{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FC24","uniProtkbId":"A0ABW3FC24_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915439.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915439.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915439.1"}],"value":"ACFQ14_03365"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057360"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Important for stationary phase survival"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915439.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":434,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Region","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":357,"modifier":"EXACT"},"end":{"value":371,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":268,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":227,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-104)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915439.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211281.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF0","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAAVEKDMNQSEGKCPVMHGTHSQVARGSTANQHWWPNQLNLKILHQNSGMVDPLGEDFDYATEFQKLDLEALYKDLESLMTTSQEWWPADYGHYGPFFIRMAWHSAGTYRIQDGRGGAGSGTQRFAPLNSWPDNGNLDKARALLWPIKQKYGNSLSWADLMVYAGNAALESMGFKTYGFGGGREDVFEPEEDIYWGPETTWLGDERYRGDRELDHPLAAVQMGLIYVNPEGPNGNPDPLGSARDIRETFARMAMNDEETVALVAGGHTFGKAHGAGDPEKFVGREPEGAPMEQMGLGWKNTMGSGKGVNTITSGVEGAWTYNPTKWDNEYFDILFGHEWELTKSPAGANQWTPKADSAKDTVPDAHDPNRRHAPMMTTADMALRMDPAYEKISRRFHENPDEFADAFAKAWYKLTHRDMGPIDRYLGSQVPSEPLIWQDPVPAVDHDLIDAADIKALKAKLLDCGLSVSQLVSTAWASASTFRGSDKRGGANGARLRLAPQKDWDVNNPAELAKALNAIEGVQKAFNDDQTGNKKVSLADLIVLGGCAAVEAAAKAAGQSVEVPFTPGRTDATDEMTDVDSFAVLEPTVDGFRNYIKDASAKGSRSTEELLIDRAQLLTLTAPEMTVLIGGLRVLGANAFGSTHGVFTDKPGTLNTGFFSTVLDYGIEWEPVAGSEEEFVGKDRTTGKTKWTGTRADLVFGANSQLRAQAEIYAQNGAEAKFANDFVAAWNKVMNLDRFDVK","length":743,"molWeight":81430,"crc64":"B2426FDEEBCAAB5E","md5":"CB88A285A65E35F0A2E35E35642CA549"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI003645C725"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FDP6","uniProtkbId":"A0ABW3FDP6_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916599.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916599.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916599.1"}],"value":"ACFQ14_09290"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs. m2A2503 modification seems to play a crucial role in the proofreading step occurring at the peptidyl transferase center and thus would serve to optimize ribosomal fidelity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007544"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916599.1"}],"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":130,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Active site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"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":208,"modifier":"EXACT"},"end":{"value":209,"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":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000009","properties":[{"key":"ProteinId","value":"MFD0916599.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377212458.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000009.1"}]},{"database":"Proteomes","id":"UP001597101","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:000008","properties":[{"key":"EntryName","value":"Dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPLSLDLTDAKTRLQWAGMTAASGDKIALIGLNKTQMAQAFKDAGVPEKQARMRASQVWQWIYVRGHDDFSRMSNIGKELRATLEEKFTLERPEIVEEQISEDGTRKWLFRFPARGAGAPVEVETVYIPEADRGTLCISSQVGCTLTCTFCHTGTQKLVRNLTAGEILMQLMVARDRLGDFPDADIPQGGVVPSEGRKVTNIVMMGMGEPLYNFEHVKQALLIAADGEGLGLSKRRITLSTSGVVPAIYRTGEEIGCALAISLHATNDALRDEIVPINKKHNIAELLQACRDYPGVSNAKRITFEYVMLKGVNDSLNEAKELVQLLKGIPAKINLIPFNPWPGSNYECSDWEEIEKFADFINANGYASPIRTPRGRDILAACGQLKSESERMRIKERMALEATRAMVAGHGED","length":413,"molWeight":45640,"crc64":"07FFE4AEB1F7EDBB","md5":"867C7B04C3F7BCF29FD44E38CE560015"},"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":"UPI003629B623"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FF99","uniProtkbId":"A0ABW3FF99_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915491.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme IspD/IspF"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2.7.7.60"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4-diphosphocytidyl-2C-methyl-D-erythritol synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MEP cytidylyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MCT"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECDP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPP-synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"MECPS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"4.6.1.12"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"ispDF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915491.1"}],"value":"ACFQ14_03625"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (IspD), and 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) (IspF)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-C-methyl-D-erythritol 4-phosphate + CTP + H(+) = 4-CDP-2-C-methyl-D-erythritol + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13429"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:57823"},{"database":"ChEBI","id":"CHEBI:58262"}],"ecNumber":"2.7.7.60","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001282"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}},{"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_01520"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"a divalent metal cation","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001968"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60240"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004787"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004709"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"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":"ARBA","id":"ARBA00009789"}],"value":"Belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008480"}],"value":"Belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the C-terminal section; belongs to the IspF family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"In the N-terminal section; belongs to the IspD/TarI cytidylyltransferase family. IspD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915491.1"}],"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":236,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02542"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":236,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Region","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":245,"modifier":"EXACT"},"end":{"value":245,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60240"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"a divalent metal cation","id":"ChEBI:CHEBI:60240"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":367,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Binding site","location":{"start":{"value":377,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57919"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"ligand":{"name":"4-CDP-2-C-methyl-D-erythritol 2-phosphate","id":"ChEBI:CHEBI:57919"}},{"type":"Site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"Positions MEP for the nucleophilic attack","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]},{"type":"Site","location":{"start":{"value":368,"modifier":"EXACT"},"end":{"value":368,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"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_01520"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01520"}],"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_01520"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"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_01520"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000003","properties":[{"key":"ProteinId","value":"MFD0915491.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211352.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000003.1"}]},{"database":"Proteomes","id":"UP001597101","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:0050518","properties":[{"key":"GoTerm","value":"F:2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase 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":"cd02516","properties":[{"key":"EntryName","value":"CDP-ME_synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00554","properties":[{"key":"EntryName","value":"MECDP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.550.10:FF:000003","properties":[{"key":"EntryName","value":"2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase"},{"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":"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_00108","properties":[{"key":"EntryName","value":"IspD"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01520","properties":[{"key":"EntryName","value":"IspDF"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00107","properties":[{"key":"EntryName","value":"IspF"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001228","properties":[{"key":"EntryName","value":"IspD"}]},{"database":"InterPro","id":"IPR026596","properties":[{"key":"EntryName","value":"IspD/F"}]},{"database":"InterPro","id":"IPR034683","properties":[{"key":"EntryName","value":"IspD/TarI"}]},{"database":"InterPro","id":"IPR018294","properties":[{"key":"EntryName","value":"ISPD_synthase_CS"}]},{"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":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"NCBIfam","id":"TIGR00453","properties":[{"key":"EntryName","value":"ispD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00151","properties":[{"key":"EntryName","value":"ispF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006899","properties":[{"key":"EntryName","value":"PRK09382.1"},{"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":"PF01128","properties":[{"key":"EntryName","value":"IspD"},{"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":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01295","properties":[{"key":"EntryName","value":"ISPD"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01350","properties":[{"key":"EntryName","value":"ISPF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEPLKIAAIIVAAGRGARAGVADGPKQYRMLGSKPVLAHTLHAFVHHRAVTSVLTVIHEDDGASYAKAAPENPKILPPVHGGATRQASVFAGLQALAQDAPDLVLIHDAARPFLSAAVIDAVIAGLGEAKAALPATAIVDTIKRSAEDGSVADTISRDGLFAAQTPQGFDFATILEAHSKAAAAGLNDFTDDSALAEWAGHRVVLVAGSRDNLKLTTQDDIEKAQSSMGEQITDVRVGHGYDTHQLVAGEKITLCGVEIPFERKLSGHSDADVGLHALTDALLGTIADGDIGSHFPPSDPEWKGAQSDQFLAHAASLVRAAGGTITHCDVTLVCEAPKIGPHRDAMRAAMAAILDMDVTRISVKATTNERIGFIGREEGMVALATATVVMNGTTL","length":396,"molWeight":41187,"crc64":"92A571AAE585B240","md5":"EE58AEB7EED124C33C475C92D65DE5FA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":2,"Binding site":9,"Site":6},"uniParcId":"UPI0036397847"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FGF4","uniProtkbId":"A0ABW3FGF4_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916350.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthase large chain"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"6.3.5.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Carbamoyl phosphate synthetase ammonia chain"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916350.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916350.1"}],"value":"ACFQ14_08030"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057223"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Large subunit of the glutamine-dependent carbamoyl phosphate synthetase (CPSase). CPSase catalyzes the formation of carbamoyl phosphate from the ammonia moiety of glutamine, carbonate, and phosphate donated by ATP, constituting the first step of 2 biosynthetic pathways, one leading to arginine and/or urea and the other to pyrimidine nucleotides. The large subunit (synthetase) binds the substrates ammonia (free or transferred from glutamine from the small subunit), hydrogencarbonate and ATP and carries out an ATP-coupled ligase reaction, activating hydrogencarbonate by forming carboxy phosphate which reacts with ammonia to form carbamoyl phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + L-glutamine + 2 ATP + H2O = carbamoyl phosphate + L-glutamate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18633"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048816"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogencarbonate + NH4(+) + 2 ATP = carbamoyl phosphate + 2 ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18029"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17544"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047359"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Binds 4 Mg(2+) or Mn(2+) ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005077"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Amino-acid biosynthesis; L-arginine biosynthesis; carbamoyl phosphate from bicarbonate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062056"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Composed of two chains; the small (or glutamine) chain promotes the hydrolysis of glutamine to ammonia, which is used by the large (or ammonia) chain to synthesize carbamoyl phosphate. Tetramer of heterodimers (alpha,beta)4"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"The large subunit is composed of 2 ATP-grasp domains that are involved in binding the 2 ATP molecules needed for carbamoyl phosphate synthesis. The N-terminal ATP-grasp domain (referred to as the carboxyphosphate synthetic component) catalyzes the ATP-dependent phosphorylation of hydrogencarbonate to carboxyphosphate and the subsequent nucleophilic attack by ammonia to form a carbamate intermediate. The C-terminal ATP-grasp domain (referred to as the carbamoyl phosphate synthetic component) then catalyzes the phosphorylation of carbamate with the second ATP to form the end product carbamoyl phosphate. The reactive and unstable enzyme intermediates are sequentially channeled from one active site to the next through the interior of the protein over a distance of at least 96 A"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009799"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916350.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":1139,"modifier":"EXACT"}},"description":"Carbamoyl phosphate synthase large chain","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"featureId":"PRO_5049656334"},{"type":"Domain","location":{"start":{"value":178,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":741,"modifier":"EXACT"},"end":{"value":933,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1002,"modifier":"EXACT"},"end":{"value":1139,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":1002,"modifier":"EXACT"},"end":{"value":1139,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":135,"modifier":"EXACT"},"end":{"value":135,"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":218,"modifier":"EXACT"},"end":{"value":218,"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":224,"modifier":"EXACT"},"end":{"value":224,"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":225,"modifier":"EXACT"},"end":{"value":225,"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":257,"modifier":"EXACT"},"end":{"value":257,"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":259,"modifier":"EXACT"},"end":{"value":259,"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":264,"modifier":"EXACT"},"end":{"value":264,"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":290,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":292,"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":334,"modifier":"EXACT"},"end":{"value":334,"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":334,"modifier":"EXACT"},"end":{"value":334,"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":334,"modifier":"EXACT"},"end":{"value":334,"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":348,"modifier":"EXACT"},"end":{"value":348,"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":348,"modifier":"EXACT"},"end":{"value":348,"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":348,"modifier":"EXACT"},"end":{"value":348,"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":348,"modifier":"EXACT"},"end":{"value":348,"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":348,"modifier":"EXACT"},"end":{"value":348,"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":350,"modifier":"EXACT"},"end":{"value":350,"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":350,"modifier":"EXACT"},"end":{"value":350,"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":777,"modifier":"EXACT"},"end":{"value":777,"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":816,"modifier":"EXACT"},"end":{"value":816,"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":818,"modifier":"EXACT"},"end":{"value":818,"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":849,"modifier":"EXACT"},"end":{"value":849,"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":850,"modifier":"EXACT"},"end":{"value":850,"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":851,"modifier":"EXACT"},"end":{"value":851,"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":852,"modifier":"EXACT"},"end":{"value":852,"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":892,"modifier":"EXACT"},"end":{"value":892,"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":892,"modifier":"EXACT"},"end":{"value":892,"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":892,"modifier":"EXACT"},"end":{"value":892,"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":904,"modifier":"EXACT"},"end":{"value":904,"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":904,"modifier":"EXACT"},"end":{"value":904,"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":904,"modifier":"EXACT"},"end":{"value":904,"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":904,"modifier":"EXACT"},"end":{"value":904,"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":904,"modifier":"EXACT"},"end":{"value":904,"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":906,"modifier":"EXACT"},"end":{"value":906,"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":906,"modifier":"EXACT"},"end":{"value":906,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"N-palmitoyl cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]},{"type":"Lipidation","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"S-diacylglycerol cysteine","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0449","category":"PTM","name":"Lipoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0564","category":"PTM","name":"Palmitate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00303"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000005","properties":[{"key":"ProteinId","value":"MFD0916350.