","id":"RHEA-COMP:13555"},{"database":"Rhea","id":"RHEA-COMP:13556"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:82612"},{"database":"ChEBI","id":"CHEBI:137386"},{"database":"ChEBI","id":"CHEBI:137387"}],"ecNumber":"2.1.1.63","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001286"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10017"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 6-O-methyl-2'-deoxyguanosine in DNA + L-cysteinyl-[protein] = S-methyl-L-cysteinyl-[protein] + a 2'-deoxyguanosine in DNA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24000"},{"database":"Rhea","id":"RHEA-COMP:10131"},{"database":"Rhea","id":"RHEA-COMP:10132"},{"database":"Rhea","id":"RHEA-COMP:11367"},{"database":"Rhea","id":"RHEA-COMP:11368"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:82612"},{"database":"ChEBI","id":"CHEBI:85445"},{"database":"ChEBI","id":"CHEBI:85448"}],"ecNumber":"2.1.1.63","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049348"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10017"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"This enzyme catalyzes only one turnover and therefore is not strictly catalytic. According to one definition, an enzyme is a biocatalyst that acts repeatedly and over many reaction cycles"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008711"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"value":"Belongs to the MGMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010817"}],"value":"Belongs to the alkylbase DNA glycosidase AlkA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99867.1"}],"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":49,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"HhH-GPD","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00478"}]},{"type":"Active site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"Nucleophile; methyl group acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10017"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00772"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"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_00772"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99867.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99867.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000235","properties":[{"key":"ProteinId","value":"EOC99867.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006315634.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000235.1"}]},{"database":"AlphaFoldDB","id":"R1ARU4","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2091","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2056","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0122","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"eggNOG","id":"COG0350","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9785929at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0032993","properties":[{"key":"GoTerm","value":"C:protein-DNA complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032131","properties":[{"key":"GoTerm","value":"F:alkylated DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008725","properties":[{"key":"GoTerm","value":"F:DNA-3-methyladenine glycosylase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043916","properties":[{"key":"GoTerm","value":"F:DNA-7-methylguanine glycosylase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003908","properties":[{"key":"GoTerm","value":"F:methylated-DNA-[protein]-cysteine S-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006285","properties":[{"key":"GoTerm","value":"P:base-excision repair, AP site formation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006307","properties":[{"key":"GoTerm","value":"P:DNA alkylation repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd06445","properties":[{"key":"EntryName","value":"ATase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00056","properties":[{"key":"EntryName","value":"ENDO3c"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.340.30:FF:000004","properties":[{"key":"EntryName","value":"DNA-3-methyladenine glycosylase II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.10:FF:000214","properties":[{"key":"EntryName","value":"Methylated-DNA--protein-cysteine methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1670.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.340.30","properties":[{"key":"EntryName","value":"Hypothetical protein, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.160.70","properties":[{"key":"EntryName","value":"Methylated DNA-protein cysteine methyltransferase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00772","properties":[{"key":"EntryName","value":"OGT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051912","properties":[{"key":"EntryName","value":"Alkylbase_DNA_Glycosylase/TA"}]},{"database":"InterPro","id":"IPR011257","properties":[{"key":"EntryName","value":"DNA_glycosylase"}]},{"database":"InterPro","id":"IPR003265","properties":[{"key":"EntryName","value":"HhH-GPD_domain"}]},{"database":"InterPro","id":"IPR001497","properties":[{"key":"EntryName","value":"MethylDNA_cys_MeTrfase_AS"}]},{"database":"InterPro","id":"IPR014048","properties":[{"key":"EntryName","value":"MethylDNA_cys_MeTrfase_DNA-bd"}]},{"database":"InterPro","id":"IPR036217","properties":[{"key":"EntryName","value":"MethylDNA_cys_MeTrfase_DNAb"}]},{"database":"InterPro","id":"IPR008332","properties":[{"key":"EntryName","value":"MethylG_MeTrfase_N"}]},{"database":"InterPro","id":"IPR023546","properties":[{"key":"EntryName","value":"MGMT"}]},{"database":"InterPro","id":"IPR036631","properties":[{"key":"EntryName","value":"MGMT_N_sf"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"NCBIfam","id":"TIGR00589","properties":[{"key":"EntryName","value":"ogt"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43003","properties":[{"key":"EntryName","value":"DNA-3-METHYLADENINE GLYCOSYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43003:SF5","properties":[{"key":"EntryName","value":"DNA-3-METHYLADENINE GLYCOSYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01035","properties":[{"key":"EntryName","value":"DNA_binding_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00730","properties":[{"key":"EntryName","value":"HhH-GPD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02870","properties":[{"key":"EntryName","value":"Methyltransf_1N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00478","properties":[{"key":"EntryName","value":"ENDO3c"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48150","properties":[{"key":"EntryName","value":"DNA-glycosylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53155","properties":[{"key":"EntryName","value":"Methylated DNA-protein cysteine methyltransferase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF46767","properties":[{"key":"EntryName","value":"Methylated DNA-protein cysteine methyltransferase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00374","properties":[{"key":"EntryName","value":"MGMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYKKIEITKRELEHLKSCDKNMRKLIEYVGDIERYYIEDPFLALINSIVFQQLAYNAANAIWNRFLSLYDNITPEKVINTEFDTLRKCGLSKTKIEYIKNICRAIINNELDIENIDKLSDEQIIDKLVKIKGIGIWTAEMFLLFSLNRRNVLSYKDLGIRKGIKWLFNMKKEPTKDEFEKIKEKFSPYNTVASLYLWEITSRGLLNYDSTDILDRNIGYFDSPLGLIELQSKDGKLVSLDFAKEKVLEEKLDSVLEKTKQQLKEYFTGKRKKFDIPIELNGTDFQKRVWKELMNISYGKTLTYKEVAVNIGNKNASRAVGNANNKNKIAIIIPCHRVIGSSGKLIGYEGGLWRKKWLLQHEQQRENSSKSTAME","length":374,"molWeight":43569,"crc64":"38AEC947A54716FB","md5":"F19AC6511E36FB86377676DCA3CB0BE6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1},"uniParcId":"UPI00032FC0D5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AS25","uniProtkbId":"R1AS25_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2013-06-26","entryVersion":52,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99446.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"ATP synthase subunit beta"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"7.1.2.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"ATP synthase F1 sector subunit beta"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"F-ATPase subunit beta"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"atpD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99446.1"}],"value":"L21TH_2521"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Produces ATP from ADP in the presence of a proton gradient across the membrane. The catalytic sites are hosted primarily by the beta subunits"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059242"}],"value":"Produces ATP from ADP in the presence of a sodium ion gradient across the membrane. The beta chain is the catalytic subunit"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4 Na(+)(in) + ATP + H2O = 4 Na(+)(out) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:58156"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29101"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"7.2.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052325"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + 4 H(+)(in) = ADP + phosphate + 5 H(+)(out)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57720"},{"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":"7.1.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10106"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Peripheral membrane protein","id":"SL-9903"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004370"}],"value":"Membrane","id":"SL-0162"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008936"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"value":"Belongs to the ATPase alpha/beta chains family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99446.1"}],"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":145,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":344,"modifier":"EXACT"},"end":{"value":344,"modifier":"EXACT"}},"description":"Required for activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023310"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0066","category":"Biological process","name":"ATP synthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023196"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0139","category":"Cellular component","name":"CF(1)"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0375","category":"Biological process","name":"Hydrogen ion transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99446.1"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023065"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0406","category":"Biological process","name":"Ion transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01347"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99446.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99446.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000273","properties":[{"key":"ProteinId","value":"EOC99446.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006317135.