{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EAG3","uniProtkbId":"A0ABR6EAG3_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242072.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Probable dual-specificity RNA methyltransferase RlmN"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"2.1.1.192"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA (adenine(2503)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"23S rRNA m2A2503 methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Ribosomal RNA large subunit methyltransferase N"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA (adenine(37)-C(2))-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"tRNA m2A37 methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242072.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242072.1"}],"value":"GL263_00540"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Specifically methylates position 2 of adenine 2503 in 23S rRNA and position 2 of adenine 37 in tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(2503) in 23S rRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(2503) in 23S rRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:42916"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10152"},{"database":"Rhea","id":"RHEA-COMP:10282"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine(37) in tRNA + 2 reduced [2Fe-2S]-[ferredoxin] + 2 S-adenosyl-L-methionine = 2-methyladenosine(37) in tRNA + 5'-deoxyadenosine + L-methionine + 2 oxidized [2Fe-2S]-[ferredoxin] + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43332"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"Rhea","id":"RHEA-COMP:10162"},{"database":"Rhea","id":"RHEA-COMP:10485"},{"database":"ChEBI","id":"CHEBI:17319"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"},{"database":"ChEBI","id":"CHEBI:57844"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:74411"},{"database":"ChEBI","id":"CHEBI:74497"}],"ecNumber":"2.1.1.192","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 cysteines and an exchangeable S-adenosyl-L-methionine."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Reaction proceeds by a ping-pong mechanism involving intermediate methylation of a conserved cysteine residue"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Belongs to the radical SAM superfamily. RlmN family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242072.1"}],"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":117,"modifier":"EXACT"},"end":{"value":357,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":111,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":362,"modifier":"EXACT"},"end":{"value":362,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"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":135,"modifier":"EXACT"},"end":{"value":135,"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":138,"modifier":"EXACT"},"end":{"value":138,"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":186,"modifier":"EXACT"},"end":{"value":187,"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":220,"modifier":"EXACT"},"end":{"value":220,"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":243,"modifier":"EXACT"},"end":{"value":245,"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":319,"modifier":"EXACT"},"end":{"value":319,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022552"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0698","category":"Biological process","name":"rRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000004","properties":[{"key":"ProteinId","value":"MBB1242072.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853509.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000004.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0051539","properties":[{"key":"GoTerm","value":"F:4 iron, 4 sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070040","properties":[{"key":"GoTerm","value":"F:rRNA (adenine(2503)-C2-)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019843","properties":[{"key":"GoTerm","value":"F:rRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002935","properties":[{"key":"GoTerm","value":"F:tRNA (adenine(37)-C2)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070475","properties":[{"key":"GoTerm","value":"P:rRNA base methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030488","properties":[{"key":"GoTerm","value":"P:tRNA methylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01335","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000014","properties":[{"key":"EntryName","value":"Probable dual-specificity RNA methyltransferase RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.150.530","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.70","properties":[{"key":"EntryName","value":"Aldolase class I"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01849","properties":[{"key":"EntryName","value":"RNA_methyltr_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR040072","properties":[{"key":"EntryName","value":"Methyltransferase_A"}]},{"database":"InterPro","id":"IPR048641","properties":[{"key":"EntryName","value":"RlmN_N"}]},{"database":"InterPro","id":"IPR027492","properties":[{"key":"EntryName","value":"RNA_MTrfase_RlmN"}]},{"database":"InterPro","id":"IPR004383","properties":[{"key":"EntryName","value":"rRNA_lsu_MTrfase_RlmN/Cfr"}]},{"database":"InterPro","id":"IPR007197","properties":[{"key":"EntryName","value":"rSAM"}]},{"database":"InterPro","id":"IPR058240","properties":[{"key":"EntryName","value":"rSAM_sf"}]},{"database":"NCBIfam","id":"TIGR00048","properties":[{"key":"EntryName","value":"rRNA_mod_RlmN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544","properties":[{"key":"EntryName","value":"23S RRNA METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30544:SF5","properties":[{"key":"EntryName","value":"RADICAL SAM CORE DOMAIN-CONTAINING PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04055","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21016","properties":[{"key":"EntryName","value":"RlmN_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006004","properties":[{"key":"EntryName","value":"CHP00048"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00275","properties":[{"key":"EntryName","value":"adenosine_C2_methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDG01062","properties":[{"key":"EntryName","value":"methyltransferase_(Class_A)"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00029","properties":[{"key":"EntryName","value":"Radical_SAM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF102114","properties":[{"key":"EntryName","value":"Radical SAM enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51918","properties":[{"key":"EntryName","value":"RADICAL_SAM"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTPPKPGELTFVAPRGAKKPPRHLADLSPAERREALTAIGEKPFRAKQLSQHYFARFTQDPADWTDIPAAARERLAAELLPQLMTVVRNISCDDDTTRKTLWRLHDGTLVESVLMRYPDRVTMCISSQAGCGMNCPFCATGQAGLDRNLSTAEIVHQIVDGMRALRDGEVPGGPARLSNIVFMGMGEPLANYNRVVGAIRRLTDPAPDGLGLSQRGITVSTVGLVPAMLRFADEGFKCRLAVSLHAPDDELRDTLVPVNTRWKVREVLDAAWEYAARSGRRVSIEYALIRDINDHAWRADLLGRLLKGRRAHVNLIPLNPTPGSKWTASRPEDERAFVEALAAHGVPVTVRDTRGQEIDGACGQLAASEVSGS","length":373,"molWeight":40850,"crc64":"B5DBAB0D1EC8C8BD","md5":"CFD2738A83D1FDCC5A43381380652F82"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Active site":2,"Binding site":7},"uniParcId":"UPI001600AD1B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6ECP4","uniProtkbId":"A0ABR6ECP4_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1243096.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00020204"}],"value":"Multifunctional 2-oxoglutarate metabolism enzyme"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012280"}],"value":"1.2.4.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013148"}],"value":"2.2.1.5"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012945"}],"value":"2.3.1.61"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012226"}],"value":"4.1.1.71"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029773"}],"value":"2-hydroxy-3-oxoadipate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030696"}],"value":"2-oxoglutarate carboxy-lyase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032880"}],"value":"2-oxoglutarate decarboxylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032625"}],"value":"Alpha-ketoglutarate decarboxylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033243"}],"value":"Alpha-ketoglutarate-glyoxylate carboligase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1243096.1"}],"value":"GL263_05875"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-oxoglutarate + H(+) = succinate semialdehyde + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10524"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:57706"}],"ecNumber":"4.1.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049135"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-[(R)-dihydrolipoyl]-L-lysyl-[protein] + succinyl-CoA = N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15213"},{"database":"Rhea","id":"RHEA-COMP:10475"},{"database":"Rhea","id":"RHEA-COMP:20092"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57292"},{"database":"ChEBI","id":"CHEBI:83100"},{"database":"ChEBI","id":"CHEBI:83120"}],"ecNumber":"2.3.1.61","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052761"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-[(R)-lipoyl]-L-lysyl-[protein] + 2-oxoglutarate + H(+) = N(6)-[(R)-S(8)-succinyldihydrolipoyl]-L-lysyl-[protein] + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12188"},{"database":"Rhea","id":"RHEA-COMP:10474"},{"database":"Rhea","id":"RHEA-COMP:20092"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:83099"},{"database":"ChEBI","id":"CHEBI:83120"}],"ecNumber":"1.2.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051911"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"glyoxylate + 2-oxoglutarate + H(+) = 2-hydroxy-3-oxoadipate + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14341"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:16810"},{"database":"ChEBI","id":"CHEBI:36655"},{"database":"ChEBI","id":"CHEBI:57712"}],"ecNumber":"2.2.1.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047721"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"thiamine diphosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001964"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:58937"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005053"}],"value":"Carbohydrate metabolism; tricarboxylic acid cycle; succinate from 2-oxoglutarate (transferase route): step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004813"}],"value":"Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-CoA from 2-oxoglutarate (dehydrogenase route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007702"}],"value":"Belongs to the 2-oxoacid dehydrogenase family. Kgd subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1243096.1"}],"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":933,"modifier":"EXACT"},"end":{"value":1126,"modifier":"EXACT"}},"description":"Transketolase-like pyrimidine-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00861"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1253,"modifier":"EXACT"},"end":{"value":1281,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":67,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1259,"modifier":"EXACT"},"end":{"value":1269,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1243096.1"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023052"}],"id":"KW-0786","category":"Ligand","name":"Thiamine pyrophosphate"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022532"}],"id":"KW-0816","category":"Biological process","name":"Tricarboxylic acid cycle"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000052","properties":[{"key":"ProteinId","value":"MBB1243096.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182854500.