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377212207.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000005.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000013","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_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":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51257","properties":[{"key":"EntryName","value":"PROKAR_LIPOPROTEIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRQDIDSILIIGAGPIVIGQACEFDYSGTQACKALREEGYRIVLVNSNPATIMTDPDMADATYIEPITPEIVAKIIKREREMHPDEKMVLLPTMGGQTALNTALSLEKMGTLEEYDVEMIGAKAKAIDMAEDRDLFRAAMDRIGLATPASSFVNTTELKKRFEAEKKAHFKQKGNAAALQKEWDEGEEFRLEEHRLEAQRQALMAMKKTGLPAIIRPSFTMGGLGGGIAYTREELYSIVMSGVDASPTNEVLVEESVLGWKEYEMEVVRDRADNCIIICSIENVDPMGVHTGDSITVAPALTLTDKEYQIMRNASIAVLREIGVETGGSNVQFAVNPADGRLVVIEMNPRVSRSSALASKATGFPIASVAARLAVGYTLDELENDITGGATPASFEPSIDYVVTKIPRFAFEKFGAASDTLTTSMKSVGEVMAIGRTFAESMQKALRGLETGLNGFDEVEIEDWSDEDDSDNKNAIRAALGTPKADRILKVAEAMRRGTDLATIHKACRIDMWFLEQIKAIVDMEARVREHGLPEDADNLRMLKAMGFSDARLAKLSGQTAAQISDARTKMDVHPVFKRIDTCAAEFASPTAYMYSTYETPFAGETRGEDGISDRRKVMILGGGPNRIGQGIEFDYCCCHAAYALEDAGFETIMVNCNPETVSTDYDTSDRLYFEPLTTEDVLEIVRLEQSKGTFEGVIVQFGGQTPLKLANDLQAAGVPILGTSPDAIDAAEDRDRFQKMLQDEKLTQPVNGIARSVDQARTIVKQVGYPVVIRPSYVLGGRAMEIVRDDRQFERYINEAVVVSGDTPVLIDSYLTNAIEVDVDCLRDSTGDTFVAGIMEHIEEAGIHSGDSACSLPTHSLDDAMLDELERQTKAMAAALNVVGLMNVQFAIKDGTIYVLEVNPRASRTVPFVAKTIGVPIAGLAARIMAGETLNDLLPVRPRYRDLKHIAVKEAVFPFARFPGVDTLLGPEMRSTGEVMGLDRDYALAFAKAQLGASQILPLTGTVFVSVKKGDKDRILPGVKKLAALGFEIIATGGTQRFLEENGVACERINKVLEGRPHIVDAIRNKQVELIFNTTEGAKALSDSRSIREAALLNKVPYFTTVAGCIAGADAIEAMTNGEIEVAPLQSYFDAA","length":1139,"molWeight":124132,"crc64":"3B3385415B129268","md5":"E14120B2B7D468D11E837B27B79B9A21"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Chain":1,"Domain":3,"Region":2,"Binding site":38,"Lipidation":2},"uniParcId":"UPI00363A94E0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FGW4","uniProtkbId":"A0ABW3FGW4_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915612.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine hydroxymethyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"SHMT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Serine methylase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"2.1.2.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915612.1"}],"value":"glyA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915612.1"}],"value":"ACFQ14_04270"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00057572"}],"value":"Catalyzes the reversible interconversion of alpha-methyl-L-serine to D-alanine with tetrahydrofolate (THF) serving as the one-carbon carrier. Cannot use alpha-methyl-D-serine, L-serine, D-serine or L-alanine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Catalyzes the reversible interconversion of serine and glycine with tetrahydrofolate (THF) serving as the one-carbon carrier. This reaction serves as the major source of one-carbon groups required for the biosynthesis of purines, thymidylate, methionine, and other important biomolecules. Also exhibits THF-independent aldolase activity toward beta-hydroxyamino acids, producing glycine and aldehydes, via a retro-aldol mechanism"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + D-alanine + H2O = 2-methylserine + (6S)-5,6,7,8-tetrahydrofolate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10064"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:57416"},{"database":"ChEBI","id":"CHEBI:57453"},{"database":"ChEBI","id":"CHEBI:58275"}],"ecNumber":"2.1.2.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051216"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate + glycine + H2O = (6S)-5,6,7,8-tetrahydrofolate + L-serine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15481"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15636"},{"database":"ChEBI","id":"CHEBI:33384"},{"database":"ChEBI","id":"CHEBI:57305"},{"database":"ChEBI","id":"CHEBI:57453"}],"ecNumber":"2.1.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Amino-acid biosynthesis; glycine biosynthesis; glycine from L-serine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"One-carbon metabolism; tetrahydrofolate interconversion"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006376"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Belongs to the SHMT family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915612.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":396,"modifier":"EXACT"}},"description":"Serine hydroxymethyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00464"}]},{"type":"Binding site","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":132,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Binding site","location":{"start":{"value":256,"modifier":"EXACT"},"end":{"value":256,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57453"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"ligand":{"name":"(6S)-5,6,7,8-tetrahydrofolate","id":"ChEBI:CHEBI:57453"}},{"type":"Site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Plays an important role in substrate specificity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}]},{"type":"Modified residue","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000412-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00051"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"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_00051"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000003","properties":[{"key":"ProteinId","value":"MFD0915612.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211463.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000003.1"}]},{"database":"Proteomes","id":"UP001597101","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:0050413","properties":[{"key":"GoTerm","value":"F:D-alanine 2-hydroxymethyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004372","properties":[{"key":"GoTerm","value":"F:glycine hydroxymethyltransferase 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:0006545","properties":[{"key":"GoTerm","value":"P:glycine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0035999","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate interconversion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00378","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.640.10:FF:000001","properties":[{"key":"EntryName","value":"Serine hydroxymethyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00051","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"InterPro","id":"IPR001085","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase"}]},{"database":"InterPro","id":"IPR049943","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase-like"}]},{"database":"InterPro","id":"IPR019798","properties":[{"key":"EntryName","value":"Ser_HO-MeTrfase_PLP_BS"}]},{"database":"InterPro","id":"IPR039429","properties":[{"key":"EntryName","value":"SHMT-like_dom"}]},{"database":"NCBIfam","id":"NF000586","properties":[{"key":"EntryName","value":"PRK00011.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11680:SF35","properties":[{"key":"EntryName","value":"SERINE HYDROXYMETHYLTRANSFERASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00464","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000412","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00096","properties":[{"key":"EntryName","value":"SHMT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAAVEKAPQKANTFFTRSLEDTDAAVFAAIKGELGRQRHEVELIASENIVSRAVLEAQGSVMTNKYAEGYSGRRYYGGCEFVDIAEDLAIERITKLFDCGFANVQPNSGSQANQAVFQALIKPGDTILGMSLDAGGHLTHGAAPNQSGKWFNAVQYGVRKEDDLIDYDQVEALAKEHQPKLIIAGGSAYPRQIDFARFREIADMVGAYLHVDMAHFSGLVAGGAHPSPFPHAHVATSTTHKTLRGPRGGLILTNDEALAKKFNSAIFPGIQGGPLMHVIAAKAVAFGEALTPEYGSYVASVVENAKALGETLKAGGLDLVSGGTDTHVLLVDLRPKGVTGKAAEAAMGRANMTCNKNGVPFDPEKPMVTSGVRLGTPAATTRGFGVAEFQMVGECILEVLDGLAANGEEGNAEVEQAVAKKIIALTDRFPIYPLI","length":435,"molWeight":46095,"crc64":"0ADC39E189B8B536","md5":"99F1C7EF06C20C9BEA3009E254AB23B0"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":3,"Site":1,"Modified residue":1},"uniParcId":"UPI00362614BF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FHJ4","uniProtkbId":"A0ABW3FHJ4_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916274.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"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":"MFD0916274.1"}],"value":"ACFQ14_07640"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Catalyzes the addition of meso-diaminopimelic acid to the nucleotide precursor UDP-N-acetylmuramoyl-L-alanyl-D-glutamate (UMAG) in the biosynthesis of bacterial cell-wall peptidoglycan"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6-diaminopimelate + ATP = UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D-glutamyl-meso-2,6-diaminopimelate + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23676"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57791"},{"database":"ChEBI","id":"CHEBI:83900"},{"database":"ChEBI","id":"CHEBI:83905"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.2.13","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cell wall biogenesis; peptidoglycan biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004135"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Carboxylation is probably crucial for Mg(2+) binding and, consequently, for the gamma-phosphate positioning of ATP"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Belongs to the MurCDEF family. MurE subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0916274.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":327,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":404,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":27,"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":104,"modifier":"EXACT"},"end":{"value":110,"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":146,"modifier":"EXACT"},"end":{"value":147,"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":173,"modifier":"EXACT"},"end":{"value":173,"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":181,"modifier":"EXACT"},"end":{"value":181,"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":377,"modifier":"EXACT"},"end":{"value":377,"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":401,"modifier":"EXACT"},"end":{"value":404,"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":449,"modifier":"EXACT"},"end":{"value":449,"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":453,"modifier":"EXACT"},"end":{"value":453,"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":213,"modifier":"EXACT"},"end":{"value":213,"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":"MFD0916274.1"}],"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":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000005","properties":[{"key":"ProteinId","value":"MFD0916274.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377212314.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000005.1"}]},{"database":"Proteomes","id":"UP001597101","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":"MKLSELLVEGASLDGADVTVSSITMDSRKVMRGSLFAALKGTDVDGASYIPAAIEAGAVAVLADADTAACAVPIVRSDDPRRTLALMAAKFHPRQPSVMAAVTGTAGKTSVASFLRQIWESCGEQAAMIGTTGVFAPGRADYGSLTTPDPVLLHELLDELAGSGVSHCSMEASSHGLDQRRLDGVNLAVAGFTNLGRDHMDYHPTVEHYLASKMRLFDTLMDAGKPAIIYADDAYSAPAIAAAEAAGLDVKTVGRAGNFIALKRVEQRQFTQEAELDIDGEIHFLSLPMAGEFQLANALVAAGMAIATGSDPAAVLAALKRLKGAPGRLELIGQAGNGAPAYVDYAHKPEALENVLKALRPYTTGKLVVVFGCGGDRDPGKRPIMGEIAQRLADLVIVTDDNPRTEKPSSIRAQILEATPDAIEIGDRKKAIEEAVAKLEAGDCLVVAGKGHEEGQIVGKEVLPFSDHKVLAAALEATL","length":479,"molWeight":50154,"crc64":"075BC8A440AF82DD","md5":"2E2412496CB1E19D2F55DF5EE4231AF6"},"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":"UPI003633BE00"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FHX1","uniProtkbId":"A0ABW3FHX1_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917348.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Coenzyme A biosynthesis bifunctional protein CoaBC"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"DNA/pantothenate metabolism flavoprotein"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase/decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPCS-PPCDC"}]}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-DC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"4.1.1.36"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaC"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenate--cysteine ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"6.3.2.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"CoaB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"Phosphopantothenoylcysteine synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"value":"PPC-S"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917348.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917348.1"}],"value":"ACFQ14_13115"}]}],"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":"MFD0917348.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":190,"modifier":"EXACT"},"end":{"value":400,"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":194,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"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":292,"modifier":"EXACT"},"end":{"value":292,"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":310,"modifier":"EXACT"},"end":{"value":313,"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":329,"modifier":"EXACT"},"end":{"value":329,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":343,"modifier":"EXACT"},"end":{"value":343,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"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":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000012","properties":[{"key":"ProteinId","value":"MFD0917348.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377213209.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000012.1"}]},{"database":"Proteomes","id":"UP001597101","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":"MKQTLSQRSILLVIGGGIAAYKCLDLIRRLRERGADVRVVMSEAAQQFVTPMSVGAISGGTVFTDIWDREAEQDIGHIRLAREADLIIVAPATADLMAKMANGLANDLATAVLLATTAPVLVAPAMNPAMWDNPATQRNVETLSLDGKHFVGPNEGEMAESGEAGAGRMAEPMEILRAAEDLLDNTPKPLAGKRAIVTSGPTREDIDPVRYISNHSSGKQGHAIAAALAQAGAEVLLVSGPVSIPDPHDVTVVNVICAVDMQQAVDRALPADIAVFVAAVADWRVDSQASEKIKKDKSGKPPALSMIENPDILAGVGNGKKRPALVVGFAAETENVVDHARAKLAKKGADWIVANDVSEENNVFGGDANTVRLISAHDDEAWPKMSKEDVAAKLVERIAQRFETVSV","length":407,"molWeight":43115,"crc64":"460DD332DCC98DEA","md5":"1B17543F482BBBB341840B2F7DEC70FD"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI00362C25F6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FIK2","uniProtkbId":"A0ABW3FIK2_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917935.