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000273.1"}]},{"database":"AlphaFoldDB","id":"R1AS25","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2521","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2476","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0055","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9801639at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0045259","properties":[{"key":"GoTerm","value":"C:proton-transporting ATP synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046933","properties":[{"key":"GoTerm","value":"F:proton-transporting ATP synthase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046962","properties":[{"key":"GoTerm","value":"F:sodium-transporting ATPase activity, rotational mechanism"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd18110","properties":[{"key":"EntryName","value":"ATP-synt_F1_beta_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18115","properties":[{"key":"EntryName","value":"ATP-synt_F1_beta_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01133","properties":[{"key":"EntryName","value":"F1-ATPase_beta_CD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1140.10:FF:000001","properties":[{"key":"EntryName","value":"ATP synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.10.170:FF:000005","properties":[{"key":"EntryName","value":"ATP synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000026","properties":[{"key":"EntryName","value":"ATP synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.10.170","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1140.10","properties":[{"key":"EntryName","value":"Bovine Mitochondrial F1-atpase, Atp Synthase Beta Chain, Chain D, domain 3"},{"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_01347","properties":[{"key":"EntryName","value":"ATP_synth_beta_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR055190","properties":[{"key":"EntryName","value":"ATP-synt_VA_C"}]},{"database":"InterPro","id":"IPR005722","properties":[{"key":"EntryName","value":"ATP_synth_F1_bsu"}]},{"database":"InterPro","id":"IPR020003","properties":[{"key":"EntryName","value":"ATPase_a/bsu_AS"}]},{"database":"InterPro","id":"IPR050053","properties":[{"key":"EntryName","value":"ATPase_alpha/beta_chains"}]},{"database":"InterPro","id":"IPR004100","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N"}]},{"database":"InterPro","id":"IPR036121","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_N_sf"}]},{"database":"InterPro","id":"IPR000194","properties":[{"key":"EntryName","value":"ATPase_F1/V1/A1_a/bsu_nucl-bd"}]},{"database":"InterPro","id":"IPR024034","properties":[{"key":"EntryName","value":"ATPase_F1/V1_b/a_C"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR01039","properties":[{"key":"EntryName","value":"atpD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184","properties":[{"key":"EntryName","value":"ATP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR15184:SF71","properties":[{"key":"EntryName","value":"ATP SYNTHASE SUBUNIT BETA, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00006","properties":[{"key":"EntryName","value":"ATP-synt_ab"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02874","properties":[{"key":"EntryName","value":"ATP-synt_ab_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22919","properties":[{"key":"EntryName","value":"ATP-synt_VA_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF039072","properties":[{"key":"EntryName","value":"ATPase_subunit_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47917","properties":[{"key":"EntryName","value":"C-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50615","properties":[{"key":"EntryName","value":"N-terminal domain of alpha and beta subunits of F1 ATP synthase"},{"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":"PS00152","properties":[{"key":"EntryName","value":"ATPASE_ALPHA_BETA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAERNVGKIVQIIGPVVDIRFSEENLPKLLNAIEIEGNGKKVVCEVAQHIGDDTVRCIAMDSTDGFVRGMEAVDTGAPITVPVGRETLGRLFNVLGETIDEQGEVGAKEYSPIHKQAPSFEEQQTATEIFETGIKVVDLIAPYAKGGKIGLFGGAGVGKTVLIQELINNIAKEHGGLSVFAGVGERTREGNDLYYEMEESGALDKTTLVFGQMNEPPGARMRVALTGLTMAEHFRDKEGQDVLLFIDNIFRFTQAGSEVSALLGRMPSAVGYQPTLATEMGALQERITSTKKGSITSVQAVYVPADDLTDPAPATTFAHLDATTVLSRQIAELGIYPAVDPLDSTSRILDPAIVGEEHYRVARGVQEILQRYKELQDIIAILGMDELSDEDKLIVSRARKIQRFLSQPFHVAEQFTGMPGVYVPIKETVRGFKEILEGKHDDLPESAFLYVGTIDEAVEKAKNMK","length":465,"molWeight":50665,"crc64":"C525980ACEC7807F","md5":"8CF3C9486AB235AA5A2FFAFFEA8DF92C"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":1,"Site":1},"uniParcId":"UPI000331087B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1AS46","uniProtkbId":"R1AS46_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":48,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"tRNA-specific 2-thiouridylase MnmA"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"2.8.1.13"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"mnmA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99957.1"}],"value":"L21TH_2002"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056575"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"Catalyzes the 2-thiolation of uridine at the wobble position (U34) of tRNA, leading to the formation of s(2)U34"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in tRNA + AH2 + ATP = 2-thiouridine(34) in tRNA + L-cysteinyl-[protein] + A + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47032"},{"database":"Rhea","id":"RHEA-COMP:10131"},{"database":"Rhea","id":"RHEA-COMP:11726"},{"database":"Rhea","id":"RHEA-COMP:11727"},{"database":"Rhea","id":"RHEA-COMP:11728"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61963"},{"database":"ChEBI","id":"CHEBI:65315"},{"database":"ChEBI","id":"CHEBI:87170"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.8.1.