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000052.1"}]},{"database":"Proteomes","id":"UP000766698","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:0045252","properties":[{"key":"GoTerm","value":"C:oxoglutarate dehydrogenase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0050439","properties":[{"key":"GoTerm","value":"F:2-hydroxy-3-oxoadipate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008683","properties":[{"key":"GoTerm","value":"F:2-oxoglutarate decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004149","properties":[{"key":"GoTerm","value":"F:dihydrolipoyllysine-residue succinyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004591","properties":[{"key":"GoTerm","value":"F:oxoglutarate dehydrogenase (succinyl-transferring) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0030976","properties":[{"key":"GoTerm","value":"F:thiamine pyrophosphate binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006099","properties":[{"key":"GoTerm","value":"P:tricarboxylic acid cycle"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd02016","properties":[{"key":"EntryName","value":"TPP_E1_OGDC_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.559.10:FF:000011","properties":[{"key":"EntryName","value":"2-oxoglutarate dehydrogenase E1 component"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.11610:FF:000002","properties":[{"key":"EntryName","value":"2-oxoglutarate dehydrogenase E1 component"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.970:FF:000018","properties":[{"key":"EntryName","value":"2-oxoglutarate dehydrogenase E1 component"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.287.1150:FF:000003","properties":[{"key":"EntryName","value":"2-oxoglutarate dehydrogenase, E1 subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.12470","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.970","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.559.10","properties":[{"key":"EntryName","value":"Chloramphenicol acetyltransferase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.11610","properties":[{"key":"EntryName","value":"Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.287.1150","properties":[{"key":"EntryName","value":"TPP helical domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001078","properties":[{"key":"EntryName","value":"2-oxoacid_DH_actylTfrase"}]},{"database":"InterPro","id":"IPR032106","properties":[{"key":"EntryName","value":"2-oxogl_dehyd_N"}]},{"database":"InterPro","id":"IPR011603","properties":[{"key":"EntryName","value":"2oxoglutarate_DH_E1"}]},{"database":"InterPro","id":"IPR023213","properties":[{"key":"EntryName","value":"CAT-like_dom_sf"}]},{"database":"InterPro","id":"IPR001017","properties":[{"key":"EntryName","value":"DH_E1"}]},{"database":"InterPro","id":"IPR042179","properties":[{"key":"EntryName","value":"KGD_C_sf"}]},{"database":"InterPro","id":"IPR031717","properties":[{"key":"EntryName","value":"ODO-1/KGD_C"}]},{"database":"InterPro","id":"IPR029061","properties":[{"key":"EntryName","value":"THDP-binding"}]},{"database":"InterPro","id":"IPR005475","properties":[{"key":"EntryName","value":"Transketolase-like_Pyr-bd"}]},{"database":"NCBIfam","id":"TIGR00239","properties":[{"key":"EntryName","value":"2oxo_dh_E1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF006914","properties":[{"key":"EntryName","value":"PRK09404.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF008907","properties":[{"key":"EntryName","value":"PRK12270.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23152:SF4","properties":[{"key":"EntryName","value":"2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23152","properties":[{"key":"EntryName","value":"2-OXOGLUTARATE DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00198","properties":[{"key":"EntryName","value":"2-oxoacid_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16078","properties":[{"key":"EntryName","value":"2-oxogl_dehyd_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00676","properties":[{"key":"EntryName","value":"E1_dh"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16870","properties":[{"key":"EntryName","value":"OxoGdeHyase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02779","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00861","properties":[{"key":"EntryName","value":"Transket_pyr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52777","properties":[{"key":"EntryName","value":"CoA-dependent acyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52518","properties":[{"key":"EntryName","value":"Thiamin diphosphate-binding fold (THDP-binding)"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MSSQSPKTSSISTDQDGQGKTPDAGFGPNEWLVDEIYQQYLQDPNSVDRAWWDFFADYKPGKTTGDTPARPAETAAQAPAQPAPTSAAPATQPQRAEPAKAEPAARPAAAQPPAQQAKAQAAPAQAAAPAKPAPAKAAPAKAAPAKAAPAKGADDAEKPAGPELVTLRGPSAAVAKNMSASLELPTATSVRAVPVKLLFDNRIVINNHLKRARGGKVSFTHLIGYAMVQAMKLMPSMNWSFAEKDGKPTLVKPEHVNLGLAIDLVKPNGDRQLVVAAIKKAETLTFFEFWQAYEDIVRRARANKLTMDDFTGVTCSLTNPGGIGTVHSVPRLMPGQSAIIGVGAMEYPAEFQGTSQDTLNRLGVSKVMTLTSTYDHRVIQGAQSGEFLRVMHQLLLGENNFYDDIFEALRIPYEPVRWNRDIDVSHDDEVTKAARVFDLIHSYRVRGHVMADTDPLEYKQRKHPDLDIASHGLTLWDLEREFAVGGFAGKSMLRLREILGVLRDSYCRTTGIEYMHIQDPKQRKWIQDRVERPHSNPEREEQLRILRRLNAAEAFETFLQTKYVGQKRFSLEGGESVVPLLDAIIDSAAESRLDEAVIGMAHRGRLNVLANIVGKSYAQIFREFEGNLDPKSMHGSGDVKYHLGAEGTFTGLNGEQIKVSLTANPSHLEAVDPVVVGVARAKQDIIGKGGTDFTVLPIQLHGDAAFAGQGVVAETLNMSQLRGYRCGGTVHIVINNQVGFTAAPEAARSSMYCTDVARMIEAPIFHVNGDDPEAVVRVARLAFEFRQAFNKDVVIDLVCYRRRGHNESDNPSFTNPRMYNLIDKKRSVRKLYTESLIGRGDITMEEAEQALQDFQGQLEKVFSEVREAAVTPAPAEAPVPQAEFPVAVETAVSPEVVKRIAESQVNIPDRVTVHPRLLPQLQRRAAMVEDGTIDWGMGETLAVGSLLMEGTPVRLAGQDSRRGTFGQRHAVLIDQNTGEDYTPLLYLSEDQARFNVYDSLLSEYAAMGFEYGYSLARPEALVMWEAQFGDFVNGAQTVVDEFISSAEQKWNQTSGVTLLLPHGYEGQGPDHSSARIERFLQLCAQNSMTVAMPSLPSNYFHLLRWQVHNPHHKPLVVFTPKSMLRLKAAASRTEEFTTGGFRPVIGDVPVESGEVDPSQIRKVVFCSGKVYYDLDAERQKRGAKDTAIIRLERLYPLPGQEIQAEMAKYSGAEKFVWAQEEPANQGAWPFIALNLVDHLDLIIGSEPVPNADRLRRVSRPSSSSPAVGSAKRHQSEQQQLVTEVFDL","length":1287,"molWeight":141534,"crc64":"6F0C33915EB870C2","md5":"432A06AA3A1D98592566396DFE773CBD"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":4,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Compositional bias":3},"uniParcId":"UPI0015FF1A2B"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6ED18","uniProtkbId":"A0ABR6ED18_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242880.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Phosphoribosyl-AMP cyclohydrolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"PRA-CH"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"3.5.4.19"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242880.1"}],"value":"hisI"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242880.1"}],"value":"GL263_04760"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Catalyzes the hydrolysis of the adenine ring of phosphoribosyl-AMP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-(5-phospho-beta-D-ribosyl)-5'-AMP + H2O = 1-(5-phospho-beta-D-ribosyl)-5-[(5-phospho-beta-D-ribosylamino)methylideneamino]imidazole-4-carboxamide","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20049"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:58435"},{"database":"ChEBI","id":"CHEBI:59457"}],"ecNumber":"3.5.4.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000024"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1-(5-phospho-beta-D-ribosyl)-ATP + H2O = 1-(5-phospho-beta-D-ribosyl)-5'-AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22828"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:59457"},{"database":"ChEBI","id":"CHEBI:73183"}],"ecNumber":"3.6.1.31","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001460"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005204"}],"value":"Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005169"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Amino-acid biosynthesis; L-histidine biosynthesis; L-histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"value":"Belongs to the PRA-CH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007731"}],"value":"In the C-terminal section; belongs to the PRA-PH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008299"}],"value":"In the N-terminal section; belongs to the PRA-CH family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242880.1"}],"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":57,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"Phosphoribosyl-AMP cyclohydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01502"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":27,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":105,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":106,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":121,"modifier":"EXACT"},"end":{"value":121,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":128,"modifier":"EXACT"},"end":{"value":128,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023102"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0368","category":"Biological process","name":"Histidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01021"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000040","properties":[{"key":"ProteinId","value":"MBB1242880.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182854293.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000040.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004635","properties":[{"key":"GoTerm","value":"F:phosphoribosyl-AMP cyclohydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004636","properties":[{"key":"GoTerm","value":"F:phosphoribosyl-ATP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000105","properties":[{"key":"GoTerm","value":"P:L-histidine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.10.20.810:FF:000001","properties":[{"key":"EntryName","value":"Histidine biosynthesis bifunctional protein HisIE"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.20.810","properties":[{"key":"EntryName","value":"Phosphoribosyl-AMP cyclohydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01021","properties":[{"key":"EntryName","value":"HisI"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR026660","properties":[{"key":"EntryName","value":"PRA-CH"}]},{"database":"InterPro","id":"IPR002496","properties":[{"key":"EntryName","value":"PRib_AMP_CycHydrolase_dom"}]},{"database":"InterPro","id":"IPR038019","properties":[{"key":"EntryName","value":"PRib_AMP_CycHydrolase_sf"}]},{"database":"NCBIfam","id":"NF000768","properties":[{"key":"EntryName","value":"hisI"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42945","properties":[{"key":"EntryName","value":"HISTIDINE BIOSYNTHESIS BIFUNCTIONAL PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42945:SF11","properties":[{"key":"EntryName","value":"PHOSPHORIBOSYL-AMP CYCLOHYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01502","properties":[{"key":"EntryName","value":"PRA-CH"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF141734","properties":[{"key":"EntryName","value":"HisI-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSASSPTPKAPAGPGSPAASVPDSPLDPAIAARLKRNADGLLPAIAQQHDTGEVLMLGWMDDEALHRTLTTGRCTYWSRSRGEYWVKGDTSGHVQHVKSVALDCDGDTLLVRVDQVGAACHTGDRTCFDADRLPLAEQPRTEEATRP","length":148,"molWeight":15804,"crc64":"003AB2C079BFEEA6","md5":"F3152A587E3F1F9459731CC6446B7196"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":6},"uniParcId":"UPI001602E0ED"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EEF5","uniProtkbId":"A0ABR6EEF5_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1243711.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Phosphohexokinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"pfkA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1243711.1"}],"value":"GL263_09080"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate and glycerone phosphate from D-glucose: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. Mixed-substrate PFK group III subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1243711.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":297,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Active site","location":{"start":{"value":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Binding site","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":10,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":102,"modifier":"EXACT"},"end":{"value":105,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":103,"modifier":"EXACT"},"end":{"value":103,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":171,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":222,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":266,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":272,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Site","location":{"start":{"value":104,"modifier":"EXACT"},"end":{"value":104,"modifier":"EXACT"}},"description":"Important for substrate specificity; cannot use PPi as phosphoryl donor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000093","properties":[{"key":"ProteinId","value":"MBB1243711.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182855084.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000093.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003872","properties":[{"key":"GoTerm","value":"F:6-phosphofructokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016208","properties":[{"key":"GoTerm","value":"F:AMP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0047334","properties":[{"key":"GoTerm","value":"F:diphosphate-fructose-6-phosphate 1-phosphotransferase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"FunFam","id":"3.40.50.460:FF:000005","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01976","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR012829","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02483","properties":[{"key":"EntryName","value":"PFK_mixed"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF52","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRIGVLTAGGDCPGLNAVIRSVVHRAVVDRDDEVIGFEDGFKGLLEGRHRVLDLNSVSGILARGGTILGSARLERDRLREACDNSEELMGRLGIDALIPIGGEGTLTAATMLSEAGLPVVGVPKTIDNDISATDRTFGFDTAVGVATEAMDRLKTTAESHQRVMVVEVMGRHAGWIALEAGMAGGAHGICLPERPFEIDELCKMVEERFSRGKKFAVICVAEGARPAEGSMEYAKGEIDQYGHERFVGIGNRLATEMERRLGKEARPVILGHVQRGGTPTAYDRVLATRFGWHAVEAAHRGDFGMMTALRGTDIVMTPLADATRELKTVPQDRMDETEAVF","length":341,"molWeight":36811,"crc64":"4469DBE8B319DC72","md5":"B6A5C03072275232CEBB21C3565A464C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":10,"Site":1},"uniParcId":"UPI001601256D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EGE9","uniProtkbId":"A0ABR6EGE9_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1244413.