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bifunctional protein GlmU"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"UDP-N-acetylglucosamine pyrophosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.7.7.23"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"N-acetylglucosamine-1-phosphate uridyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Glucosamine-1-phosphate N-acetyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"2.3.1.157"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917935.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917935.1"}],"value":"ACFQ14_16135"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917935.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"MobA-like NTP transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12804"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Active site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":13,"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":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":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":229,"modifier":"EXACT"},"end":{"value":229,"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":229,"modifier":"EXACT"},"end":{"value":229,"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":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":351,"modifier":"EXACT"},"end":{"value":351,"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":362,"modifier":"EXACT"},"end":{"value":362,"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":365,"modifier":"EXACT"},"end":{"value":365,"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":371,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":408,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":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"}}],"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":"UP001597101"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000026","properties":[{"key":"ProteinId","value":"MFD0917935.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377213789.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000026.1"}]},{"database":"Proteomes","id":"UP001597101","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:InterPro"}]},{"database":"CDD","id":"cd02540","properties":[{"key":"EntryName","value":"GT2_GlmU_N_bac"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03353","properties":[{"key":"EntryName","value":"LbH_GlmU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.160.10.10","properties":[{"key":"EntryName","value":"Hexapeptide repeat proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.550.10","properties":[{"key":"EntryName","value":"Spore Coat Polysaccharide Biosynthesis Protein SpsA, Chain A"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01631","properties":[{"key":"EntryName","value":"GlmU"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005882","properties":[{"key":"EntryName","value":"Bifunctional_GlmU"}]},{"database":"InterPro","id":"IPR050065","properties":[{"key":"EntryName","value":"GlmU-like"}]},{"database":"InterPro","id":"IPR038009","properties":[{"key":"EntryName","value":"GlmU_C_LbH"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010933","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSRTCLTIILAAGEGKRMASAMPKVLHPVAGLSMVGHVIAAAKLAGSNDVAVVVGNQAQRVSQHVLALDKSLKVYEQTERKGTAHAVLAASEAIQQGYDDIIILFGDVPLLKAETLATARQGLANGGDIIVCGFETATPHGYGRMIMDGNSLVAIREHKDASEEERQITFCNSGIMAFRGDRLLDLLTAVKNDNEQGEYYLPDTVQIGVANGLNTMAVEVPENDTLGVNDRVQLARVSELWQARKAEELMRAGVTISAPSTVLFQHDTVVEPDAVLEPNIVFDAGVIVKSGATIRSFSHLEGTIVSQDAVIGPFARLRPGTVIEKSAKVGNFVETKNTVLGEGAKINHLSYIGDAKVGTKANIGAGTVTCNYDGVNKHATTIGAGAFIGTNSSLVAPIEIGRDAMTAAGSVVTKDVPDEALAVERSEQKTIKGLAAKIRKRNQAIKNAKKA","length":451,"molWeight":47668,"crc64":"C3730FF59AE289CB","md5":"DFD8733B73DCEEF49B72FAA93AB40BFD"},"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":"UPI00363A65B0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FJ21","uniProtkbId":"A0ABW3FJ21_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917523.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"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":"MFD0917523.1"}],"value":"ACFQ14_14020"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00059148"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0917523.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":265,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":380,"modifier":"EXACT"},"end":{"value":380,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":519,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":521,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":54,"modifier":"EXACT"},"end":{"value":54,"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":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":71,"modifier":"EXACT"},"end":{"value":71,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":146,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":353,"modifier":"EXACT"},"end":{"value":353,"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":381,"modifier":"EXACT"},"end":{"value":384,"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":404,"modifier":"EXACT"},"end":{"value":404,"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":472,"modifier":"EXACT"},"end":{"value":472,"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":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000013","properties":[{"key":"ProteinId","value":"MFD0917523.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377213382.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000013.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MARYVFITGGVVSSLGKGLASAALGALLQARGYKVRLRKLDPYLNVDPGTMSPYQHGECFVTDDGAETDLDLGHYERFTGRPANQSDNITTGRIYSDILAKERRGDYLGATVQVIPHVTNAIKEFVLDGNDDYDFVLMEIGGTVGDIEGLPFFESIRQLGNDLPKGGAIYLHLSYMPYIAAAGELKTKPTQHSVKELRSIGIQPDILLVRADREIPLEERRKLALFCNVRPEAVIQALDAKSIYDVPMAYHREGLDQQVLDAFGIDPAPKPQMQVWEDISRRLHNPEGEVSVAIVGKYTVLKDAYKSLMEALVHGGLANGVRVNLKWIDSSDLENDQPEDHLSDVDAILVPGGFGERGSEGKIVAATYAREHKIPYFGICFGMQMAVLDAARNLAGIADATSSELDEKNTSKNHVVGLMTEWLKGNQLEKREAAGDLGGTMRLGAYPHPLKEGSHIAEIYGSNEVSERHRHRYEVNIDYKDRLEEAGLVFSGMSPDGLLPETVEYPRDEHPWFIGVQYHPELKSRPFEPHPLFASFIAAAKEQSRLV","length":547,"molWeight":60540,"crc64":"D2D66FE410B13013","md5":"2C05F201E610741B777F3047D06D6566"},"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":"UPI003625D47E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F8V6","uniProtkbId":"A0ABW3F8V6_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914904.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012060"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012060"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"4.2.1.10"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"Type II DHQase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914904.1"}],"value":"aroQ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914904.1"}],"value":"ACFQ14_00625"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003924"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"Catalyzes a trans-dehydration via an enolate intermediate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-dehydroquinate = 3-dehydroshikimate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21096"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:32364"}],"ecNumber":"4.2.1.10","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001864"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004902"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011193"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"Homododecamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011037"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"value":"Belongs to the type-II 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914904.1"}],"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":24,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-1"}]},{"type":"Active site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-1"}]},{"type":"Binding site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":88,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-2"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001399-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00169"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0914904.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377210761.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0003855","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019631","properties":[{"key":"GoTerm","value":"P:quinate catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00466","properties":[{"key":"EntryName","value":"DHQase_II"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.9100","properties":[{"key":"EntryName","value":"Dehydroquinase, class II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00169","properties":[{"key":"EntryName","value":"AroQ"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001874","properties":[{"key":"EntryName","value":"DHquinase_II"}]},{"database":"InterPro","id":"IPR018509","properties":[{"key":"EntryName","value":"DHquinase_II_CS"}]},{"database":"InterPro","id":"IPR036441","properties":[{"key":"EntryName","value":"DHquinase_II_sf"}]},{"database":"NCBIfam","id":"TIGR01088","properties":[{"key":"EntryName","value":"aroQ"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003805","properties":[{"key":"EntryName","value":"PRK05395.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003806","properties":[{"key":"EntryName","value":"PRK05395.1-3"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF003807","properties":[{"key":"EntryName","value":"PRK05395.1-4"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21272","properties":[{"key":"EntryName","value":"CATABOLIC 3-DEHYDROQUINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21272:SF3","properties":[{"key":"EntryName","value":"CATABOLIC 3-DEHYDROQUINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01220","properties":[{"key":"EntryName","value":"DHquinase_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001399","properties":[{"key":"EntryName","value":"DHquinase_II"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52304","properties":[{"key":"EntryName","value":"Type II 3-dehydroquinate dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01029","properties":[{"key":"EntryName","value":"DEHYDROQUINASE_II"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPSSILLLNGPNLNMLGLRQPEIYGRDTLADVEAMCIEAGKQLGLTVEARQSNYEGELVTWIQQARDVFDGIVINPGAYSHTSIAILDALNAFEGKVVEVHISDIHAREEFRHHSYVSHRADHVIVGQGIKGYTMALDELANRLLA","length":146,"molWeight":16121,"crc64":"8FECB9C7719A42A3","md5":"C436C9832089B21CF46B239DE84BC474"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":2,"Binding site":5,"Site":1},"uniParcId":"UPI0036443852"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F8X2","uniProtkbId":"A0ABW3F8X2_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914919.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003738"}],"value":"Diaminopimelate decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"value":"DAP decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"value":"DAPDC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003738"}],"value":"4.1.1.20"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914919.1"}],"value":"lysA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914919.1"}],"value":"ACFQ14_00700"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"value":"Specifically catalyzes the decarboxylation of meso-diaminopimelate (meso-DAP) to L-lysine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"meso-2,6-diaminopimelate + H(+) = L-lysine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15101"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:32551"},{"database":"ChEBI","id":"CHEBI:57791"}],"ecNumber":"4.1.1.20","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003738"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001933"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600183-50"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003738"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003738"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"value":"Belongs to the Orn/Lys/Arg decarboxylase class-II family. LysA subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914919.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":374,"modifier":"EXACT"}},"description":"Orn/DAP/Arg decarboxylase 2 C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00278"}]},{"type":"Domain","location":{"start":{"value":35,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"Orn/DAP/Arg decarboxylase 2 N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02784"}]},{"type":"Active site","location":{"start":{"value":347,"modifier":"EXACT"},"end":{"value":347,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600183-50"}]},{"type":"Binding site","location":{"start":{"value":239,"modifier":"EXACT"},"end":{"value":239,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":278,"modifier":"EXACT"},"end":{"value":278,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":314,"modifier":"EXACT"},"end":{"value":314,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"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_02120"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":376,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"ligand":{"name":"substrate"}},{"type":"Modified residue","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600183-50"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003738"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02120"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0914919.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377210774.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0008836","properties":[{"key":"GoTerm","value":"F:diaminopimelate decarboxylase 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:0009085","properties":[{"key":"GoTerm","value":"P:L-lysine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06828","properties":[{"key":"EntryName","value":"PLPDE_III_DapDC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.10:FF:000003","properties":[{"key":"EntryName","value":"Diaminopimelate decarboxylase"},{"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_02120","properties":[{"key":"EntryName","value":"LysA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009006","properties":[{"key":"EntryName","value":"Ala_racemase/Decarboxylase_C"}]},{"database":"InterPro","id":"IPR002986","properties":[{"key":"EntryName","value":"DAP_deCOOHase_LysA"}]},{"database":"InterPro","id":"IPR022643","properties":[{"key":"EntryName","value":"De-COase2_C"}]},{"database":"InterPro","id":"IPR022657","properties":[{"key":"EntryName","value":"De-COase2_CS"}]},{"database":"InterPro","id":"IPR022644","properties":[{"key":"EntryName","value":"De-COase2_N"}]},{"database":"InterPro","id":"IPR022653","properties":[{"key":"EntryName","value":"De-COase2_pyr-phos_BS"}]},{"database":"InterPro","id":"IPR000183","properties":[{"key":"EntryName","value":"Orn/DAP/Arg_de-COase"}]},{"database":"InterPro","id":"IPR029066","properties":[{"key":"EntryName","value":"PLP-binding_barrel"}]},{"database":"NCBIfam","id":"TIGR01048","properties":[{"key":"EntryName","value":"lysA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43727","properties":[{"key":"EntryName","value":"DIAMINOPIMELATE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43727:SF2","properties":[{"key":"EntryName","value":"GROUP IV DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02784","properties":[{"key":"EntryName","value":"Orn_Arg_deC_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00278","properties":[{"key":"EntryName","value":"Orn_DAP_Arg_deC"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01181","properties":[{"key":"EntryName","value":"DAPDCRBXLASE"}]},{"database":"PRINTS","id":"PR01179","properties":[{"key":"EntryName","value":"ODADCRBXLASE"}]},{"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":"PS00878","properties":[{"key":"EntryName","value":"ODR_DC_2_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00879","properties":[{"key":"EntryName","value":"ODR_DC_2_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNHFDYRDGILHAENVSLPDIAAAVGTPFYCYSTATLERHYQVFAKAFDDVPSLVCYAMKANSNQAVLKTLARLGSGADVVSEGELRRAIAAGIPPKKIVFSGVGKTAREIDYALEADILCFNVESEPELEMLSARAMAMGKTAHVSFRINPDVDAKTHAKISTGKKEDKFGIPWKDATRVYARAAELGGVKVTGIDMHIGSQIIELAPFDDAFSRLTDLVAALRSEGHTIDHVDVGGGLGIPYHEDNNPPPNPDDYAAVVKKHVRDLDAMVMFEPGRLIAGNAGIFVTEVIYVKEGQDRFFVIIDGAMNDLIRPTLYDAHHEVRMVSATKGSNAPRITADIVGPVCESGDYLAKAREIPMPQAGDLLAFGSAGAYGAVQAGTYNTRLLVPEVLVNGDEFHVIRPRTSYEELIGLDSIPEWLAD","length":424,"molWeight":45987,"crc64":"820205CC96666E23","md5":"D9CB32ADEFE24CFE01DFF13E3CFE38A2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":8,"Modified residue":1},"uniParcId":"UPI003640D6FB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F8Y4","uniProtkbId":"A0ABW3F8Y4_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914911.