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051542"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"Belongs to the MnmA/TRMU family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99957.1"}],"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":210,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"tRNA-specific 2-thiouridylase MnmA-like central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF20259"}]},{"type":"Domain","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"tRNA-specific 2-thiouridylase MnmA-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF20258"}]},{"type":"Region","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Region","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Active site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Binding site","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":16,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Site","location":{"start":{"value":126,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]},{"type":"Site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"Interaction with tRNA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99957.1"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022555"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00144"}],"id":"KW-0820","category":"Molecular function","name":"tRNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99957.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000221","properties":[{"key":"ProteinId","value":"EOC99957.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006315254.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000221.1"}]},{"database":"AlphaFoldDB","id":"R1AS46","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2002","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.1967","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0482","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9800696at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0103016","properties":[{"key":"GoTerm","value":"F:tRNA-uridine 2-sulfurtransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0002143","properties":[{"key":"GoTerm","value":"P:tRNA wobble position uridine thiolation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01998","properties":[{"key":"EntryName","value":"MnmA_TRMU-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.30.280:FF:000001","properties":[{"key":"EntryName","value":"tRNA-specific 2-thiouridylase MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.30.10:FF:000023","properties":[{"key":"EntryName","value":"tRNA-specific 2-thiouridylase MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000115","properties":[{"key":"EntryName","value":"tRNA-specific 2-thiouridylase MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.280","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like domains"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.30.10","properties":[{"key":"EntryName","value":"Translation factors"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00144","properties":[{"key":"EntryName","value":"tRNA_thiouridyl_MnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004506","properties":[{"key":"EntryName","value":"MnmA-like"}]},{"database":"InterPro","id":"IPR046885","properties":[{"key":"EntryName","value":"MnmA-like_C"}]},{"database":"InterPro","id":"IPR046884","properties":[{"key":"EntryName","value":"MnmA-like_central"}]},{"database":"InterPro","id":"IPR023382","properties":[{"key":"EntryName","value":"MnmA-like_central_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF001138","properties":[{"key":"EntryName","value":"mnmA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00420","properties":[{"key":"EntryName","value":"trmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11933:SF5","properties":[{"key":"EntryName","value":"MITOCHONDRIAL TRNA-SPECIFIC 2-THIOURIDYLASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11933","properties":[{"key":"EntryName","value":"TRNA 5-METHYLAMINOMETHYL-2-THIOURIDYLATE -METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03054","properties":[{"key":"EntryName","value":"tRNA_Me_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20258","properties":[{"key":"EntryName","value":"tRNA_Me_trans_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF20259","properties":[{"key":"EntryName","value":"tRNA_Me_trans_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDKNKVVIGMSGGVDSSVAAYLLKKQGYEVIGVTMEIYEEKNAKNDVQEISSVVSDAKKVAEKLNIPHYVVDLKDIFKEKVIDYFLHEYGRGRTPNPCIQCNKHVKFKALMQKAFDLGAYYLATGHYANVIYDKDVDRYLIKKSEADKKDQTYMLYNLTQEQLKHVLMPLGNFEDKEKVREIASELGLSVANKEESQEICFIEDDDYIRFIKENASYKIKPGHFIDTEGNILGKHKGITNYTIGQRKGLGLALGKPVYVIDILPEENVVVVGDAEKVFGKELIAEDINFISMSNLEEPMEVKAKIRYNFKEQPATIYPIEKDKVKVVFEKPVRAITPGQAVVFYKDDILVGGGTIVRKVR","length":360,"molWeight":40822,"crc64":"ACAA8DB72FB4F314","md5":"CCBA00D9909CB8D43DE4083454A676D4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":2,"Binding site":3,"Site":2},"uniParcId":"UPI00032DAE6D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ASF2","uniProtkbId":"R1ASF2_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":57,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00068.