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"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":"MBB1244413.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1244413.1"}],"value":"GL263_12700"}]}],"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":"MBB1244413.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":142,"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":240,"modifier":"EXACT"}},"description":"Pyrophosphorylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":261,"modifier":"EXACT"}},"description":"Linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":493,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":458,"modifier":"EXACT"},"end":{"value":493,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":373,"modifier":"EXACT"},"end":{"value":373,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Binding site","location":{"start":{"value":12,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":113,"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":150,"modifier":"EXACT"},"end":{"value":150,"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":165,"modifier":"EXACT"},"end":{"value":165,"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":180,"modifier":"EXACT"},"end":{"value":180,"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":238,"modifier":"EXACT"},"end":{"value":238,"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":238,"modifier":"EXACT"},"end":{"value":238,"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":343,"modifier":"EXACT"},"end":{"value":343,"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":361,"modifier":"EXACT"},"end":{"value":361,"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":376,"modifier":"EXACT"},"end":{"value":376,"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":387,"modifier":"EXACT"},"end":{"value":387,"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":390,"modifier":"EXACT"},"end":{"value":390,"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":396,"modifier":"EXACT"},"end":{"value":397,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Binding site","location":{"start":{"value":415,"modifier":"EXACT"},"end":{"value":415,"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":433,"modifier":"EXACT"},"end":{"value":433,"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":450,"modifier":"EXACT"},"end":{"value":450,"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":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000153","properties":[{"key":"ProteinId","value":"MBB1244413.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182855773.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000153.1"}]},{"database":"Proteomes","id":"UP000766698","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":"NF010932","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00132","properties":[{"key":"EntryName","value":"Hexapep"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSAIRPAAVVVLAAGEGTRMKSATPKVLHEICGLSLVGHVVSASRELDPEHLVVVVGHAREQVAGHLAGLDAGVRTAVQEEQNGTGHAVRMGLEALAADGVELRGTVVVTCGDTPLLTGTTLRALADTHAADGNAVTVLSAEVPDATGYGRIVRAADGSVTAIVEHKDADGAQLAIREINSGVFAFDAELLVESLGKVRTDNSQGEEYLTDVLGILREAGHRVGAAVAGDHREIAGINNRVQLAQARRLMNDRLLEAAMLAGVTVVDPATTWMDVAVTVEPDAVVLPGTQLLGATHLSEGCEVGPNARLTDTHVGPGAVVGDSVAVGARVGPGASVGPYAYLRPGTVLGERAKAGTYVEMKNATIGEGTKVPHLSYVGDATIGDFTNIGAASVFVNYDGEHKHHTTVGSHCKTGSDNMFVAPVTIGDGAYTAAGSVITKDVPPGSLAVARGQQRNIEGWVARKRPGSAAAQAAARAEGDPDTGDEAGRGKGRD","length":493,"molWeight":50510,"crc64":"6B85BA63856DD946","md5":"BC7C5C3734A454E08341C9D29696D7F0"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":3,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":4,"Compositional bias":1,"Active site":1,"Binding site":19},"uniParcId":"UPI001603A601"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EIT2","uniProtkbId":"A0ABR6EIT2_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245259.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"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":"MBB1245259.1"}],"value":"GL263_17025"}]}],"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":"MBB1245259.1"}],"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":86,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":401,"modifier":"EXACT"},"end":{"value":532,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":477,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":93,"modifier":"EXACT"},"end":{"value":93,"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":176,"modifier":"EXACT"},"end":{"value":182,"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":221,"modifier":"EXACT"},"end":{"value":222,"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":248,"modifier":"EXACT"},"end":{"value":248,"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":256,"modifier":"EXACT"},"end":{"value":256,"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":450,"modifier":"EXACT"},"end":{"value":450,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57791"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}],"ligand":{"name":"meso-2,6-diaminopimelate","id":"ChEBI:CHEBI:57791"}},{"type":"Binding site","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":477,"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":530,"modifier":"EXACT"},"end":{"value":530,"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":534,"modifier":"EXACT"},"end":{"value":534,"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":288,"modifier":"EXACT"},"end":{"value":288,"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":"MBB1245259.1"}],"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":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000255","properties":[{"key":"ProteinId","value":"MBB1245259.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000766698","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":"MTDAVDPGGGPRQPRPSRGPTDAGPGNLTAVPQADLTPSETEPAGKPEALALRPTGLRPVPLAELAASLDVRPRRATDAGAEDVTVTGITHDSRAVRPGDVYAALPGARFHGVDFATQAASLGAVAVLTDPAGVERALATGLPVLTVDDPRGRMGRLAAEIYGEPGRDLLQIGITGTSGKTTTAYLVEGGLRAAAKEGELTGLIGTVESRVGDRRVKSERTTPEATDLQALFAVMRENGVTSVAMEVSSHALVLGRVDGCVFDVAVFNNLSPEHLDFHPDMDDYFRAKAALFTPERSRVGVVNVDDEWGQRLVTEAGVPVITFSAEGHPDAHWRAEDVEIGPLGSTFTAVGPNGTRVRAAAPLSGTFNVSNTLAALVALVVAGVDAQTAADGIAAVPGVPGRLERVDAGQPYLAVVDYAHKPDAVESVLRAVRKVTPGRVHAVLGCGGDRDPHKRTAMGAALARLADTAVLTSDNPRSEDPLMILAAMLAGAAEVPSHDRGTVLLEEDRAAAIAAAVARAEPGDTVVVAGKGHEQGQDIAGVIRPFDDREVLREAILAAGHATSRSEDEERDAR","length":574,"molWeight":59619,"crc64":"D4F3F216C8F4DA1D","md5":"E3177A1B99B74D0FEA6F63531AEAFD01"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":1,"Motif":1,"Binding site":9,"Modified residue":1},"uniParcId":"UPI001603DBAA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EIV5","uniProtkbId":"A0ABR6EIV5_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245284.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"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":"MBB1245284.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245284.1"}],"value":"GL263_17150"}]}],"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":"MBB1245284.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":876,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":958,"modifier":"EXACT"},"end":{"value":1103,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":958,"modifier":"EXACT"},"end":{"value":1107,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":214,"modifier":"EXACT"},"end":{"value":214,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":249,"modifier":"EXACT"},"end":{"value":249,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":721,"modifier":"EXACT"},"end":{"value":721,"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":760,"modifier":"EXACT"},"end":{"value":760,"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":762,"modifier":"EXACT"},"end":{"value":762,"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":767,"modifier":"EXACT"},"end":{"value":767,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":792,"modifier":"EXACT"},"end":{"value":792,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":793,"modifier":"EXACT"},"end":{"value":793,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":794,"modifier":"EXACT"},"end":{"value":794,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":795,"modifier":"EXACT"},"end":{"value":795,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"3"}},{"type":"Binding site","location":{"start":{"value":835,"modifier":"EXACT"},"end":{"value":835,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI: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":847,"modifier":"EXACT"},"end":{"value":847,"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":847,"modifier":"EXACT"},"end":{"value":847,"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":847,"modifier":"EXACT"},"end":{"value":847,"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":847,"modifier":"EXACT"},"end":{"value":847,"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":847,"modifier":"EXACT"},"end":{"value":847,"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":849,"modifier":"EXACT"},"end":{"value":849,"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":849,"modifier":"EXACT"},"end":{"value":849,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"4"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022571"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0055","category":"Biological process","name":"Arginine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"id":"KW-0677","category":"Domain","name":"Repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000259","properties":[{"key":"ProteinId","value":"MBB1245284.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182856602.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000259.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000014","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPKRTDIKSVLVIGSGPIVIGQAAEFDYSGTQACRVLKAEGLRVVLVNSNPATIMTDPEIADATYVEPITPEFVEKIIAKERPDALLPTLGGQTALNTAISLHASGTLEKYNVELIGANVEAINKGEDRDLFKEVVEAVNARIGHGESARSVICHSMDDVLAGVEQLGGYPVVVRPSFTMGGAGSGFAHDEDELRRIAGQGLTLSPTTEVLLEESILGWKEYELELMRDRNDNVVVVCSIENFDPMGVHTGDSITVAPAMTLTDREYQVLRDVGIEIIREVGVDTGGCNIQFAVDPEDGRVIVIEMNPRVSRSSALASKATGFPIAKIAAKLAVGYTLDEIPNDITEQTPASFEPTLDYVVVKAPRFAFEKFPAADSTLTTTMKSVGEAMAIGRNFPEALQKALRSLEKKDSQFDFTTPVAELGDKAALLAEIPRPTDGRINTVMAAIRAGATPDEIFEATRLDPWFVDQLFLVKEIADELAAAERLDHELLAEAKRYGFSDAQIAGIRGLREDVVREVRHALGVRPVYKTVDTCAAEFAARTPYFYSSYDEETEVAPREKPAVIILGSGPNRIGQGIEFDYSCVHASFALSEAGYETVMVNCNPETVSTDYDTSDRLYFEPLTLEDVLEIVHAEQQAGPVAGVIVQLGGQTPLGLSQSLKDNGVPIVGTSPEAIHAAEDRGAFGRVLTDAGLPAPKYGTAYSFDEAKAIAAGIGYPVMVRPSYVLGGRGMEIVYDEPSLAGYLERHAGLISEHPVLIDRFLDDAIEIDVDALYDGTELYLGGVMEHIEEAGIHSGDSACALPPITLGGYDIKRLRASTEAIAEGVGVRGLINIQFAMAGDILYVLEANPRASRTVPFTSKATAVPLAKAAARISLGATIAQLREEGLLPAAGDGGTLPMDAPISVKEAVMPWSRFRDVHGRGVDTVLGPEMRSTGEVMGIDTVFGTAYAKSQAGAYGALPTKGRAFVSVANRDKRSLIFPARELVALGFELLATTGTAEVLKRNGINATIVRKQSQGEGPNGEKTIVQLIHDGEVDLIVNTPYGTGGRLDGYEIRTAAVARGVPCLTTVQALAAAVQGIEALGRGAVGVRSLQEHAAHLTAARDGE","length":1107,"molWeight":118226,"crc64":"FFD01318B25ECFB0","md5":"3F12441469AA1EE304DB60BF563A5C2F"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SUBUNIT":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Binding site":38},"uniParcId":"UPI0015FF0448"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EJ55","uniProtkbId":"A0ABR6EJ55_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245379.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00069359"}],"value":"Broad-specificity linear acyl-CoA dehydrogenase FadE5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012033"}],"value":"1.3.8.7"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012040"}],"value":"1.3.8.8"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077090"}],"value":"Long-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077336"}],"value":"Medium-chain-acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075470"}],"value":"Short-chain-acyl-CoA dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245379.1"}],"value":"GL263_17665"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054301"}],"value":"Acyl-CoA dehydrogenase that exhibits broad specificity for linear acyl-CoA substrates, with a preference for long-chain substrates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a long-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a long-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17721"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83721"},{"database":"ChEBI","id":"CHEBI:83727"}],"ecNumber":"1.3.8.8","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049247"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a medium-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a medium-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:14477"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:83723"},{"database":"ChEBI","id":"CHEBI:83726"}],"ecNumber":"1.3.8.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047882"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a short-chain 2,3-saturated fatty acyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = a short-chain (2E)-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47196"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:87487"},{"database":"ChEBI","id":"CHEBI:87488"}],"ecNumber":"1.3.8.