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"value":"4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin)"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"value":"1.17.7.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"value":"1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914911.1"}],"value":"ispG"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914911.1"}],"value":"gcpE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914911.1"}],"value":"ACFQ14_00660"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"value":"Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + oxidized [flavodoxin] + H2O + 2 H(+) = 2-C-methyl-D-erythritol 2,4-cyclic diphosphate + reduced [flavodoxin]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43604"},{"database":"Rhea","id":"RHEA-COMP:10622"},{"database":"Rhea","id":"RHEA-COMP:10623"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57618"},{"database":"ChEBI","id":"CHEBI:58210"},{"database":"ChEBI","id":"CHEBI:58483"},{"database":"ChEBI","id":"CHEBI:128753"}],"ecNumber":"1.17.7.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"value":"Binds 1 [4Fe-4S] cluster."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"value":"Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 5/6"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"value":"Belongs to the IspG family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914911.1"}],"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":277,"modifier":"EXACT"}},"description":"IspG TIM-barrel","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04551"}]},{"type":"Domain","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"IspG C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF26540"}]},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":341,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023229"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"id":"KW-0414","category":"Biological process","name":"Isoprene biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00159"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0914911.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211323.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"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:0046429","properties":[{"key":"GoTerm","value":"F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity (ferredoxin)"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0141197","properties":[{"key":"GoTerm","value":"F:4-hydroxy-3-methylbut-2-enyl-diphosphate synthase activity (flavodoxin)"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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":"FunFam","id":"3.20.20.20:FF:000001","properties":[{"key":"EntryName","value":"4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.413.10:FF:000012","properties":[{"key":"EntryName","value":"4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.20","properties":[{"key":"EntryName","value":"Dihydropteroate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.413.10","properties":[{"key":"EntryName","value":"Sulfite Reductase Hemoprotein, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00159","properties":[{"key":"EntryName","value":"IspG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011005","properties":[{"key":"EntryName","value":"Dihydropteroate_synth-like_sf"}]},{"database":"InterPro","id":"IPR016425","properties":[{"key":"EntryName","value":"IspG_bac"}]},{"database":"InterPro","id":"IPR004588","properties":[{"key":"EntryName","value":"IspG_bac-typ"}]},{"database":"InterPro","id":"IPR058579","properties":[{"key":"EntryName","value":"IspG_C"}]},{"database":"InterPro","id":"IPR058578","properties":[{"key":"EntryName","value":"IspG_TIM"}]},{"database":"InterPro","id":"IPR045854","properties":[{"key":"EntryName","value":"NO2/SO3_Rdtase_4Fe4S_sf"}]},{"database":"NCBIfam","id":"NF001540","properties":[{"key":"EntryName","value":"ispG"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00612","properties":[{"key":"EntryName","value":"ispG_gcpE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30454","properties":[{"key":"EntryName","value":"4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30454:SF0","properties":[{"key":"EntryName","value":"4-HYDROXY-3-METHYLBUT-2-EN-1-YL DIPHOSPHATE SYNTHASE (FERREDOXIN), CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04551","properties":[{"key":"EntryName","value":"GcpE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF26540","properties":[{"key":"EntryName","value":"GcpE_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF004640","properties":[{"key":"EntryName","value":"IspG"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56014","properties":[{"key":"EntryName","value":"Nitrite and sulphite reductase 4Fe-4S domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGRQKTVGVSVGGVMVGGGAPIVVQSMTNTDTADIDKTVEQVAALHRAGSEIVRITVDRDESAAAVPKVRERLDRLGVDVPLVGDFHYIGHKLLTDHPACAEALAKYRINPGNVGFKAKKDKQFGEIIDIANRYNKPVRIGVNWGSLDQELLTRLMDENAASPDPASAEAVMREAIVQSALLSAAEAERLGMGRDKIILSAKVSDVQQLIAVYADLASRCDYALHLGLTEAGMGTKGIVSSSAALGILLQQGIGDTIRISLTPEPGGDRTREVQVAQELLQVMGFRAFIPVVAACPGCGRTTSTTFQELAAKIQGQLREAMPEWREKYPGVADLKVAVMGCIVNGPGESKHADIGISLPGTGETPAAPVFIDGKKAVTLRGEGIAEEFEALVHNYVETRFGGGAKSDAAE","length":410,"molWeight":43419,"crc64":"231BB7712939D486","md5":"63ECADA76BD6AD7EA891DC254B70B9CC"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Binding site":4},"uniParcId":"UPI00362ED44D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F935","uniProtkbId":"A0ABW3F935_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914979.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011895"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"value":"Hypoxanthine phosphoribosyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011895"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"value":"2.4.2.8"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914979.1"}],"value":"hpt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914979.1"}],"value":"ACFQ14_01005"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GMP + diphosphate = guanine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25424"},{"database":"ChEBI","id":"CHEBI:16235"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58115"}],"ecNumber":"2.4.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048811"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:25426"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048811"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"IMP + diphosphate = hypoxanthine + 5-phospho-alpha-D-ribose 1-diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17973"},{"database":"ChEBI","id":"CHEBI:17368"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58017"},{"database":"ChEBI","id":"CHEBI:58053"}],"ecNumber":"2.4.2.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049402"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:17975"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049402"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004669"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"value":"Purine metabolism; IMP biosynthesis via salvage pathway; IMP from hypoxanthine: step 1/1"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008391"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"value":"Belongs to the purine/pyrimidine phosphoribosyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0914979.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"Phosphoribosyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00156"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022726"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"id":"KW-0660","category":"Biological process","name":"Purine salvage"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU364099"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0914979.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377210831.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","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:0004422","properties":[{"key":"GoTerm","value":"F:hypoxanthine phosphoribosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032263","properties":[{"key":"GoTerm","value":"P:GMP salvage"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006178","properties":[{"key":"GoTerm","value":"P:guanine salvage"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046100","properties":[{"key":"GoTerm","value":"P:hypoxanthine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0032264","properties":[{"key":"GoTerm","value":"P:IMP salvage"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006166","properties":[{"key":"GoTerm","value":"P:purine ribonucleoside salvage"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06223","properties":[{"key":"EntryName","value":"PRTases_typeI"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2020","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050408","properties":[{"key":"EntryName","value":"HGPRT"}]},{"database":"InterPro","id":"IPR005904","properties":[{"key":"EntryName","value":"Hxn_phspho_trans"}]},{"database":"InterPro","id":"IPR029057","properties":[{"key":"EntryName","value":"PRTase-like"}]},{"database":"InterPro","id":"IPR000836","properties":[{"key":"EntryName","value":"PRTase_dom"}]},{"database":"NCBIfam","id":"TIGR01203","properties":[{"key":"EntryName","value":"HGPRTase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43340:SF1","properties":[{"key":"EntryName","value":"HYPOXANTHINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43340","properties":[{"key":"EntryName","value":"HYPOXANTHINE-GUANINE PHOSPHORIBOSYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00156","properties":[{"key":"EntryName","value":"Pribosyltran"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53271","properties":[{"key":"EntryName","value":"PRTase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MITVRGKKISTLFSANEIKQRNLEMAKEIGEHSHVNLVAIAVLKGSFVFAADLIRAMHETGLEPEVEFITLSSYGAGTVGGEVKILRDIDTHVNGRDVLLIDDILESGNTLAFARKLMLDRGANSVKVAVLLDKHSRRKAAVGADYVGFDCPDKFVVGYGMDVGHAFRELPFVGVVEGDA","length":180,"molWeight":19512,"crc64":"7503606531ABB1EF","md5":"E751CD1A7C5A4F4C3F617897C29AEC08"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI0036377515"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F9E1","uniProtkbId":"A0ABW3F9E1_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915081.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"Ubiquinone biosynthesis O-methyltransferase"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"2-polyprenyl-6-hydroxyphenol methylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"2.1.1.222"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"3-demethylubiquinone 3-O-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"2.1.1.64"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915081.1"}],"value":"ubiG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915081.1"}],"value":"ACFQ14_01520"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"O-methyltransferase that catalyzes the 2 O-methylation steps in the ubiquinone biosynthetic pathway"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-(all-trans-polyprenyl)benzene-1,2-diol + S-adenosyl-L-methionine = a 2-methoxy-6-(all-trans-polyprenyl)phenol + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31411"},{"database":"Rhea","id":"RHEA-COMP:9550"},{"database":"Rhea","id":"RHEA-COMP:9551"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:62729"},{"database":"ChEBI","id":"CHEBI:62731"}],"ecNumber":"2.1.1.222","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44380"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"Rhea","id":"RHEA-COMP:10914"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:84422"}],"ecNumber":"2.1.1.64","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"Cofactor biosynthesis; ubiquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"value":"Belongs to the methyltransferase superfamily. UbiG/COQ3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915081.1"}],"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":74,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"Methyltransferase type 11","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08241"}]},{"type":"Binding site","location":{"start":{"value":46,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":77,"modifier":"EXACT"},"end":{"value":77,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"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_00472"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022688"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00472"}],"id":"KW-0831","category":"Biological process","name":"Ubiquinone biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915081.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377210932.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0102208","properties":[{"key":"GoTerm","value":"F:2-polyprenyl-6-hydroxyphenol methylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0061542","properties":[{"key":"GoTerm","value":"F:3-demethylubiquinol 3-O-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010420","properties":[{"key":"GoTerm","value":"F:polyprenyldihydroxybenzoate methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00472","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013216","properties":[{"key":"EntryName","value":"Methyltransf_11"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR010233","properties":[{"key":"EntryName","value":"UbiG_MeTrfase"}]},{"database":"NCBIfam","id":"TIGR01983","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464","properties":[{"key":"EntryName","value":"METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464:SF19","properties":[{"key":"EntryName","value":"UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08241","properties":[{"key":"EntryName","value":"Methyltransf_11"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSEARAHTPPETTIDQAEVDRFSAMAAEWWNPTGKFKPLHKFNPVRLEYIREEVCARFGRDVRDHDALKGIRVLDIGCGGGLLCEPMARMGADVVGADASEFNIEVAKVHAEQSGVKVDYRATTAEALEAAGEKFDVVLNMEVVEHVSDVDFFLTSCCNMVKPNGLMFVATINRTLKARALAIFMAENVLRWLPKGTHEFDKLVKPEEIEAPVRAAGMEVIDRTGVFYNVLQDRWNKSSDMDVNYMMLTSRPPKK","length":255,"molWeight":28566,"crc64":"7CC9A1ABCE3A527B","md5":"8C8D6BA69E405C0344B8C8AA30362BFF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":4},"uniParcId":"UPI0036259E7C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F9Q8","uniProtkbId":"A0ABW3F9Q8_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915201.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"FMN dependent NADH:quinone oxidoreductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"1.6.5.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"Azo-dye reductase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"FMN-dependent NADH-azo compound oxidoreductase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"FMN-dependent NADH-azoreductase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"1.7.1.17"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"azoR"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915201.1"}],"value":"ACFQ14_02155"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"Also exhibits azoreductase activity. Catalyzes the reductive cleavage of the azo bond in aromatic azo compounds to the corresponding amines"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"Quinone reductase that provides resistance to thiol-specific stress caused by electrophilic quinones"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 a quinone + NADH + H(+) = 2 a 1,4-benzosemiquinone + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65952"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:132124"},{"database":"ChEBI","id":"CHEBI:134225"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N,N-dimethyl-1,4-phenylenediamine + anthranilate + 2 NAD(+) = 2-(4-dimethylaminophenyl)diazenylbenzoate + 2 NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:55872"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15783"},{"database":"ChEBI","id":"CHEBI:16567"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:71579"}],"ecNumber":"1.7.1.17","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048542"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:55874"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048542"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"FMN","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58210"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"Binds 1 FMN per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"Belongs to the azoreductase type 1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915201.1"}],"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":199,"modifier":"EXACT"}},"description":"Flavodoxin-like fold","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02525"}]},{"type":"Binding site","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":14,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58210"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"ligand":{"name":"FMN","id":"ChEBI:CHEBI:58210"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022643"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"id":"KW-0288","category":"Ligand","name":"FMN"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01216"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915201.