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012579"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"MECDP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"MECPP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"MECPS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012579"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"4.6.1.12"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"ispF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00068.1"}],"value":"L21TH_1878"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"Involved in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP), two major building blocks of isoprenoid compounds. Catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + CMP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23864"},{"database":"ChEBI","id":"CHEBI:57919"},{"database":"ChEBI","id":"CHEBI:58483"},{"database":"ChEBI","id":"CHEBI:60377"}],"ecNumber":"4.6.1.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000200"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004395"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"Binds 1 divalent metal cation per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004709"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 4/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008480"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004395"}],"value":"Belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00068.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":154,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02542"}]},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":8,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":35,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":61,"modifier":"EXACT"},"end":{"value":65,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":142,"modifier":"EXACT"},"end":{"value":142,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Site","location":{"start":{"value":34,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}]},{"type":"Site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"id":"KW-0414","category":"Biological process","name":"Isoprene biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00107"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00068.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOD00068.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000207","properties":[{"key":"ProteinId","value":"EOD00068.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006314755.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000207.1"}]},{"database":"AlphaFoldDB","id":"R1ASF2","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_1878","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.1846","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0245","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9804336at2","properties":[{"key":"Description","value":"-"}]},{"database":"UniPathway","id":"UPA00056","properties":[{"key":"RectionId","value":"UER00095"}]},{"database":"Proteomes","id":"UP000013378","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008685","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019288","properties":[{"key":"GoTerm","value":"P:isopentenyl diphosphate biosynthetic process, methylerythritol phosphate pathway"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016114","properties":[{"key":"GoTerm","value":"P:terpenoid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00554","properties":[{"key":"EntryName","value":"MECDP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1330.50:FF:000001","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1330.50","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00107","properties":[{"key":"EntryName","value":"IspF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003526","properties":[{"key":"EntryName","value":"MECDP_synthase"}]},{"database":"InterPro","id":"IPR020555","properties":[{"key":"EntryName","value":"MECDP_synthase_CS"}]},{"database":"InterPro","id":"IPR036571","properties":[{"key":"EntryName","value":"MECDP_synthase_sf"}]},{"database":"NCBIfam","id":"TIGR00151","properties":[{"key":"EntryName","value":"ispF"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43181:SF1","properties":[{"key":"EntryName","value":"2-C-METHYL-D-ERYTHRITOL 2,4-CYCLODIPHOSPHATE SYNTHASE, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02542","properties":[{"key":"EntryName","value":"YgbB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69765","properties":[{"key":"EntryName","value":"IpsF-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01350","properties":[{"key":"EntryName","value":"ISPF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRIGIGYDVHKLVEGRKLVLGGVEIEHSKGLLGHSDADVLIHAIMDSILGALGLGDIGRHFPDTDNKYKDISSMKLLEEVYEKMNEKGYKVNNIDAIIVAQKPKLAPYIEEMRQNIAAVLNTSKDNVNIKATTTEKLGFEGREEGISAQAVCTIDRM","length":157,"molWeight":17308,"crc64":"41FD098C163213A8","md5":"1ED164A9370694F8D45AD3166B0A46F3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":10,"Site":2},"uniParcId":"UPI00032F1D37"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"R1ASG7","uniProtkbId":"R1ASG7_9FIRM","entryAudit":{"firstPublicDate":"2013-06-26","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2013-06-26","entryVersion":58,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Caldisalinibacter kiritimatiensis","taxonId":1304284,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99601.