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050315"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"butanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-butenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24004"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:57371"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050695"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"decanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-decenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48176"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:61406"},{"database":"ChEBI","id":"CHEBI:61430"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050703"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dodecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-dodecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47296"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57330"},{"database":"ChEBI","id":"CHEBI:57375"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050336"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hexanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-hexenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43464"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62077"},{"database":"ChEBI","id":"CHEBI:62620"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048375"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octadecanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-octadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:47240"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57394"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:71412"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050877"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxidized [electron-transfer flavoprotein] + hexadecanoyl-CoA + H(+) = (2E)-hexadecenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43448"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57379"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:61526"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052387"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004872"}],"value":"Lipid metabolism; fatty acid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009347"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"value":"Belongs to the acyl-CoA dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245379.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02770"}]},{"type":"Domain","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":452,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]},{"type":"Domain","location":{"start":{"value":472,"modifier":"EXACT"},"end":{"value":604,"modifier":"EXACT"}},"description":"Acetyl-CoA dehydrogenase-like C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF12806"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022832"}],"id":"KW-0276","category":"Biological process","name":"Fatty acid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362125"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000273","properties":[{"key":"ProteinId","value":"MBB1245379.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182856691.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000273.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004466","properties":[{"key":"GoTerm","value":"F:long-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070991","properties":[{"key":"GoTerm","value":"F:medium-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0016937","properties":[{"key":"GoTerm","value":"F:short-chain fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"CDD","id":"cd01153","properties":[{"key":"EntryName","value":"ACAD_fadE5"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.110.20:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase AidB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000016","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase FadE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.140.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 3"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR025878","properties":[{"key":"EntryName","value":"Acyl-CoA_dh-like_C_dom"}]},{"database":"InterPro","id":"IPR036250","properties":[{"key":"EntryName","value":"AcylCo_DH-like_C"}]},{"database":"InterPro","id":"IPR009075","properties":[{"key":"EntryName","value":"AcylCo_DH/oxidase_C"}]},{"database":"InterPro","id":"IPR006091","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_M"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"InterPro","id":"IPR052166","properties":[{"key":"EntryName","value":"Diverse_Acyl-CoA_DH"}]},{"database":"InterPro","id":"IPR034188","properties":[{"key":"EntryName","value":"FadE5-like"}]},{"database":"PANTHER","id":"PTHR42803","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42803:SF1","properties":[{"key":"EntryName","value":"BROAD-SPECIFICITY LINEAR ACYL-COA DEHYDROGENASE FADE5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12806","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47203","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase C-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56645","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase NM domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGHYKSNLRDIEFNLFEVLGRDTVYGTGPFAEMDVETAKSVLSEIARLSENELAASFEDADRNPPVFDPETNTAPIPESFKKSYQAYMDAEWWRLGIPEEIGGTTAPRSLLWGFAETILGANPAVWMYASGPAFAGVLYEEATEEQHKIAQRMVDRQWGSTMVLTEPDAGSDVGAGRAKAIKQEDGSWHIEGVKRFITSGEHDMSENIIHFVLARPEGHGPGTKGLSLFIVPKYDFDWETGELGERNGAYATNVEHKMGLKASNTCEMTFGDKHPAKGWLLGEKHDGIRQMFKIIEFARMMVGTKAIATLSTGYLNALEYAKERVQGADLAKFTDKTAPRVTITHHPDVRRSLMTQKAYAEGMRALVLYTAAVQDEILIKEHAGEDASAAIRLNDLLLPIVKGYGSEKSYEQLAQSLQTFGGSGYLQEYPIEQYIRDAKIDTLYEGTTAIQGQDYFFRKIVRDQGQALTALSEEIKKFLAEAAGGEGLAASRDQLAKSAADLEGMVGTMLTDLAATEQDVKSIYKVGLNTTRFLMASGDVVIGYLLLRGAAVAAEKLAGASAKDKAFYEGKIAAAKFFAANILPGVTVQRELAENIDLSVMELPEEAF","length":608,"molWeight":66686,"crc64":"1145AFA46B37B686","md5":"958E43C2C405AD9650DF5A00D858D778"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":9,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0015FF05F6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EKJ7","uniProtkbId":"A0ABR6EKJ7_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245039.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"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":"MBB1245039.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245039.1"}],"value":"GL263_15895"}]}],"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":"MBB1245039.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":2,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":405,"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":198,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":297,"modifier":"EXACT"},"end":{"value":297,"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":315,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":335,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":349,"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":353,"modifier":"EXACT"},"end":{"value":353,"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":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000225","properties":[{"key":"ProteinId","value":"MBB1245039.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182856378.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000225.1"}]},{"database":"Proteomes","id":"UP000766698","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":"MDKPRVVLGVGGGIAAYKACELLRRLTESGHDVRVVPTSSALHFVGEATWSALSGHPAGTEVWESVHEVPHVRIGQRADLVVVAPATADLLAKAAHGLADDLLTNTLLTARCPVVFAPAMHTEMWEHPATRANVETLRRRGAVVIEPAVGRLTGADTGKGRLPDPGDIFDVCLRTLAGRPAGGAPGGPARAGDMTGRHVVVSAGGTREPIDPVRFLGNRSSGRQGYALATTAAARGARVTLVAANTSLPDPAGVTVVPVGTALQLREAVLKAAADADAVVMAAAVADFRPVRYAEGKIKKRDGEEPAPIALVRNPDVLAEISADRPRAGQLVVGFAAETDQVLANGRAKLARKGCDLLVVNEVGADKTFGSTDNEAIVLAADGTEVPVSHGPKEKLADTVWDLVVQRWSPPPGS","length":414,"molWeight":43032,"crc64":"E920AE65F5EDB339","md5":"74CE0548CBA59418A96865DDB7A8556F"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI0015FF77CA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EKR4","uniProtkbId":"A0ABR6EKR4_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245114.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase subunit PdxT"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"4.3.3.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pdx2"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Pyridoxal 5'-phosphate synthase glutaminase subunit"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"3.5.1.2"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245114.1"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245114.1"}],"value":"GL263_16275"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054599"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Catalyzes the hydrolysis of glutamine to glutamate and ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The resulting ammonia molecule is channeled to the active site of PdxS"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"ecNumber":"3.5.1.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049534"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"aldehydo-D-ribose 5-phosphate + D-glyceraldehyde 3-phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + phosphate + 3 H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:31507"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58273"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:59776"},{"database":"ChEBI","id":"CHEBI:597326"}],"ecNumber":"4.3.3.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047992"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Cofactor biosynthesis; pyridoxal 5'-phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064749"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"In the presence of PdxS, forms a dodecamer of heterodimers. Only shows activity in the heterodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008345"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"value":"Belongs to the glutaminase PdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"value":"Belongs to the glutamine amidotransferase pdxT/SNO family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245114.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":181,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Active site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"Charge relay system","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-1"}]},{"type":"Binding site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":57,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":116,"modifier":"EXACT"},"end":{"value":116,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005639-2"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01615"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00480"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000235","properties":[{"key":"ProteinId","value":"MBB1245114.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182856446.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000235.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:1903600","properties":[{"key":"GoTerm","value":"C:glutaminase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036381","properties":[{"key":"GoTerm","value":"F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016740","properties":[{"key":"GoTerm","value":"F:transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006543","properties":[{"key":"GoTerm","value":"P:L-glutamine catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042823","properties":[{"key":"GoTerm","value":"P:pyridoxal 5'-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008614","properties":[{"key":"GoTerm","value":"P:pyridoxine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01749","properties":[{"key":"EntryName","value":"GATase1_PB"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000010","properties":[{"key":"EntryName","value":"uncharacterized protein LOC100176842 isoform X2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01615","properties":[{"key":"EntryName","value":"PdxT"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002161","properties":[{"key":"EntryName","value":"PdxT/SNO"}]},{"database":"InterPro","id":"IPR021196","properties":[{"key":"EntryName","value":"PdxT/SNO_CS"}]},{"database":"NCBIfam","id":"TIGR03800","properties":[{"key":"EntryName","value":"PLP_synth_Pdx2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR31559:SF0","properties":[{"key":"EntryName","value":"PYRIDOXAL 5'-PHOSPHATE SYNTHASE SUBUNIT SNO1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01174","properties":[{"key":"EntryName","value":"SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005639","properties":[{"key":"EntryName","value":"Glut_amidoT_SNO"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51274","properties":[{"key":"EntryName","value":"GATASE_COBBQ"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01236","properties":[{"key":"EntryName","value":"PDXT_SNO_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51130","properties":[{"key":"EntryName","value":"PDXT_SNO_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSTEATTSQPVVGVLALQGDVREHLAALRAAGADAREVRRPEELAAVDGLVIPGGESTTMSKLATIFGLLEPLRERVRSGMPAYGSCAGMIMLADKILDPRSGQETVGGIDMIVRRNAFGRQNESFEASLEVAGLEGGPVEGVFIRAPWVESTGAATEVLATYDGHPVAVRQGALLATSFHPELTGDHRVHRLFTDMVRAAAPAR","length":205,"molWeight":21700,"crc64":"15AE90324A6E85AA","md5":"684712FC7F470D8A7CE5FD9DF5D2E6A6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI00160430A0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6EL23","uniProtkbId":"A0ABR6EL23_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245848.