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211051.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009055","properties":[{"key":"GoTerm","value":"F:electron transfer activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010181","properties":[{"key":"GoTerm","value":"F:FMN binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016652","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on NAD(P)H as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016655","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on NAD(P)H, quinone or similar compound as acceptor"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.360","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01216","properties":[{"key":"EntryName","value":"Azoreductase_type1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003680","properties":[{"key":"EntryName","value":"Flavodoxin_fold"}]},{"database":"InterPro","id":"IPR029039","properties":[{"key":"EntryName","value":"Flavoprotein-like_sf"}]},{"database":"InterPro","id":"IPR023048","properties":[{"key":"EntryName","value":"NADH:quinone_OxRdtase_FMN_depd"}]},{"database":"PANTHER","id":"PTHR43741","properties":[{"key":"EntryName","value":"FMN-DEPENDENT NADH-AZOREDUCTASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43741:SF4","properties":[{"key":"EntryName","value":"FMN-DEPENDENT NADH:QUINONE OXIDOREDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02525","properties":[{"key":"EntryName","value":"Flavodoxin_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52218","properties":[{"key":"EntryName","value":"Flavoproteins"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTPSAPTILRIDSSGRSKQSHSRPLADRMIKQLTTRFPDATVITRDLTSNVPPVVDEAWFEAAYTVEDERSDESNAALAISDEIVDEFMSADAIVITVPIYNFSVSAQLKLWIDQVARFGRTFTYTENGPQPLAPDRPTYLIVASGGTVIDSDIDFATGYMRHVLGFIGIKTVHVVEADQLMSKADEKLSAARAAIDRHATAFKMNGEVDRPEMA","length":215,"molWeight":23666,"crc64":"FBE466A9A33C6AF8","md5":"CFEA7F45FA6A38AA074B26C2CB879AA7"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":2},"uniParcId":"UPI003635CADF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F9U7","uniProtkbId":"A0ABW3F9U7_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915040.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Signal recognition particle receptor FtsY"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"SRP receptor"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"3.6.5.4"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915040.1"}],"value":"ftsY"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915040.1"}],"value":"ACFQ14_01315"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00053570"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Acts as a receptor for the complex formed by the signal recognition particle (SRP) and the ribosome-nascent chain (RNC). Interaction with SRP-RNC leads to the transfer of the RNC complex to the Sec translocase for insertion into the membrane, the hydrolysis of GTP by both Ffh and FtsY, and the dissociation of the SRP-FtsY complex into the individual components"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = GDP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19669"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58189"}],"ecNumber":"3.6.5.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY. SRP is a ribonucleoprotein composed of Ffh and a 4.5S RNA molecule"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004515"}],"value":"Cell inner membrane","id":"SL-0037"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004515"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004515"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"value":"Belongs to the GTP-binding SRP family. FtsY subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915040.1"}],"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":586,"modifier":"EXACT"},"end":{"value":599,"modifier":"EXACT"}},"description":"SRP54-type proteins GTP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00300"}]},{"type":"Region","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":40,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":53,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":119,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":419,"modifier":"EXACT"},"end":{"value":426,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":501,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":565,"modifier":"EXACT"},"end":{"value":568,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023170"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00920"}],"id":"KW-0675","category":"Molecular function","name":"Receptor"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915040.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377210891.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","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:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"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:0005047","properties":[{"key":"GoTerm","value":"F:signal recognition particle binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006614","properties":[{"key":"GoTerm","value":"P:SRP-dependent cotranslational protein targeting to membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"1.20.120.140:FF:000002","properties":[{"key":"EntryName","value":"Signal recognition particle receptor FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000053","properties":[{"key":"EntryName","value":"Signal recognition particle receptor FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.140","properties":[{"key":"EntryName","value":"Signal recognition particle SRP54, nucleotide-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00920","properties":[{"key":"EntryName","value":"FtsY"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR013822","properties":[{"key":"EntryName","value":"Signal_recog_particl_SRP54_hlx"}]},{"database":"InterPro","id":"IPR004390","properties":[{"key":"EntryName","value":"SR_rcpt_FtsY"}]},{"database":"InterPro","id":"IPR036225","properties":[{"key":"EntryName","value":"SRP/SRP_N"}]},{"database":"InterPro","id":"IPR000897","properties":[{"key":"EntryName","value":"SRP54_GTPase_dom"}]},{"database":"InterPro","id":"IPR042101","properties":[{"key":"EntryName","value":"SRP54_N_sf"}]},{"database":"NCBIfam","id":"TIGR00064","properties":[{"key":"EntryName","value":"ftsY"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43134","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43134:SF1","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE RECEPTOR SUBUNIT ALPHA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00448","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02881","properties":[{"key":"EntryName","value":"SRP54_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00962","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00963","properties":[{"key":"EntryName","value":"SRP54_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47364","properties":[{"key":"EntryName","value":"Domain of the SRP/SRP receptor G-proteins"},{"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":"PS00300","properties":[{"key":"EntryName","value":"SRP54"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAGFLKRLFKFGKKKKEDEEPPLQEVEDATSDTALAPAPNEPVVAHAEAASTVITDEEAGADLTGDAGITPIKDVPGPDEVAAEAERLAKLKAEREAAEAQALEAERIAQEELAAQEAAAEKAAAEADERAKEEAERLAVKKAEAEKLEAKRVAEEKAAEEKAAKAKAEQEKAEKDAAKEKAEKEKADEAERLERAQAKKEEAAKRTAEEKLSEEKRAEEARKAEEEKLAQEAERAEQARLAEEAAQAKRAEEERLAAELAEAERAENERLAAEAEDAAVSEPEPEPEPEPEPEPEPEPVAASTGDEPAPKKTWFKRLKDGLTRSSSSLTENITAVFTKRKLDEDTLQELEDILIQADLGVETAMNVTDKLASQRMGKDVSDEEVREFMAAEIETVLTPVAAELELDLDHTPHVILVVGVNGSGKTTTIGKLSQKLYDAGFSTLLVAGDTFRAAAIEQLKIWGERTQSPVVSRPLGSDAAGLAFDAYDQAREEGRDVMLMDTAGRLQNKKELMDELEKIIRVLRKQDPTAPHTVLLTLDATTGQNAVNQVDIFKDVAGVNGLVMTKLDGTARGGILVAISAKHQLPVYFLGVGESVDDLEPFEARDFARSIAGLS","length":615,"molWeight":66655,"crc64":"C069E22E26AF5C52","md5":"A8C04E0C65C3CBCA0686FD3F189D0FDA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Compositional bias":3,"Binding site":3},"uniParcId":"UPI0036392D44"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3F9X6","uniProtkbId":"A0ABW3F9X6_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915264.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013152"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00232"}],"value":"Transketolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013152"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR00232"}],"value":"2.2.1.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915264.1"}],"value":"tkt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915264.1"}],"value":"ACFQ14_02480"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00096212"}],"value":"Catalyzes the transfer of a two-carbon ketol group from a ketose donor to an aldose acceptor, via a covalent intermediate with the cofactor thiamine pyrophosphate. Thus, catalyzes the reversible transfer of a two-carbon ketol group from sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate, producing xylulose-5-phosphate and ribose-5-phosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10508"},{"database":"ChEBI","id":"CHEBI:57483"},{"database":"ChEBI","id":"CHEBI:57737"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"2.2.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049473"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001913"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001941"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}},{"name":"Co(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:48828"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"value":"Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"value":"Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent metal cations, such as Ca(2+), Mn(2+) and Co(2+)."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"value":"Binds 1 thiamine pyrophosphate per subunit. During the reaction, the substrate forms a covalent intermediate with the cofactor."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005215"}],"value":"Carbohydrate biosynthesis; Calvin cycle"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004959"}],"value":"Carbohydrate degradation; pentose phosphate pathway"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007131"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"value":"Belongs to the transketolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915264.1"}],"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":352,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"Transketolase-like pyrimidine-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00861"}]},{"type":"Region","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":409,"modifier":"EXACT"},"end":{"value":409,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-1"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":157,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":355,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":435,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58937"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"ligand":{"name":"thiamine diphosphate","id":"ChEBI:CHEBI:58937"}},{"type":"Binding site","location":{"start":{"value":459,"modifier":"EXACT"},"end":{"value":459,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":467,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":471,"modifier":"EXACT"},"end":{"value":471,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Binding site","location":{"start":{"value":518,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:78346"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-2"}],"ligand":{"name":"D-ribose 5-phosphate","id":"ChEBI:CHEBI:78346","label":"(ligand shared between dimeric partners)"}},{"type":"Site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-5"}]},{"type":"Site","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":260,"modifier":"EXACT"}},"description":"Important for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-5"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-4"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR605478-3"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004996"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915264.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211114.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","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:0004802","properties":[{"key":"GoTerm","value":"F:transketolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006098","properties":[{"key":"GoTerm","value":"P:pentose-phosphate shunt"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd07033","properties":[{"key":"EntryName","value":"TPP_PYR_DXS_TK_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02012","properties":[{"key":"EntryName","value":"TPP_TK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000003","properties":[{"key":"EntryName","value":"Transketolase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000004","properties":[{"key":"EntryName","value":"Transketolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.920","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR009014","properties":[{"key":"EntryName","value":"Transketo_C/PFOR_II"}]},{"database":"InterPro","id":"IPR055152","properties":[{"key":"EntryName","value":"Transketolase-like_C_2"}]},{"database":"InterPro","id":"IPR005475","properties":[{"key":"EntryName","value":"Transketolase-like_Pyr-bd"}]},{"database":"InterPro","id":"IPR005478","properties":[{"key":"EntryName","value":"Transketolase_bac-like"}]},{"database":"InterPro","id":"IPR020826","properties":[{"key":"EntryName","value":"Transketolase_BS"}]},{"database":"InterPro","id":"IPR049557","properties":[{"key":"EntryName","value":"Transketolase_CS"}]},{"database":"InterPro","id":"IPR033247","properties":[{"key":"EntryName","value":"Transketolase_fam"}]},{"database":"InterPro","id":"IPR005474","properties":[{"key":"EntryName","value":"Transketolase_N"}]},{"database":"NCBIfam","id":"TIGR00232","properties":[{"key":"EntryName","value":"tktlase_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43522","properties":[{"key":"EntryName","value":"TRANSKETOLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43522:SF2","properties":[{"key":"EntryName","value":"TRANSKETOLASE 1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02779","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22613","properties":[{"key":"EntryName","value":"Transketolase_C_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00456","properties":[{"key":"EntryName","value":"Transketolase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00861","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52922","properties":[{"key":"EntryName","value":"TK C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00801","properties":[{"key":"EntryName","value":"TRANSKETOLASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00802","properties":[{"key":"EntryName","value":"TRANSKETOLASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTSESKHAGMANAIRFLSADAVQAANSGHPGLPMGAADIATVLFTQHMKFDPKNPNWPDRDRFVLSAGHGSMLLYSSLFLLGYEDIDMDQIRNFRQIGSKTAGHPEYGHAAGIETTTGPLGQGIANAVGMAMAERKLADEFGADIVDHHTYCLVGDGCLMEGISQEAITLAGHLKLNKLIVIWDNNNISIDGPISVSDSTDQIMRFKSCQWNTIEVDGHDPEDISAALEQAKKSDKPTMIAAKTIIGFGAPTKAGTKDAHGAPLGNEEIKIARETLGWDAEPFTLPADICDAWRIAGLRSAQAHKEWQKRLETSDSTLRGEFERRQRGELPAGFGDAIAAYKKELADEQPKKATRKASQAALEVINGVVPETIGGSADLTGSNNTNTSQTPPITPDDFSGRFVHYGIREHAMAAAMNGIALHGGLIPYSGGFLIFSDYCRPSIRLAALMEIRVVHVLTHDSIGLGEDGPTHQPVEQLAALRSIPNLNVFRPADVTETAECWQLALEAEKTPSAIALTRQDLPSVRATFEAENLCARGAYELAAAEDEAQVSIFASGSEVELALEAKEKLDSAGVPTRVVSVPCFELFETQSGEYRAATLGDAPIRVGVEAAVRQGWDAIIGSDGIFIGMDSFGASGPYKELYEHFGITADALVDAVQARLQA","length":662,"molWeight":71021,"crc64":"74A4B3F3155CE54F","md5":"9448796E7D917B8A11CBD6409D6F0FA1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":6,"PATHWAY":2,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":17,"Site":2},"uniParcId":"UPI00363F19A6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FA69","uniProtkbId":"A0ABW3FA69_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915354.