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"lineage":["Bacteria","Bacillati","Bacillota","Tissierellia","Tissierellales","Thermohalobacteraceae","Caldisalinibacter"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"ATP-dependent Clp protease proteolytic subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000549"}],"value":"3.4.21.92"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Endopeptidase Clp"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"clpP"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99601.1"}],"value":"L21TH_2374"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000550"}],"value":"Cleaves peptides in various proteins in a process that requires ATP hydrolysis. Has a chymotrypsin-like activity. Plays a major role in the degradation of misfolded proteins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).","ecNumber":"3.4.21.92","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034021"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10086"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Fourteen ClpP subunits assemble into 2 heptameric rings which stack back to back to give a disk-like structure with a central cavity, resembling the structure of eukaryotic proteasomes"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007039"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003567"}],"value":"Belongs to the peptidase S14 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99601.1"}],"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":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10085"}]},{"type":"Active site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}]},{"type":"Active site","location":{"start":{"value":123,"modifier":"EXACT"},"end":{"value":123,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10086"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00444"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-9KAHVQQCFDD3","citationType":"journal article","authors":["Ben Hania W.","Joseph M.","Fiebig A.","Bunk B.","Klenk H.-P.","Fardeau M.-L.","Spring S."],"title":"Caldisalinibacter kiritimatiensis gen. nov., sp. nov., a moderately thermohalophilic thiosulfate-reducing bacterium from a hypersaline microbial mat.","publicationDate":"2015","journal":"Geomicrobiol. J.","firstPage":"347","lastPage":"354","volume":"32"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99601.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}],"value":"L21-TH-D2","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"EOC99601.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000013378"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"ARZA01000262","properties":[{"key":"ProteinId","value":"EOC99601.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_006316704.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_ARZA01000262.1"}]},{"database":"AlphaFoldDB","id":"R1ASG7","properties":[{"key":"Description","value":"-"}]},{"database":"STRING","id":"1304284.L21TH_2374","properties":[{"key":"Description","value":"-"}]},{"database":"PATRIC","id":"fig|1304284.3.peg.2328","properties":[{"key":"GeneDesignation","value":"-"}]},{"database":"eggNOG","id":"COG0740","properties":[{"key":"ToxonomicScope","value":"Bacteria"}]},{"database":"OrthoDB","id":"9802800at2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000013378","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:0009368","properties":[{"key":"GoTerm","value":"C:endopeptidase Clp complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051117","properties":[{"key":"GoTerm","value":"F:ATPase binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006515","properties":[{"key":"GoTerm","value":"P:protein quality control for misfolded or incompletely synthesized proteins"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07017","properties":[{"key":"EntryName","value":"S14_ClpP_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.226.10:FF:000001","properties":[{"key":"EntryName","value":"ATP-dependent Clp protease proteolytic subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.226.10","properties":[{"key":"EntryName","value":"2-enoyl-CoA Hydratase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00444","properties":[{"key":"EntryName","value":"ClpP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001907","properties":[{"key":"EntryName","value":"ClpP"}]},{"database":"InterPro","id":"IPR029045","properties":[{"key":"EntryName","value":"ClpP/crotonase-like_dom_sf"}]},{"database":"InterPro","id":"IPR023562","properties":[{"key":"EntryName","value":"ClpP/TepA"}]},{"database":"InterPro","id":"IPR033135","properties":[{"key":"EntryName","value":"ClpP_His_AS"}]},{"database":"InterPro","id":"IPR018215","properties":[{"key":"EntryName","value":"ClpP_Ser_AS"}]},{"database":"NCBIfam","id":"TIGR00493","properties":[{"key":"EntryName","value":"clpP"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001368","properties":[{"key":"EntryName","value":"PRK00277.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009205","properties":[{"key":"EntryName","value":"PRK12553.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10381:SF70","properties":[{"key":"EntryName","value":"ATP-DEPENDENT CLP PROTEASE PROTEOLYTIC SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00574","properties":[{"key":"EntryName","value":"CLP_protease"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00127","properties":[{"key":"EntryName","value":"CLPPROTEASEP"}]},{"database":"SUPFAM","id":"SSF52096","properties":[{"key":"EntryName","value":"ClpP/crotonase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00382","properties":[{"key":"EntryName","value":"CLP_PROTEASE_HIS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00381","properties":[{"key":"EntryName","value":"CLP_PROTEASE_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MALVPVVVEQTNRGERSYDIYSRLLKERIIFISDEINDATASLVVAQLLFLEADDPDKDIQLYINSPGGSITSGFAIYDTMQYIKPDVSTICIGMAASMGAFLLAAGAKGKRYALPNAEVMIHQPLGGTRGQAEDIKIHAERIIKMREQINKILSERTGQPYDKVSRDTDRDFFMTSQEAKEYGIIDEVITFRK","length":194,"molWeight":21700,"crc64":"8C439A8625929084","md5":"742CB26A1364452E2C453BAB8A0A1C60"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":3},"uniParcId":"UPI00032E460F"}}]}