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Riboflavin biosynthesis protein RibBA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"4.1.99.12"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase II"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245848.1"}],"value":"ribB"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"ribBA"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245848.1"}],"value":"GL263_20155"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002284"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043932"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Catalyzes the conversion of GTP to 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate (DARP), formate and pyrophosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-ribulose 5-phosphate = (2S)-2-hydroxy-3-oxobutyl phosphate + formate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18457"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:58121"},{"database":"ChEBI","id":"CHEBI:58830"}],"ecNumber":"4.1.99.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"GTP + 4 H2O = 2,5-diamino-6-hydroxy-4-(5-phosphoribosylamino)-pyrimidine + formate + 2 phosphate + 3 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23704"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15740"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58614"}],"ecNumber":"3.5.4.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049295"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}},{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 2 divalent metal cations per subunit. Magnesium or manganese."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004904"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004853"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Cofactor biosynthesis; riboflavin biosynthesis; 5-amino-6-(D-ribitylamino)uracil from GTP: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the C-terminal section; belongs to the GTP cyclohydrolase II family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005520"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"In the N-terminal section; belongs to the DHBP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1245848.1"}],"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":258,"modifier":"EXACT"},"end":{"value":424,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"DHBP synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":382,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"Proton acceptor; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Active site","location":{"start":{"value":384,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":47,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":48,"modifier":"EXACT"},"end":{"value":48,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":52,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":309,"modifier":"EXACT"},"end":{"value":309,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":320,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":322,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":325,"modifier":"EXACT"},"end":{"value":325,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":348,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":370,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":405,"modifier":"EXACT"},"end":{"value":405,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":410,"modifier":"EXACT"},"end":{"value":410,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022619"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0686","category":"Biological process","name":"Riboflavin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000357","properties":[{"key":"ProteinId","value":"MBB1245848.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182857142.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000357.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01283","properties":[{"key":"EntryName","value":"RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"InterPro","id":"IPR016299","properties":[{"key":"EntryName","value":"Riboflavin_synth_RibBA"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTALSSLGQYLPAAEPVDEDLTLDPIERAIADIAAGRPVVVVDDEDRENEGDLVVAAEKATPEIIAFMMSECRGLICVPMEGPELDRLELPQMVGRNTESMSTAFTVSVDASAAHGVSTGISAADRATTIALLADPTAVADDFVRPGHVFPLRAREGGVLVRQGHTEAGVDLARLAGLRPAAAIVEIADRDGTMMRLPRLVPFAREHGLAIVSIADLVEYRRAREEAADPTPEAAAPAERAAVPAAARPVPLPAVLREAETRLPTAYGEFRAFGYRSTADGVEHIALVAGDIKDDQDGEDVLVRMHSECLTGDILASHRCDCGPQLAESLRRIQAEGRGVLVYLRGHEGRGIGLLPKLRAYELQERGRDTLDANVELGLPADARDYAAGARILTDLGVRSLRLLTNNPEKARALGDHGLLVTAREAVPVQAGEHNLHYLRTKRDRMGHDLPWLEEAAEVAGPHFAGALSACRS","length":473,"molWeight":50652,"crc64":"00F11A3C0DB8EC2B","md5":"9CE06482BB84BF1D6674589C2A6E23EC"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Active site":2,"Binding site":16,"Site":2},"uniParcId":"UPI0016008EC8"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9E7","uniProtkbId":"A0ABR6E9E7_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241976.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00015938"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR02402"}],"value":"Malto-oligosyltrehalose trehalohydrolase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}],"value":"MTHase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012268"},{"evidenceCode":"ECO:0000256","source":"NCBIfam","id":"TIGR02402"}],"value":"3.2.1.141"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033284"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}],"value":"4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00032057"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}],"value":"Maltooligosyl trehalose trehalohydrolase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241976.1"}],"value":"treZ"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241976.1"}],"value":"GL263_00060"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-[(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-alpha-D-glucan.","ecNumber":"3.2.1.141","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005199"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}],"value":"Glycan biosynthesis; trehalose biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006337-1"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008061"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}],"value":"Belongs to the glycosyl hydrolase 13 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241976.1"}],"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":98,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Glycosyl hydrolase family 13 catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00642"}]},{"type":"Active site","location":{"start":{"value":244,"modifier":"EXACT"},"end":{"value":244,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006337-1"}]},{"type":"Active site","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":281,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006337-1"}]},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006337-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":306,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006337-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":383,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006337-2"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":379,"modifier":"EXACT"},"end":{"value":379,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR006337-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023295"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}],"id":"KW-0326","category":"Molecular function","name":"Glycosidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006337"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000001","properties":[{"key":"ProteinId","value":"MBB1241976.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853417.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000001.1"}]},{"database":"Proteomes","id":"UP000766698","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:0033942","properties":[{"key":"GoTerm","value":"F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005992","properties":[{"key":"GoTerm","value":"P:trehalose biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd11325","properties":[{"key":"EntryName","value":"AmyAc_GTHase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd02853","properties":[{"key":"EntryName","value":"E_set_MTHase_like_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.760","properties":[{"key":"EntryName","value":"E-set domains of sugar-utilizing enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.80","properties":[{"key":"EntryName","value":"Glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.10","properties":[{"key":"EntryName","value":"Immunoglobulins"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006047","properties":[{"key":"EntryName","value":"GH13_cat_dom"}]},{"database":"InterPro","id":"IPR017853","properties":[{"key":"EntryName","value":"GH_hydrolase_sf"}]},{"database":"InterPro","id":"IPR013783","properties":[{"key":"EntryName","value":"Ig-like_fold"}]},{"database":"InterPro","id":"IPR014756","properties":[{"key":"EntryName","value":"Ig_E-set"}]},{"database":"InterPro","id":"IPR012768","properties":[{"key":"EntryName","value":"Trehalose_TreZ"}]},{"database":"InterPro","id":"IPR044901","properties":[{"key":"EntryName","value":"Trehalose_TreZ_E-set_sf"}]},{"database":"NCBIfam","id":"TIGR02402","properties":[{"key":"EntryName","value":"trehalose_TreZ"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43651","properties":[{"key":"EntryName","value":"1,4-ALPHA-GLUCAN-BRANCHING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43651:SF11","properties":[{"key":"EntryName","value":"MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00128","properties":[{"key":"EntryName","value":"Alpha-amylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006337","properties":[{"key":"EntryName","value":"Trehalose_TreZ"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00642","properties":[{"key":"EntryName","value":"Aamy"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51445","properties":[{"key":"EntryName","value":"(Trans)glycosidases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81296","properties":[{"key":"EntryName","value":"E set domains"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLFEVWAPNAGKVELRLDGRTRPMDPDPAASGWWRLTAAATAGARYGFVLDDGPVLPDPRARRQPDGPEGLSAVVDHTAHHWHHPWPGRDLTGAVLYELHVGTFTEEGTFAAAAERLGHLADLGVSHVQLMPVCPFPGTHGWGYDGVAPWAVHEPYGGPDGLKAFVDAAHGHGLGVVLDVVHNHLGPSGNRLPEFGPYFTDRYHTPWGSAVNLDGPGSDEVRDYFVGSALAFLRDYRLDGLRLDAVHALADSRAEHFLHQLSAAVGELSADLGRPLFLIAESDRNDPLTCTPREQNGLGLEAQWNDDFHHALHVALTGESHGYYADFARAPLATLARTLTDGFFHAGTYSSFRGRRHGRPLDRSTTPASRLLGYTQTHDQVGNRATGDRLTPALDPGLAACAAALVLCGPFTPMLFMGEEWGASTPWQYFTDHPDPELAEAVRVGRRREFADHGWPADAVPDPQDPATRARSVLDWTEPTRAPHAELLDWYRTLLAIRRTHLAPGLPLAATHVDHDEEARTLTVRHGVLAVSVNLGEGIASPAVPPGALPLAASAGAEALTLPPHSAAVFLLPPDEARQHGS","length":582,"molWeight":62876,"crc64":"DB4D116CF048CE15","md5":"99A389D20212DDE733AF5A2D7257995C"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":3,"Site":1},"uniParcId":"UPI00160113E3"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9H8","uniProtkbId":"A0ABR6E9H8_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241996.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00014413"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"Coproheme decarboxylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050019"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"1.3.98.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029882"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"Coproheme III oxidative decarboxylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00030236"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"Hydrogen peroxide-dependent heme synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"chdC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241996.1"}],"value":"GL263_00160"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"Involved in coproporphyrin-dependent heme b biosynthesis. Catalyzes the decarboxylation of Fe-coproporphyrin III (coproheme) to heme b (protoheme IX), the last step of the pathway. The reaction occurs in a stepwise manner with a three-propionate intermediate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Fe-coproporphyrin III + 2 H2O2 + 2 H(+) = heme b + 2 CO2 + 4 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:56516"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:68438"}],"ecNumber":"1.3.98.