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000607"}],"value":"Ferrochelatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000607"}],"value":"4.98.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"value":"Heme synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"value":"Protoheme ferro-lyase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915354.1"}],"value":"hemH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915354.1"}],"value":"ACFQ14_02930"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000607"}],"value":"Catalyzes the ferrous insertion into protoporphyrin IX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Fe-coproporphyrin III + 2 H(+) = coproporphyrin III + Fe(2+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:49572"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:68438"},{"database":"ChEBI","id":"CHEBI:131725"}],"ecNumber":"4.99.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024536"}]},"physiologicalReactions":[{"directionType":"right-to-left","reactionCrossReference":{"database":"Rhea","id":"RHEA:49574"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024536"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"heme b + 2 H(+) = protoporphyrin IX + Fe(2+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22584"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29033"},{"database":"ChEBI","id":"CHEBI:57306"},{"database":"ChEBI","id":"CHEBI:60344"}],"ecNumber":"4.98.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000607"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000607"}],"value":"Porphyrin-containing compound metabolism; protoheme biosynthesis; protoheme from protoporphyrin-IX: step 1/1"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000607"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007718"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000607"}],"value":"Belongs to the ferrochelatase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915354.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":261,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}},{"type":"Binding site","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29033"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"ligand":{"name":"Fe(2+)","id":"ChEBI:CHEBI:29033"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023133"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"id":"KW-0350","category":"Biological process","name":"Heme biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00323"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915354.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211200.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","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:0004325","properties":[{"key":"GoTerm","value":"F:protoporphyrin ferrochelatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00419","properties":[{"key":"EntryName","value":"Ferrochelatase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03411","properties":[{"key":"EntryName","value":"Ferrochelatase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1400:FF:000002","properties":[{"key":"EntryName","value":"Ferrochelatase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1400","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00323","properties":[{"key":"EntryName","value":"Ferrochelatase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001015","properties":[{"key":"EntryName","value":"Ferrochelatase"}]},{"database":"InterPro","id":"IPR019772","properties":[{"key":"EntryName","value":"Ferrochelatase_AS"}]},{"database":"InterPro","id":"IPR033644","properties":[{"key":"EntryName","value":"Ferrochelatase_C"}]},{"database":"InterPro","id":"IPR033659","properties":[{"key":"EntryName","value":"Ferrochelatase_N"}]},{"database":"NCBIfam","id":"TIGR00109","properties":[{"key":"EntryName","value":"hemH"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11108","properties":[{"key":"EntryName","value":"FERROCHELATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11108:SF1","properties":[{"key":"EntryName","value":"FERROCHELATASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00762","properties":[{"key":"EntryName","value":"Ferrochelatase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53800","properties":[{"key":"EntryName","value":"Chelatase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00534","properties":[{"key":"EntryName","value":"FERROCHELATASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNQAVKTKASKADAPAAKSGPAPKAKAKKTVVPKPAPAKTSGSLAFSRDVSAEHFPPEHPKVAFGKIGVLLVNLGTPDGHDKKNMRKYLKEFLSDRRVIETPRVIWWPLLNGIILNVRPKKSGALYASIWNEEMDESPLRTFTRSQSDQLAERMSKHTDIVFDWGMRYGNPSIESRMKALQDAGCERILVFPLYPQYSAATTATVNDKTFESLMKMRWMPALRTVPPYHDDPAYIEALAKSIQKHLDGLDFEPEHIVASYHGIPKSYFRKGDPYHCHCLKTSRLLKEHMGWEDGFLISTFQSRFGPEEWLQPYTDKTVEQLAKDGIKRICVVNPGFSSDCLETLEEIAGEVCEEFEDNGGEQFSHIPCLNDGPEGMDLIEQIVRRELQGWI","length":391,"molWeight":44133,"crc64":"E0F653085A1DDAEA","md5":"1766B9EFB534585CB8784F22DA46F734"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Binding site":2},"uniParcId":"UPI0036292FD7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FAC0","uniProtkbId":"A0ABW3FAC0_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915411.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365040"}],"value":"Glutathione reductase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365040"}],"value":"GRase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365040"}],"value":"1.8.1.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915411.1"}],"value":"gor"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915411.1"}],"value":"ACFQ14_03225"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365040"}],"value":"Catalyzes the reduction of glutathione disulfide (GSSG) to reduced glutathione (GSH)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 glutathione + NADP(+) = glutathione disulfide + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11740"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57925"},{"database":"ChEBI","id":"CHEBI:58297"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.8.1.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049142"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365040"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"value":"Binds 1 FAD per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007532"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"value":"Belongs to the class-I pyridine nucleotide-disulfide oxidoreductase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915411.1"}],"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":5,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"FAD/NAD(P)-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07992"}]},{"type":"Domain","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Pyridine nucleotide-disulphide oxidoreductase dimerisation","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02852"}]},{"type":"Active site","location":{"start":{"value":438,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-2"}]},{"type":"Binding site","location":{"start":{"value":51,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57692"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"FAD","id":"ChEBI:CHEBI:57692"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Disulfide bond","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":47,"modifier":"EXACT"}},"description":"Redox-active","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-4"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023157"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU365040"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000350-3"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023284"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003691"}],"id":"KW-0676","category":"Domain","name":"Redox-active center"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915411.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211255.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","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:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004362","properties":[{"key":"GoTerm","value":"F:glutathione-disulfide reductase (NADPH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0045454","properties":[{"key":"GoTerm","value":"P:cell redox homeostasis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0034599","properties":[{"key":"GoTerm","value":"P:cellular response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006749","properties":[{"key":"GoTerm","value":"P:glutathione metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.50.50.60:FF:000051","properties":[{"key":"EntryName","value":"Glutathione reductase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.390.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR023753","properties":[{"key":"EntryName","value":"FAD/NAD-binding_dom"}]},{"database":"InterPro","id":"IPR016156","properties":[{"key":"EntryName","value":"FAD/NAD-linked_Rdtase_dimer_sf"}]},{"database":"InterPro","id":"IPR006324","properties":[{"key":"EntryName","value":"GSHR"}]},{"database":"InterPro","id":"IPR046952","properties":[{"key":"EntryName","value":"GSHR/TRXR-like"}]},{"database":"InterPro","id":"IPR001100","properties":[{"key":"EntryName","value":"Pyr_nuc-diS_OxRdtase"}]},{"database":"InterPro","id":"IPR004099","properties":[{"key":"EntryName","value":"Pyr_nucl-diS_OxRdtase_dimer"}]},{"database":"InterPro","id":"IPR012999","properties":[{"key":"EntryName","value":"Pyr_OxRdtase_I_AS"}]},{"database":"NCBIfam","id":"TIGR01424","properties":[{"key":"EntryName","value":"gluta_reduc_2"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004776","properties":[{"key":"EntryName","value":"gorA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42737","properties":[{"key":"EntryName","value":"GLUTATHIONE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42737:SF2","properties":[{"key":"EntryName","value":"GLUTATHIONE REDUCTASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07992","properties":[{"key":"EntryName","value":"Pyr_redox_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02852","properties":[{"key":"EntryName","value":"Pyr_redox_dim"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000350","properties":[{"key":"EntryName","value":"Mercury_reductase_MerA"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00368","properties":[{"key":"EntryName","value":"FADPNR"}]},{"database":"PRINTS","id":"PR00411","properties":[{"key":"EntryName","value":"PNDRDTASEI"}]},{"database":"SUPFAM","id":"SSF51905","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55424","properties":[{"key":"EntryName","value":"FAD/NAD-linked reductases, dimerisation (C-terminal) domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00076","properties":[{"key":"EntryName","value":"PYRIDINE_REDOX_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNYDYDLFVIGGGSGGVRAANRTAALGHRVAIAEESRYGGTCVIRGCVPKKLYVYASTFHEHFEDAAGYGWTVGDTKFDWDKLVASKEAEITRLEGLYKKGLMSNSVELFDSRAELRGQHEIWLKSEDRVVTADKVLIAVGGTPNPHADLEGHEHAIVSDQAFDLSALPESIIIAGAGYIAIEFAGIFNGLGVDTTILYRGQEILSGFDDDVRELLHEEYEKRGIKIITQQVFSKIERLENGKRKATLSDGSAIEVDQVMFALGRVPQTDSLGLENAGVKTDECGYIPVDGYSKTNIANIWAVGDVTDRVQLTPVAIHESMCFVSTEFKGNPQEPNHDNIATAVFSHPEIGTVGMTEHDAARKYEKLNIFKTTFRPMKYTLAKRDSKMLMKLIVDAQTDRLVGAHILGPDAGEMAQLIAVPMKMGCTKQDFDDTMALHPSAAEELVTMYEPSYSVKSGVRVQ","length":462,"molWeight":50766,"crc64":"AF08212223ACCB7B","md5":"638065079AD5F4DE31D395AB23DFED3D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":4,"Disulfide bond":1},"uniParcId":"UPI00362EC676"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FAF2","uniProtkbId":"A0ABW3FAF2_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915441.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Bifunctional protein PutA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Proline dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"1.5.5.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Proline oxidase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"1-pyrroline-5-carboxylate dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"P5C dehydrogenase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"1.2.1.88"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"L-glutamate gamma-semialdehyde dehydrogenase"}}]}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915441.1"}],"value":"ACFQ14_03375"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Oxidizes proline to glutamate for use as a carbon and nitrogen source"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamate 5-semialdehyde + NAD(+) + H2O = L-glutamate + NADH + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30235"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:58066"}],"ecNumber":"1.2.1.88","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048142"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-proline + a quinone = (S)-1-pyrroline-5-carboxylate + a quinol + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23784"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17388"},{"database":"ChEBI","id":"CHEBI:24646"},{"database":"ChEBI","id":"CHEBI:60039"},{"database":"ChEBI","id":"CHEBI:132124"}],"ecNumber":"1.5.5.2","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004786"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"Amino-acid degradation; L-proline degradation into L-glutamate; L-glutamate from L-proline: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"In the C-terminal section; belongs to the aldehyde dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"value":"In the N-terminal section; belongs to the proline dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915441.1"}],"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":59,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Proline dehydrogenase PutA","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14850"}]},{"type":"Domain","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":472,"modifier":"EXACT"}},"description":"Proline dehydrogenase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01619"}]},{"type":"Domain","location":{"start":{"value":539,"modifier":"EXACT"},"end":{"value":977,"modifier":"EXACT"}},"description":"Aldehyde dehydrogenase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00171"}]},{"type":"Active site","location":{"start":{"value":756,"modifier":"EXACT"},"end":{"value":756,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000197-1"}]},{"type":"Active site","location":{"start":{"value":790,"modifier":"EXACT"},"end":{"value":790,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000197-1"}]},{"type":"Active site","location":{"start":{"value":790,"modifier":"EXACT"},"end":{"value":790,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10008"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023062"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000197"}],"id":"KW-0642","category":"Biological process","name":"Proline metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915441.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211283.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0009898","properties":[{"key":"GoTerm","value":"C:cytoplasmic side of plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003700","properties":[{"key":"GoTerm","value":"F:DNA-binding transcription factor activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003842","properties":[{"key":"GoTerm","value":"F:L-glutamate gamma-semialdehyde dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004657","properties":[{"key":"GoTerm","value":"F:proline dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0055129","properties":[{"key":"GoTerm","value":"P:L-proline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006562","properties":[{"key":"GoTerm","value":"P:L-proline catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd07125","properties":[{"key":"EntryName","value":"ALDH_PutA-P5CDH"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.309.10:FF:000005","properties":[{"key":"EntryName","value":"1-pyrroline-5-carboxylate dehydrogenase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.220","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.605.