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049896"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:56517"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049896"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Fe-coproporphyrin III + H2O2 + H(+) = harderoheme III + CO2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57940"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:68438"},{"database":"ChEBI","id":"CHEBI:142463"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"harderoheme III + H2O2 + H(+) = heme b + CO2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:57944"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:142463"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Fe-coproporphyrin III","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:68438"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"Fe-coproporphyrin III acts as both substrate and redox cofactor."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"Porphyrin-containing compound metabolism; protoheme biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"value":"Belongs to the ChdC family. Type 2 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241996.1"}],"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":140,"modifier":"EXACT"},"end":{"value":140,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}]},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:68438"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"ligand":{"name":"Fe-coproporphyrin III","id":"ChEBI:CHEBI:68438"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"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_02244"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02244"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000001","properties":[{"key":"ProteinId","value":"MBB1241996.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853432.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000001.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016634","properties":[{"key":"GoTerm","value":"F:oxidoreductase activity, acting on the CH-CH group of donors, oxygen as acceptor"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006785","properties":[{"key":"GoTerm","value":"P:heme B biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.70.1030","properties":[{"key":"EntryName","value":"Apc35880, domain 1"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_02244","properties":[{"key":"EntryName","value":"Coproheme_decarbox_2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010644","properties":[{"key":"EntryName","value":"ChdC/CLD"}]},{"database":"InterPro","id":"IPR011008","properties":[{"key":"EntryName","value":"Dimeric_a/b-barrel"}]},{"database":"NCBIfam","id":"NF042928","properties":[{"key":"EntryName","value":"HemQ_actino"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36843:SF1","properties":[{"key":"EntryName","value":"COPROHEME DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR36843","properties":[{"key":"EntryName","value":"HEME-DEPENDENT PEROXIDASE YWFI-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06778","properties":[{"key":"EntryName","value":"Chlor_dismutase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54909","properties":[{"key":"EntryName","value":"Dimeric alpha+beta barrel"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAAPEKTPNAGKRAKDLNEVIRYTLWSVFRLREALPADRAGYAEEVQELFDQLAAKDVTVRGTYDVSGLRADADVMIWWHAETSDELQTAYNLFRRTRLGRALEPVWSNMALHRPAEFNKSHIPAFLADETPREYVSVYPFVRSYDWYLLPDEDRRRMLADHGKMARGFPDVRANTVASFSLGDYEWILAFEADELYRIVDLMRHLRGSEARMHVREEVPFYTGRRRSVAELVEGLA","length":238,"molWeight":27575,"crc64":"102B8DE19169449E","md5":"25AB1E299F0F50E3AF0CD680AD319E44"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":1,"Binding site":1},"uniParcId":"UPI0016018943"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9I0","uniProtkbId":"A0ABR6E9I0_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241998.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012288"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Uroporphyrinogen decarboxylase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"UPD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"URO-D"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012288"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"4.1.1.37"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241998.1"}],"value":"hemE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241998.1"}],"value":"GL263_00170"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Catalyzes the decarboxylation of four acetate groups of uroporphyrinogen-III to yield coproporphyrinogen-III"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"uroporphyrinogen III + 4 H(+) = coproporphyrinogen III + 4 CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19865"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57308"},{"database":"ChEBI","id":"CHEBI:57309"}],"ecNumber":"4.1.1.37","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000554"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004804"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000554"}],"value":"Porphyrin-containing compound metabolism; protoporphyrin-IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009935"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU004169"}],"value":"Belongs to the uroporphyrinogen decarboxylase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1241998.1"}],"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":32,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Uroporphyrinogen decarboxylase (URO-D)","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00906"}]},{"type":"Domain","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Uroporphyrinogen decarboxylase (URO-D)","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS00907"}]},{"type":"Binding site","location":{"start":{"value":37,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":330,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023244"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00218"}],"id":"KW-0627","category":"Biological process","name":"Porphyrin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000001","properties":[{"key":"ProteinId","value":"MBB1241998.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853434.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000001.1"}]},{"database":"Proteomes","id":"UP000766698","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:0004853","properties":[{"key":"GoTerm","value":"F:uroporphyrinogen decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006783","properties":[{"key":"GoTerm","value":"P:heme biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00717","properties":[{"key":"EntryName","value":"URO-D"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.210:FF:000005","properties":[{"key":"EntryName","value":"Uroporphyrinogen decarboxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.210","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00218","properties":[{"key":"EntryName","value":"URO_D"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR038071","properties":[{"key":"EntryName","value":"UROD/MetE-like_sf"}]},{"database":"InterPro","id":"IPR006361","properties":[{"key":"EntryName","value":"Uroporphyrinogen_deCO2ase_HemE"}]},{"database":"InterPro","id":"IPR000257","properties":[{"key":"EntryName","value":"Uroporphyrinogen_deCOase"}]},{"database":"NCBIfam","id":"TIGR01464","properties":[{"key":"EntryName","value":"hemE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21091","properties":[{"key":"EntryName","value":"METHYLTETRAHYDROFOLATE:HOMOCYSTEINE METHYLTRANSFERASE RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21091:SF169","properties":[{"key":"EntryName","value":"UROPORPHYRINOGEN DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01208","properties":[{"key":"EntryName","value":"URO-D"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51726","properties":[{"key":"EntryName","value":"UROD/MetE-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00906","properties":[{"key":"EntryName","value":"UROD_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00907","properties":[{"key":"EntryName","value":"UROD_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSVDDRPTGPQRKTADSAFVRACRREPVPHTPVWFMRQAGRSLPEYRKVREGVAMLDSCMRPDLVTEITLQPVRRHGVDAAIYFSDIVVPLKAIGVDLDIKPGVGPVVDRPIRSRADLERLRPLEPDDVSYVTEAIGMLTGELGTTPLIGFAGAPFTLASYLVEGGPSRNHEHTKALMYGDPELWADLLDRLADITAAFLEVQIRAGASAVQLFDSWVGALAPRDYRELVMPASEKVFRAVEHHGVPRIHFGVGTGELLGLLGEAGADVVGVDWRVPLDEAARRVGPGRALQGNLDPAVLFAPRDAVERQADRVLEAAASLEGHVFNLGHGVLPDTDPDALTRLVEYVHERTAR","length":354,"molWeight":38642,"crc64":"E92B478F70C79776","md5":"F7AB9016EF2E65EA8750116350AD0FD4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":5,"Site":1},"uniParcId":"UPI00160078E0"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9L8","uniProtkbId":"A0ABR6E9L8_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242035.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00019397"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"value":"Triosephosphate isomerase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"value":"TIM"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"value":"TPI"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011940"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"value":"5.3.1.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"value":"Triose-phosphate isomerase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"value":"tpiA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242035.1"}],"value":"GL263_00355"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00055680"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"value":"Involved in the gluconeogenesis. Catalyzes stereospecifically the conversion of dihydroxyacetone phosphate (DHAP) to D-glyceraldehyde-3-phosphate (G3P)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glyceraldehyde 3-phosphate = dihydroxyacetone phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18585"},{"database":"ChEBI","id":"CHEBI:57642"},{"database":"ChEBI","id":"CHEBI:59776"}],"ecNumber":"5.3.1.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000474"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004742"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Carbohydrate degradation; glycolysis; D-glyceraldehyde 3-phosphate from glycerone phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007422"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU363013"}],"value":"Belongs to the triosephosphate isomerase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242035.1"}],"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":101,"modifier":"EXACT"},"end":{"value":101,"modifier":"EXACT"}},"description":"Electrophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}]},{"type":"Active site","location":{"start":{"value":173,"modifier":"EXACT"},"end":{"value":173,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}]},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":11,"modifier":"EXACT"},"end":{"value":11,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":13,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10127"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":219,"modifier":"EXACT"},"end":{"value":219,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":240,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00147"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000003","properties":[{"key":"ProteinId","value":"MBB1242035.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853473.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000003.1"}]},{"database":"Proteomes","id":"UP000766698","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:0004807","properties":[{"key":"GoTerm","value":"F:triose-phosphate isomerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046166","properties":[{"key":"GoTerm","value":"P:glyceraldehyde-3-phosphate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019563","properties":[{"key":"GoTerm","value":"P:glycerol catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006096","properties":[{"key":"GoTerm","value":"P:glycolytic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00311","properties":[{"key":"EntryName","value":"TIM"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000020","properties":[{"key":"EntryName","value":"Triosephosphate isomerase"},{"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_00147_B","properties":[{"key":"EntryName","value":"TIM_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR035990","properties":[{"key":"EntryName","value":"TIM_sf"}]},{"database":"InterPro","id":"IPR022896","properties":[{"key":"EntryName","value":"TrioseP_Isoase_bac/euk"}]},{"database":"InterPro","id":"IPR000652","properties":[{"key":"EntryName","value":"Triosephosphate_isomerase"}]},{"database":"InterPro","id":"IPR020861","properties":[{"key":"EntryName","value":"Triosephosphate_isomerase_AS"}]},{"database":"NCBIfam","id":"TIGR00419","properties":[{"key":"EntryName","value":"tim"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21139","properties":[{"key":"EntryName","value":"TRIOSEPHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21139:SF42","properties":[{"key":"EntryName","value":"TRIOSEPHOSPHATE ISOMERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00121","properties":[{"key":"EntryName","value":"TIM"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51351","properties":[{"key":"EntryName","value":"Triosephosphate isomerase (TIM)"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00171","properties":[{"key":"EntryName","value":"TIM_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51440","properties":[{"key":"EntryName","value":"TIM_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSRTPIMAGNWKMNLNHLEAISHVQKLAFTLDDKDYEGTEVVVLPPFTDLRSVQSLVNGDKLKIGFGAQDISVHDSGAYTGEVSGPMLAKLNCSYVVVGHSERRQYHGEDEAVCNAKVKAAFRNEIVPILCVGEGLDVRKAGNQVAHTLAQVDGALEGVPAEQAERLVIAYEPVWAIGTGEVATPEDAQEVCGAIRGRLAELYHQDVADKVRIQYGGSVKGDNVNAIMSQPDVDGALVGGASLNADEFAKIVRFRDQ","length":258,"molWeight":27758,"crc64":"5264461055C8EB2D","md5":"ADC2E27BFBE1E2D2BBEF350E652F4D59"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Active site":2,"Binding site":6},"uniParcId":"UPI0015FFBDA2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9M2","uniProtkbId":"A0ABR6E9M2_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242044.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Glucose-6-phosphate 1-dehydrogenase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"G6PD"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"1.1.1.49"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"zwf"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242044.1"}],"value":"GL263_00400"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Catalyzes the oxidation of glucose 6-phosphate to 6-phosphogluconolactone"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glucose 6-phosphate + NADP(+) = 6-phospho-D-glucono-1,5-lactone + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15841"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:57955"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:61548"}],"ecNumber":"1.1.1.49","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004937"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Carbohydrate degradation; pentose phosphate pathway; D-ribulose 5-phosphate from D-glucose 6-phosphate (oxidative stage): step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Belongs to the glucose-6-phosphate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242044.1"}],"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":214,"modifier":"EXACT"}},"description":"Glucose-6-phosphate dehydrogenase NAD-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00479"}]},{"type":"Domain","location":{"start":{"value":216,"modifier":"EXACT"},"end":{"value":511,"modifier":"EXACT"}},"description":"Glucose-6-phosphate dehydrogenase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02781"}]},{"type":"Active site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":267,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}]},{"type":"Binding site","location":{"start":{"value":68,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58349"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"NADP(+)","id":"ChEBI:CHEBI:58349"}},{"type":"Binding site","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10005"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022526"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0313","category":"Biological process","name":"Glucose metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00966"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000003","properties":[{"key":"ProteinId","value":"MBB1242044.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"Proteomes","id":"UP000766698","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:0004345","properties":[{"key":"GoTerm","value":"F:glucose-6-phosphate dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006006","properties":[{"key":"GoTerm","value":"P:glucose metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009051","properties":[{"key":"GoTerm","value":"P:pentose-phosphate shunt, oxidative branch"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"3.30.360.10:FF:000011","properties":[{"key":"EntryName","value":"Glucose-6-phosphate 1-dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.360.10","properties":[{"key":"EntryName","value":"Dihydrodipicolinate Reductase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00966","properties":[{"key":"EntryName","value":"G6PD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR001282","properties":[{"key":"EntryName","value":"G6P_DH"}]},{"database":"InterPro","id":"IPR019796","properties":[{"key":"EntryName","value":"G6P_DH_AS"}]},{"database":"InterPro","id":"IPR022675","properties":[{"key":"EntryName","value":"G6P_DH_C"}]},{"database":"InterPro","id":"IPR022674","properties":[{"key":"EntryName","value":"G6P_DH_NAD-bd"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00871","properties":[{"key":"EntryName","value":"zwf"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23429:SF0","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23429","properties":[{"key":"EntryName","value":"GLUCOSE-6-PHOSPHATE 1-DEHYDROGENASE G6PD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02781","properties":[{"key":"EntryName","value":"G6PD_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00479","properties":[{"key":"EntryName","value":"G6PD_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000110","properties":[{"key":"EntryName","value":"G6PD"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00079","properties":[{"key":"EntryName","value":"G6PDHDRGNASE"}]},{"database":"SUPFAM","id":"SSF55347","properties":[{"key":"EntryName","value":"Glyceraldehyde-3-phosphate dehydrogenase-like, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00069","properties":[{"key":"EntryName","value":"G6P_DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSGESGVPSVNLLRDAQDRRLPRIAGPSGLVIFGVTGDLSRKKLMPAVYDLANRGLLPPGFSLVGFARRDWEHEDFAQVVRDAVREHARTPFREEVWEQLAQGMRFVPGVFDDDEAFSTLKNTIEALDKERGTGGNFAFYLSVPPKFFPTVVQQLKKHGLSDAPEGSWRRAVVEKPFGHDLKSAQELNQVVHGVFRASQVFRIDHYLGKETVQNILALRFANTMFEPLWNRSYVDHVQITMAEDIGIGGRAGYYDGIGSARDVIQNHLLQLLALTAMEEPSSFGAKALVQEKLKVLNAVRLPDDLGLHTVRGQYTAGWQGGEKVPGYLDEEGINPHSKTDTYAAIKLEIDNRRWAGVPFYLRTGKRLGRRVTEIAVVFQRAPYSPFNATDTQELGQNALVIRVQPDEGVTIRFGSKVPGTSMEIRDVTMDFAYGESFTESSPEAYERLILDVLLGDANLFPRHQEVERSWEILDPVEEYWEAHGRPEPYVAGTWGPKAADEMLKRDGRSWRRP","length":513,"molWeight":57650,"crc64":"39A25CE34C0071BB","md5":"B9ABD1A9851FF599303CCEA1E13B0234"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":7},"uniParcId":"UPI0016025C05"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9N7","uniProtkbId":"A0ABR6E9N7_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242059.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"2.3.1.117"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"Tetrahydrodipicolinate N-succinyltransferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"THDP succinyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"THP succinyltransferase"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"Tetrahydropicolinate succinylase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242059.1"}],"value":"dapD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242059.1"}],"value":"GL263_00475"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"Catalyzes the conversion of the cyclic tetrahydrodipicolinate (THDP) into the acyclic N-succinyl-L-2-amino-6-oxopimelate using succinyl-CoA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(S)-2,3,4,5-tetrahydrodipicolinate + succinyl-CoA + H2O = (S)-2-succinylamino-6-oxoheptanedioate + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17325"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15685"},{"database":"ChEBI","id":"CHEBI:16845"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57292"}],"ecNumber":"2.3.1.117","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate (succinylase route): step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011233"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"value":"Belongs to the type 2 tetrahydrodipicolinate N-succinyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242059.1"}],"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":120,"modifier":"EXACT"},"end":{"value":160,"modifier":"EXACT"}},"description":"2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase middle","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14789"}]},{"type":"Active site","location":{"start":{"value":209,"modifier":"EXACT"},"end":{"value":209,"modifier":"EXACT"}},"description":"Acyl-anhydride intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}]},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1","note":"ligand shared between trimeric partners"}},{"type":"Binding site","location":{"start":{"value":193,"modifier":"EXACT"},"end":{"value":193,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2","note":"ligand shared between trimeric partners"}},{"type":"Binding site","location":{"start":{"value":211,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}},{"type":"Binding site","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":226,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}},{"type":"Binding site","location":{"start":{"value":229,"modifier":"EXACT"},"end":{"value":229,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}},{"type":"Binding site","location":{"start":{"value":252,"modifier":"EXACT"},"end":{"value":252,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}},{"type":"Binding site","location":{"start":{"value":267,"modifier":"EXACT"},"end":{"value":268,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}},{"type":"Binding site","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":287,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}},{"type":"Binding site","location":{"start":{"value":300,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57292"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"ligand":{"name":"succinyl-CoA","id":"ChEBI:CHEBI:57292"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"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_02122"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022915"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"id":"KW-0220","category":"Biological process","name":"Diaminopimelate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02122"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"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_02122"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000003","properties":[{"key":"ProteinId","value":"MBB1242059.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853493.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000003.1"}]},{"database":"Proteomes","id":"UP000766698","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:0008666","properties":[{"key":"GoTerm","value":"F:2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase 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":"CDD","id":"cd04649","properties":[{"key":"EntryName","value":"LbH_THP_succinylT_putative"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.160.10.10:FF:000009","properties":[{"key":"EntryName","value":"2,3,4,5-tetrahydropyridine-2,6-dicarboxylate N-succinyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.2010","properties":[{"key":"EntryName","value":"-"},{"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":"3.30.60.70","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02122","properties":[{"key":"EntryName","value":"DapD_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR019875","properties":[{"key":"EntryName","value":"DapD_actinobacteria"}]},{"database":"InterPro","id":"IPR001451","properties":[{"key":"EntryName","value":"Hexapep"}]},{"database":"InterPro","id":"IPR032784","properties":[{"key":"EntryName","value":"THDPS_M"}]},{"database":"InterPro","id":"IPR038361","properties":[{"key":"EntryName","value":"THDPS_M_sf"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"InterPro","id":"IPR026586","properties":[{"key":"EntryName","value":"Type2_DapD"}]},{"database":"NCBIfam","id":"TIGR03535","properties":[{"key":"EntryName","value":"DapD_actino"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14602","properties":[{"key":"EntryName","value":"Hexapep_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14789","properties":[{"key":"EntryName","value":"THDPS_M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTDATHRTTGAVAAGLATVTADGTVLDTWFPAPELTAEPGPAGTERLTAERAAELLGDAAPKALGPDPLRGVEVIAVRTTLASLDDKPLDAHDAYLRLHLISHRLVKPHGLSLDGVFGLLANVAWTSLGPVAVDSLEQVRLAARAEGRHLTVTSVDKFPRMTDYVVPKGVRIGDADRVRLGAHLAEGTTVMHEGFVNFNAGTLGTSMVEGRISAGVVVGDGSDIGGGASIMGTLSGGGKQTISLGEHCLLGAEAGIGISLGDDCIVEAGLYVTAGTRVTLPDGKVVKALELSGVTNLLFRRNSTTGVVEALPRSGSWGGLNEALHSHN","length":328,"molWeight":33765,"crc64":"FEF0BD0FC213A765","md5":"239BD196F7E0768CB2C99DD3FF850DCB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":10},"uniParcId":"UPI00160181D1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9Q1","uniProtkbId":"A0ABR6E9Q1_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242061.