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.309.10","properties":[{"key":"EntryName","value":"Aldehyde Dehydrogenase, Chain A, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.460","properties":[{"key":"EntryName","value":"Single helix bin"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016161","properties":[{"key":"EntryName","value":"Ald_DH/histidinol_DH"}]},{"database":"InterPro","id":"IPR016163","properties":[{"key":"EntryName","value":"Ald_DH_C"}]},{"database":"InterPro","id":"IPR016160","properties":[{"key":"EntryName","value":"Ald_DH_CS_CYS"}]},{"database":"InterPro","id":"IPR016162","properties":[{"key":"EntryName","value":"Ald_DH_N"}]},{"database":"InterPro","id":"IPR015590","properties":[{"key":"EntryName","value":"Aldehyde_DH_dom"}]},{"database":"InterPro","id":"IPR025703","properties":[{"key":"EntryName","value":"Bifunct_PutA"}]},{"database":"InterPro","id":"IPR029041","properties":[{"key":"EntryName","value":"FAD-linked_oxidoreductase-like"}]},{"database":"InterPro","id":"IPR024089","properties":[{"key":"EntryName","value":"PRODH_PutA_dom_I/II"}]},{"database":"InterPro","id":"IPR024082","properties":[{"key":"EntryName","value":"PRODH_PutA_dom_II"}]},{"database":"InterPro","id":"IPR002872","properties":[{"key":"EntryName","value":"Proline_DH_dom"}]},{"database":"InterPro","id":"IPR050485","properties":[{"key":"EntryName","value":"Proline_metab_enzyme"}]},{"database":"InterPro","id":"IPR005933","properties":[{"key":"EntryName","value":"PutA_C"}]},{"database":"NCBIfam","id":"TIGR01238","properties":[{"key":"EntryName","value":"D1pyr5carbox3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42862","properties":[{"key":"EntryName","value":"DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 1, ISOFORM A-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42862:SF1","properties":[{"key":"EntryName","value":"DELTA-1-PYRROLINE-5-CARBOXYLATE DEHYDROGENASE 2, ISOFORM A-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00171","properties":[{"key":"EntryName","value":"Aldedh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01619","properties":[{"key":"EntryName","value":"Pro_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14850","properties":[{"key":"EntryName","value":"Pro_dh-DNA_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000197","properties":[{"key":"EntryName","value":"Bifunct_PutA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53720","properties":[{"key":"EntryName","value":"ALDH-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51730","properties":[{"key":"EntryName","value":"FAD-linked oxidoreductase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81935","properties":[{"key":"EntryName","value":"N-terminal domain of bifunctional PutA protein"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00070","properties":[{"key":"EntryName","value":"ALDEHYDE_DEHYDR_CYS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTNFLAPFAAAYAPADEAVLPDLLQRIARDGVAQKQIDDKARSLIEGIRERAGSVGGMEDFLRDYGLSTKEGLALMVMAEALLRVPDAATQDALIADKITAGNWEDTEGADTWFVSAATWGLGLSSKIVRPDDSPSGLLSHLTKRIGGPAVRQGVRQSMRYLGHQFVLGQTIEEGLKRAGAQEAKGYRYSYDMLGEGARTWDDAKRYAASYADAIEEIGRKAGNKPLPDRPGISIKLSALHPRYTARNRDAVLRELVPEVLKLVQSAKSFDLNLTIDAEEADRLELSLDVIDAVFSDPSLRGWDGFGLAIQAYQKRAIAVIDWVADLCRKNDGRMMVRLVKGAYWDSEVKHAQVEGAADFPVFTRKAATDVSYTACARQMLLHRDVLYPQFATHNALTVATILAFAGDGEKGGYEFQRLHGMGEELFEQITEGRDGVPCRIYAPVGHHRDLLAYLVRRLLENGANSSFVAQVGDKDVPIDDLLTSPASWLDDGAYRHPDIQLPRRLYAPRKNSRGIEFGSRVELKHTLDGMAAASLSGSLEAFGAEDVEACMAKAQAAFPAWRGRDVKERASILERAADLLESDTTRIMGVLAKEAGKTVDDGIAEVREAVDFLRYYAAEARRIMVPRMLPGPVGEDNAYSLTGRGVVVTIAPWNFPLAIFLGQVSAALAAGNAVVAKPAPQTPIIAAEALALLHKAGVPKDALILAPGGAETGQALVGDPRVAAIAFTGSTATAKAINLQLAQKPGAIIPFIAETGGTNAMIADATALPEQVTDDVILSAFRSAGQRCSACRILYVQEDVAERMLTMIQGSAATLEMGDPMLPQTDIGPVIDADALSRLRDYVVEKKDQIVWQGKAPEGGLFMAPTIIRLRDDEVLDREIFGPVLHVKTYKAGKLDAVIDEINSTGFGLTFALHSRIQAVIDHVTARVGAGNVYVNRNQIGAIVESQPFGGQGLSGTGPKAGGPLYLTRFVQERVVSTDTTAAGGNASLIALEDH","length":997,"molWeight":107347,"crc64":"0CC6B0F9B2097592","md5":"BC1C50D4937C782B7A952F9BAA711C59"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":3,"Active site":3},"uniParcId":"UPI0036443C30"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FAG4","uniProtkbId":"A0ABW3FAG4_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915407.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00016181"}],"value":"Beta-ketoadipyl-CoA thiolase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012233"}],"value":"2.3.1.174"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041222"}],"value":"3-oxoadipyl-CoA thiolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00080155"}],"value":"Beta-ketothiolase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915407.1"}],"value":"pcaF"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915407.1"}],"value":"ACFQ14_03205"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003720"}],"value":"Catalyzes thiolytic cleavage of beta-ketoadipyl-CoA to succinyl-CoA and acetyl-CoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"succinyl-CoA + acetyl-CoA = 3-oxoadipyl-CoA + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19481"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57292"},{"database":"ChEBI","id":"CHEBI:57348"}],"ecNumber":"2.3.1.174","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048527"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005071"}],"value":"Aromatic compound metabolism; beta-ketoadipate pathway; acetyl-CoA and succinyl-CoA from 3-oxoadipate: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004683"}],"value":"Biopolymer metabolism; poly-(R)-3-hydroxybutanoate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00037924"}],"value":"Metabolic intermediate biosynthesis; (R)-mevalonate biosynthesis; (R)-mevalonate from acetyl-CoA: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010982"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003557"}],"value":"Belongs to the thiolase-like superfamily. Thiolase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915407.1"}],"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":5,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Thiolase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00108"}]},{"type":"Domain","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":399,"modifier":"EXACT"}},"description":"Thiolase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02803"}]},{"type":"Active site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000429-1"}]},{"type":"Active site","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000429-1"}]},{"type":"Active site","location":{"start":{"value":386,"modifier":"EXACT"},"end":{"value":386,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000429-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003557"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022797"}],"id":"KW-0058","category":"Biological process","name":"Aromatic hydrocarbons catabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022752"}],"id":"KW-0583","category":"Biological process","name":"PHB biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003557"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915407.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211251.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0033812","properties":[{"key":"GoTerm","value":"F:3-oxoadipyl-CoA thiolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0019619","properties":[{"key":"GoTerm","value":"P:3,4-dihydroxybenzoate catabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006629","properties":[{"key":"GoTerm","value":"P:lipid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00751","properties":[{"key":"EntryName","value":"thiolase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.47.10:FF:000010","properties":[{"key":"EntryName","value":"Acetyl-CoA acetyltransferase (Thiolase)"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.47.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR012793","properties":[{"key":"EntryName","value":"PcaF"}]},{"database":"InterPro","id":"IPR002155","properties":[{"key":"EntryName","value":"Thiolase"}]},{"database":"InterPro","id":"IPR016039","properties":[{"key":"EntryName","value":"Thiolase-like"}]},{"database":"InterPro","id":"IPR020615","properties":[{"key":"EntryName","value":"Thiolase_acyl_enz_int_AS"}]},{"database":"InterPro","id":"IPR020617","properties":[{"key":"EntryName","value":"Thiolase_C"}]},{"database":"InterPro","id":"IPR020613","properties":[{"key":"EntryName","value":"Thiolase_CS"}]},{"database":"InterPro","id":"IPR020616","properties":[{"key":"EntryName","value":"Thiolase_N"}]},{"database":"NCBIfam","id":"TIGR01930","properties":[{"key":"EntryName","value":"AcCoA-C-Actrans"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02430","properties":[{"key":"EntryName","value":"pcaF"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006551","properties":[{"key":"EntryName","value":"PRK09050.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR18919:SF107","properties":[{"key":"EntryName","value":"ACETYL-COA ACETYLTRANSFERASE, CYTOSOLIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR18919","properties":[{"key":"EntryName","value":"ACETYL-COA C-ACYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02803","properties":[{"key":"EntryName","value":"Thiolase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00108","properties":[{"key":"EntryName","value":"Thiolase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000429","properties":[{"key":"EntryName","value":"Ac-CoA_Ac_transf"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53901","properties":[{"key":"EntryName","value":"Thiolase-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00098","properties":[{"key":"EntryName","value":"THIOLASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00737","properties":[{"key":"EntryName","value":"THIOLASE_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPEAYICAYTRTPIGRFGGALSSVRADDLGALPIKSLMEKHRQVDWEGIDEVIYGCANQAGEDNRNVARMSALLANLPKTVPGTTINRLCGSGMDAVIIAARGIKSGEIDIAIAGGVESMSRAPFVMPKADAAFSRVTEIHDTTIGWRFINPVMKTQYGVDSMPETGENVAEDFNVTREDQDLFALRSQQAAKKAQSSGRLAKEITPVSIDQRRGDPVVFDKDEHLRDTTIEKLAALKAPFRKGGSVTAGNASGVNDGAAALIIASENAAARHGLTPIARILGAATAGVPPRIMGIGPAPASNKLMARLGMTQEQFGVIELNEAFASQALATLRELGIADDDPRINRNGGAIALGHPLGMSGARITGTAAVELSETSAQYSLSAMCIGVGQGIAIALERV","length":400,"molWeight":42063,"crc64":"BAF7C5D96414B112","md5":"566771997A3B9AA6A4FF0D3C679F0187"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":3,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":3},"uniParcId":"UPI00363A4393"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FAJ2","uniProtkbId":"A0ABW3FAJ2_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915474.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"Glutathione hydrolase proenzyme"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"2.3.2.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"3.4.19.13"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"Glutathione hydrolase large chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"Glutathione hydrolase small chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915474.1"}],"value":"ggt"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915474.1"}],"value":"ACFQ14_03540"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an N-terminal (5-L-glutamyl)-[peptide] + an alpha-amino acid = 5-L-glutamyl amino acid + an N-terminal L-alpha-aminoacyl-[peptide]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23904"},{"database":"Rhea","id":"RHEA-COMP:9780"},{"database":"Rhea","id":"RHEA-COMP:9795"},{"database":"ChEBI","id":"CHEBI:77644"},{"database":"ChEBI","id":"CHEBI:78597"},{"database":"ChEBI","id":"CHEBI:78599"},{"database":"ChEBI","id":"CHEBI:78608"}],"ecNumber":"2.3.2.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047417"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an S-substituted glutathione + H2O = an S-substituted L-cysteinylglycine + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:59468"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:90779"},{"database":"ChEBI","id":"CHEBI:143103"}],"ecNumber":"3.4.19.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001049"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glutathione + H2O = L-cysteinylglycine + L-glutamate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28807"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:57925"},{"database":"ChEBI","id":"CHEBI:61694"}],"ecNumber":"3.4.19.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001089"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"Sulfur metabolism; glutathione metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"This enzyme consists of two polypeptide chains, which are synthesized in precursor form from a single polypeptide"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"Cleaved by autocatalysis into a large and a small subunit"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009381"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"value":"Belongs to the gamma-glutamyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915474.1"}],"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":26,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}]},{"type":"Chain","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":590,"modifier":"EXACT"}},"description":"Glutathione hydrolase proenzyme","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"featureId":"PRO_5046400543"},{"type":"Region","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":479,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":411,"modifier":"EXACT"},"end":{"value":411,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600101-1"}]},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29985"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600101-2"}],"ligand":{"name":"L-glutamate","id":"ChEBI:CHEBI:29985"}},{"type":"Binding site","location":{"start":{"value":451,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29985"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600101-2"}],"ligand":{"name":"L-glutamate","id":"ChEBI:CHEBI:29985"}},{"type":"Binding site","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29985"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600101-2"}],"ligand":{"name":"L-glutamate","id":"ChEBI:CHEBI:29985"}},{"type":"Binding site","location":{"start":{"value":497,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29985"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600101-2"}],"ligand":{"name":"L-glutamate","id":"ChEBI:CHEBI:29985"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"id":"KW-0317","category":"Biological process","name":"Glutathione biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"SignalP"}],"id":"KW-0732","category":"Domain","name":"Signal"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU368036"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915474.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211315.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0036374","properties":[{"key":"GoTerm","value":"F:glutathione gamma-glutamate hydrolase"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006751","properties":[{"key":"GoTerm","value":"P:glutathione catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.10.246.130","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.20.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR051792","properties":[{"key":"EntryName","value":"GGT_bact"}]},{"database":"InterPro","id":"IPR055262","properties":[{"key":"EntryName","value":"GGT_CS"}]},{"database":"InterPro","id":"IPR043138","properties":[{"key":"EntryName","value":"GGT_lsub"}]},{"database":"InterPro","id":"IPR000101","properties":[{"key":"EntryName","value":"GGT_peptidase"}]},{"database":"InterPro","id":"IPR043137","properties":[{"key":"EntryName","value":"GGT_ssub_C"}]},{"database":"InterPro","id":"IPR029055","properties":[{"key":"EntryName","value":"Ntn_hydrolases_N"}]},{"database":"NCBIfam","id":"TIGR00066","properties":[{"key":"EntryName","value":"g_glut_trans"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43199","properties":[{"key":"EntryName","value":"GLUTATHIONE HYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43199:SF1","properties":[{"key":"EntryName","value":"GLUTATHIONE HYDROLASE PROENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01019","properties":[{"key":"EntryName","value":"G_glu_transpept"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01210","properties":[{"key":"EntryName","value":"GGTRANSPTASE"}]},{"database":"SUPFAM","id":"SSF56235","properties":[{"key":"EntryName","value":"N-terminal nucleophile aminohydrolases (Ntn hydrolases)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00462","properties":[{"key":"EntryName","value":"G_GLU_TRANSPEPTIDASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDSRKVFRATIVLTAILALSSPLFAQQAADEVAPEATTSLAAKRAIQPVKSKSWMVSVANPYAANAAANVLAKGGSAADAAIAAQLVLGLIEPQSSGLGGGAFVVHYNATTQRLTTLDGRETAPLAADSNLFLSADGEPLKFFDAVIGGRSVGTPGTPALLDTMHSKWGELEWSALFDDAIPLAENGFIVSSRLSGLIERNAESLARHAPSAAYFLPNGQPLKMGVRLQNPAYADTLKAFLNERSRPFYQGQIATDIISTVKGFSANPGLLEQADFNAYQAKERPAVCAKFLAYNVCGMGPPSSGALTLGQILQIVEPWKIETRSPDDAQTWRLIGDASRLAFADRGRYMADSDFIKMPTKGLLKQSYTDARSRLLKIEKALEKAPVGEPEWDDAALPRADDESLELPSTSHLSIVDAQGNIVSMTTTIENGFGSRLMTNGFLLNNELTDFSFRPERNGKPIANRVEPGKRPRSSMSPTIVMKEGKPVLVIGSPGGSRIIPYVANAIIAHLAWGENIQQAIARPHLVNRFGTYDLEKGTSAEAFEPSLQALGFKTNIRELNSGLHAISITPEGLSGGADPRREGIVLGK","length":590,"molWeight":63125,"crc64":"976F744043E9A116","md5":"0E0C620335F0B663921ED17A02957C3F"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"PATHWAY":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Signal":1,"Chain":1,"Region":1,"Active site":1,"Binding site":4},"uniParcId":"UPI0036369DD0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FAN9","uniProtkbId":"A0ABW3FAN9_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915516.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Anhydro-N-acetylmuramic acid kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"2.7.1.170"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"AnhMurNAc kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"anmK"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915516.1"}],"value":"ACFQ14_03750"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Catalyzes the specific phosphorylation of 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) with the simultaneous cleavage of the 1,6-anhydro ring, generating MurNAc-6-P. Is required for the utilization of anhMurNAc either imported from the medium or derived from its own cell wall murein, and thus plays a role in cell wall recycling"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,6-anhydro-N-acetyl-beta-muramate + ATP + H2O = N-acetyl-D-muramate 6-phosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24952"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58690"},{"database":"ChEBI","id":"CHEBI:58722"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.170","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Amino-sugar metabolism; 1,6-anhydro-N-acetylmuramate degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Cell wall biogenesis; peptidoglycan recycling"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"value":"Belongs to the anhydro-N-acetylmuramic acid kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915516.1"}],"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":"Binding site","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915516.1"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01270"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915516.1"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000003","properties":[{"key":"ProteinId","value":"MFD0915516.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377212061.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000003.1"}]},{"database":"Proteomes","id":"UP001597101","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016773","properties":[{"key":"GoTerm","value":"F:phosphotransferase activity, alcohol group as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0097175","properties":[{"key":"GoTerm","value":"P:1,6-anhydro-N-acetyl-beta-muramic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006040","properties":[{"key":"GoTerm","value":"P:amino sugar metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009254","properties":[{"key":"GoTerm","value":"P:peptidoglycan turnover"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.420.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01270","properties":[{"key":"EntryName","value":"AnhMurNAc_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005338","properties":[{"key":"EntryName","value":"Anhydro_N_Ac-Mur_kinase"}]},{"database":"InterPro","id":"IPR043129","properties":[{"key":"EntryName","value":"ATPase_NBD"}]},{"database":"NCBIfam","id":"NF007141","properties":[{"key":"EntryName","value":"PRK09585.1-5"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30605","properties":[{"key":"EntryName","value":"ANHYDRO-N-ACETYLMURAMIC ACID KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30605:SF0","properties":[{"key":"EntryName","value":"ANHYDRO-N-ACETYLMURAMIC ACID KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03702","properties":[{"key":"EntryName","value":"AnmK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53067","properties":[{"key":"EntryName","value":"Actin-like ATPase domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGTSMDGIDVAMLSSDGEGWIEFGPSISCGYSPSDRTLLERALVDAAQIRIRTERLGALGDAEAMIIQRHVEAVGQFLKVNNLRPSDIDLIGFHGQTVLHRPDERLTVQIGDGHMLARELGIDTVFDMRAADIAAGGQGAPLVPVFHEALATRLHIEGPICFVNIGGISNITYLREGDPPVAFDTGPGNALIDQWMQTVGGIPYDAAGAIASEGQVVGTVVERYMATPYFQKTLPKSLDRLDFPALDPSEADLSDGARSLARLTAEAIFAGLDHLPEPPKNWIVCGGGRHNRAIMSDLRELAGEYSASVHSAEDVNLDGDMMEAQAFAYLAIRARADLPLTFPTTTGCPQPMSGGVFAPAKEAKDA","length":367,"molWeight":39180,"crc64":"BB1955C4217A7628","md5":"A39727D90D2DD30CF64492446B5D7C4F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Binding site":1},"uniParcId":"UPI00363783BB"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FAS6","uniProtkbId":"A0ABW3FAS6_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915564.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"GTP cyclohydrolase 1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"3.5.4.16"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"GTP cyclohydrolase I"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"GTP-CH-I"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915564.1"}],"value":"folE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915564.1"}],"value":"ACFQ14_04005"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + H2O = 7,8-dihydroneopterin 3'-triphosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17473"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:58462"}],"ecNumber":"3.5.4.16","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001052"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"Cofactor biosynthesis; 7,8-dihydroneopterin triphosphate biosynthesis; 7,8-dihydroneopterin triphosphate from GTP: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"Homopolymer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011857"}],"value":"Toroid-shaped homodecamer, composed of two pentamers of five dimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008085"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"value":"Belongs to the GTP cyclohydrolase I family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915564.1"}],"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":31,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"GTP cyclohydrolase I","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01227"}]},{"type":"Binding site","location":{"start":{"value":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":172,"modifier":"EXACT"},"end":{"value":172,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022563"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0554","category":"Biological process","name":"One-carbon metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00223"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000003","properties":[{"key":"ProteinId","value":"MFD0915564.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211422.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000003.1"}]},{"database":"Proteomes","id":"UP001597101","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:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003934","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase I 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:0006730","properties":[{"key":"GoTerm","value":"P:one-carbon metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006729","properties":[{"key":"GoTerm","value":"P:tetrahydrobiopterin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046654","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"1.10.286.10:FF:000001","properties":[{"key":"EntryName","value":"GTP cyclohydrolase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1130.10:FF:000001","properties":[{"key":"EntryName","value":"GTP cyclohydrolase 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.286.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1130.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00223","properties":[{"key":"EntryName","value":"FolE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR043133","properties":[{"key":"EntryName","value":"GTP-CH-I_C/QueF"}]},{"database":"InterPro","id":"IPR043134","properties":[{"key":"EntryName","value":"GTP-CH-I_N"}]},{"database":"InterPro","id":"IPR001474","properties":[{"key":"EntryName","value":"GTP_CycHdrlase_I"}]},{"database":"InterPro","id":"IPR018234","properties":[{"key":"EntryName","value":"GTP_CycHdrlase_I_CS"}]},{"database":"InterPro","id":"IPR020602","properties":[{"key":"EntryName","value":"GTP_CycHdrlase_I_dom"}]},{"database":"NCBIfam","id":"NF006825","properties":[{"key":"EntryName","value":"folE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006826","properties":[{"key":"EntryName","value":"folE"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00063","properties":[{"key":"EntryName","value":"folE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11109:SF7","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE 1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11109","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01227","properties":[{"key":"EntryName","value":"GTP_cyclohydroI"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55620","properties":[{"key":"EntryName","value":"Tetrahydrobiopterin biosynthesis enzymes-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00859","properties":[{"key":"EntryName","value":"GTP_CYCLOHYDROL_1_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDEIVDKAALTAASKPTPNAQLKRPTREQAEAAVRTLLLWSGDDPSREGLLDTPKRVAKAYSELFEGYGQDPHEVLGRTFEEVAGYDDMVVVRDIEFHSHCEHHMVPIIGRAHVGYLPDGRVLGLSKIARVVDIFARRLQTQESMTAQVADAIQESLEPRGVAVMIEAEHMCMAMRGIRKQGSTTLTTTFTGAFRDEPAEQMHFMSLVNSAKK","length":213,"molWeight":23649,"crc64":"AFB783CA399672F1","md5":"8DF844FBB748440966A8199886D8F0C5"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Binding site":3},"uniParcId":"UPI00362AAF3F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABW3FAU6","uniProtkbId":"A0ABW3FAU6_9HYPH","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Pseudahrensia aquimaris","taxonId":744461,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915355.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"lineage":["Bacteria","Pseudomonadati","Pseudomonadota","Alphaproteobacteria","Hyphomicrobiales","Ahrensiaceae","Pseudahrensia"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00017462"}],"value":"Alkyl hydroperoxide reductase C"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013021"}],"value":"1.11.1.26"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032077"}],"value":"Peroxiredoxin"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915355.1"}],"value":"ACFQ14_02935"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a hydroperoxide + NADH + H(+) = an alcohol + NAD(+) + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:62628"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30879"},{"database":"ChEBI","id":"CHEBI:35924"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.11.1.26","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047572"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011654"}],"value":"Homodimer; disulfide-linked, upon oxidation. 5 homodimers assemble to form a ring-like decamer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009796"}],"value":"Belongs to the peroxiredoxin family. AhpC/Prx1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025719"}],"value":"Belongs to the peroxiredoxin family. Prx6 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00691"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915355.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":167,"modifier":"EXACT"}},"description":"Thioredoxin","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51352"}]},{"type":"Active site","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":45,"modifier":"EXACT"}},"description":"Cysteine sulfenic acid (-SOH) intermediate; for peroxidase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000239-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022862"}],"id":"KW-0049","category":"Molecular function","name":"Antioxidant"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915355.1"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFD0915355.1"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023284"}],"id":"KW-0676","category":"Domain","name":"Redox-active center"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}],"value":"CCUG 60023","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001597101"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHTJV010000002","properties":[{"key":"ProteinId","value":"MFD0915355.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_377211201.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_JBHTJV010000002.1"}]},{"database":"Proteomes","id":"UP001597101","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:0102039","properties":[{"key":"GoTerm","value":"F:NADH-dependent peroxiredoxin activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008379","properties":[{"key":"GoTerm","value":"F:thioredoxin peroxidase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0045454","properties":[{"key":"GoTerm","value":"P:cell redox homeostasis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033554","properties":[{"key":"GoTerm","value":"P:cellular response to stress"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006979","properties":[{"key":"GoTerm","value":"P:response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03016","properties":[{"key":"EntryName","value":"PRX_1cys"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.30.10:FF:000011","properties":[{"key":"EntryName","value":"Peroxiredoxin PRX1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1020.10","properties":[{"key":"EntryName","value":"Antioxidant, Horf6, Chain A, domain2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.30.10","properties":[{"key":"EntryName","value":"Glutaredoxin"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000866","properties":[{"key":"EntryName","value":"AhpC/TSA"}]},{"database":"InterPro","id":"IPR050217","properties":[{"key":"EntryName","value":"Peroxiredoxin"}]},{"database":"InterPro","id":"IPR024706","properties":[{"key":"EntryName","value":"Peroxiredoxin_AhpC-typ"}]},{"database":"InterPro","id":"IPR019479","properties":[{"key":"EntryName","value":"Peroxiredoxin_C"}]},{"database":"InterPro","id":"IPR045020","properties":[{"key":"EntryName","value":"PRX_1cys"}]},{"database":"InterPro","id":"IPR036249","properties":[{"key":"EntryName","value":"Thioredoxin-like_sf"}]},{"database":"InterPro","id":"IPR013766","properties":[{"key":"EntryName","value":"Thioredoxin_domain"}]},{"database":"PANTHER","id":"PTHR10681:SF121","properties":[{"key":"EntryName","value":"ALKYL HYDROPEROXIDE REDUCTASE C"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10681","properties":[{"key":"EntryName","value":"THIOREDOXIN PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10417","properties":[{"key":"EntryName","value":"1-cysPrx_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00578","properties":[{"key":"EntryName","value":"AhpC-TSA"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000239","properties":[{"key":"EntryName","value":"AHPC"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52833","properties":[{"key":"EntryName","value":"Thioredoxin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51352","properties":[{"key":"EntryName","value":"THIOREDOXIN_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGLRINDTIPDLTVTTDHGKISLHDWVGDSWAVIFSHPKDFTPVCTTEFGAVAQLADEWAKRNTKVLGVSVDGVEDHVKWKKDIEAVGGAEATFAIVADDGLEMAKAFDMLPAEYVLPDGRTPADSATVRSVFIIGPDKQVKLMMTYPMTVGRNFAEILRALDGLQMSTKGVATPANWEIGQDVIVPATVSTEDAEAKFGKVNVVLPYLRTVKAPN","length":216,"molWeight":23415,"crc64":"0430982ECCDB0FB3","md5":"8D776E4C92019F5DCAF52B7BAF0FD357"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1},"uniParcId":"UPI003642FC10"}}]}