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012086"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"4-hydroxy-tetrahydrodipicolinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"HTPA synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012086"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"4.3.3.7"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242061.1"}],"value":"dapA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242061.1"}],"value":"GL263_00485"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003294"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"Catalyzes the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy-tetrahydrodipicolinate (HTPA)"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-aspartate 4-semialdehyde + pyruvate = (2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate + H2O + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:34171"},{"database":"ChEBI","id":"CHEBI:15361"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:67139"},{"database":"ChEBI","id":"CHEBI:537519"}],"ecNumber":"4.3.3.7","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047836"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005120"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"Homotetramer; dimer of dimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007592"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR001365"}],"value":"Belongs to the DapA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242061.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"value":"Was originally thought to be a dihydrodipicolinate synthase (DHDPS), catalyzing the condensation of (S)-aspartate-beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate (DHDP). However, it was shown in E.coli that the product of the enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that the consecutive dehydration reaction leading to DHDP is not spontaneous but catalyzed by DapB"}],"commentType":"CAUTION"}],"features":[{"type":"Active site","location":{"start":{"value":138,"modifier":"EXACT"},"end":{"value":138,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001365-1"}]},{"type":"Active site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001365-1"}]},{"type":"Binding site","location":{"start":{"value":50,"modifier":"EXACT"},"end":{"value":50,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15361"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001365-2"}],"ligand":{"name":"pyruvate","id":"ChEBI:CHEBI:15361"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:15361"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR001365-2"}],"ligand":{"name":"pyruvate","id":"ChEBI:CHEBI:15361"}},{"type":"Site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Part of a proton relay during catalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}]},{"type":"Site","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":112,"modifier":"EXACT"}},"description":"Part of a proton relay during catalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"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_00418"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022915"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"id":"KW-0220","category":"Biological process","name":"Diaminopimelate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023154"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"id":"KW-0457","category":"Biological process","name":"Lysine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00418"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000003","properties":[{"key":"ProteinId","value":"MBB1242061.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853495.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000003.1"}]},{"database":"Proteomes","id":"UP000766698","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:0008840","properties":[{"key":"GoTerm","value":"F:4-hydroxy-tetrahydrodipicolinate synthase activity"},{"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":"cd00950","properties":[{"key":"EntryName","value":"DHDPS"},{"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_00418","properties":[{"key":"EntryName","value":"DapA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR005263","properties":[{"key":"EntryName","value":"DapA"}]},{"database":"InterPro","id":"IPR002220","properties":[{"key":"EntryName","value":"DapA-like"}]},{"database":"InterPro","id":"IPR020624","properties":[{"key":"EntryName","value":"Schiff_base-form_aldolases_CS"}]},{"database":"NCBIfam","id":"TIGR00674","properties":[{"key":"EntryName","value":"dapA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12128:SF66","properties":[{"key":"EntryName","value":"4-HYDROXY-2-OXOGLUTARATE ALDOLASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12128","properties":[{"key":"EntryName","value":"DIHYDRODIPICOLINATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00701","properties":[{"key":"EntryName","value":"DHDPS"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001365","properties":[{"key":"EntryName","value":"DHDPS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00146","properties":[{"key":"EntryName","value":"DHPICSNTHASE"}]},{"database":"SMART","id":"SM01130","properties":[{"key":"EntryName","value":"DHDPS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00665","properties":[{"key":"EntryName","value":"DHDPS_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSGPFGRLAAAMITPFGDDGALDLPGARRLAAHLVDRGGCDALVVNGTTGESVTTSDAEKLALLRAVLAEVGDRATVTAGVGSADTRHTVELARASEEAGAHGLLVVTPYYSRPTQEMVAHHLATVADATALPVLLYDIPERTGAGTALTPETLRRLAEHPKVAGVKDCSHDLLGAGRTIAETGLALYAGADEEILPLRAIGAAGAVSTVAHVAGPLVREMLDAFDAGDVGTARERHQALLPLLDAMRAVPGTVAVKALYGAAGLPGGPVRGPLLPAGADVVERLVTALRRTMGG","length":296,"molWeight":30155,"crc64":"07412AB1A968E872","md5":"B9A1DA17BD49A85705BFB469247617DA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Active site":2,"Binding site":2,"Site":2},"uniParcId":"UPI0016010515"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9Q2","uniProtkbId":"A0ABR6E9Q2_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242075.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Uridylate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"UK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"2.7.4.22"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Uridine monophosphate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"UMP kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"UMPK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"pyrH"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242075.1"}],"value":"GL263_00555"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Catalyzes the reversible phosphorylation of UMP to UDP"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UMP + ATP = UDP + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24400"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:57865"},{"database":"ChEBI","id":"CHEBI:58223"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.4.22","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047767"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Allosterically activated by GTP. Inhibited by UTP"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004791"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Homohexamer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007614"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Belongs to the UMP kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242075.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":13,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"Aspartate/glutamate/uridylate kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00696"}]},{"type":"Region","location":{"start":{"value":25,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Involved in allosteric activation by GTP","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}]},{"type":"Binding site","location":{"start":{"value":17,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":59,"modifier":"EXACT"},"end":{"value":59,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57865"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"UMP","id":"ChEBI:CHEBI:57865"}},{"type":"Binding site","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":60,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":64,"modifier":"EXACT"},"end":{"value":64,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":79,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57865"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"UMP","id":"ChEBI:CHEBI:57865"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57865"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"UMP","id":"ChEBI:CHEBI:57865"}},{"type":"Binding site","location":{"start":{"value":168,"modifier":"EXACT"},"end":{"value":168,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":174,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":177,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01220"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000004","properties":[{"key":"ProteinId","value":"MBB1242075.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853512.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000004.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0033862","properties":[{"key":"GoTerm","value":"F:UMP kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006225","properties":[{"key":"GoTerm","value":"P:UDP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04254","properties":[{"key":"EntryName","value":"AAK_UMPK-PyrH-Ec"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1160.10:FF:000001","properties":[{"key":"EntryName","value":"Uridylate kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1160.10","properties":[{"key":"EntryName","value":"Acetylglutamate kinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01220_B","properties":[{"key":"EntryName","value":"PyrH_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036393","properties":[{"key":"EntryName","value":"AceGlu_kinase-like_sf"}]},{"database":"InterPro","id":"IPR001048","properties":[{"key":"EntryName","value":"Asp/Glu/Uridylate_kinase"}]},{"database":"InterPro","id":"IPR011817","properties":[{"key":"EntryName","value":"Uridylate_kinase"}]},{"database":"InterPro","id":"IPR015963","properties":[{"key":"EntryName","value":"Uridylate_kinase_bac"}]},{"database":"NCBIfam","id":"TIGR02075","properties":[{"key":"EntryName","value":"pyrH_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42833","properties":[{"key":"EntryName","value":"URIDYLATE KINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42833:SF4","properties":[{"key":"EntryName","value":"URIDYLATE KINASE PUMPKIN, CHLOROPLASTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00696","properties":[{"key":"EntryName","value":"AA_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005650","properties":[{"key":"EntryName","value":"Uridylate_kin"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53633","properties":[{"key":"EntryName","value":"Carbamate kinase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSKETDNDSSRRFLLKLSGEAFAGGGGLGVDPDVVHKIAREIAAVVRDGAQIAVVIGGGNFFRGAELQQRGMDRARSDYMGMLGTVMNCLALQDFLEKEGIDSRVQTAITMGQVAEPYIPLRAIRHLEKGRVVIFGAGMGMPYFSTDTTAAQRALEIHAEAMLMGKNGVDGVYDSDPAKNPDAVKFDSLSYDEVIARDLKVADLTAITLCRDNGLPIVVFELLAEGNIARAVKSEKIGTLVGVQAPRD","length":249,"molWeight":26705,"crc64":"A29DC5DC1D3C443A","md5":"608676D8187254E49EF00C2B600A4D3D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Binding site":9},"uniParcId":"UPI001602B587"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9R6","uniProtkbId":"A0ABR6E9R6_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242088.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Signal peptidase I"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"3.4.21.89"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242088.1"}],"value":"lepB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242088.1"}],"value":"GL263_00620"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.","ecNumber":"3.4.21.89","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000677"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004401"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004401"}],"value":"Single-pass type II membrane protein","id":"SL-9906"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Single-pass type II membrane protein","id":"SL-9906"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009370"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Belongs to the peptidase S26 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242088.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":27,"modifier":"EXACT"},"end":{"value":49,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}]},{"type":"Domain","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"Peptidase S26","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10502"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":155,"modifier":"EXACT"},"end":{"value":174,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600223-1"}]},{"type":"Active site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600223-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000004","properties":[{"key":"ProteinId","value":"MBB1242088.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853521.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000004.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009003","properties":[{"key":"GoTerm","value":"F:signal peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0051604","properties":[{"key":"GoTerm","value":"P:protein maturation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06530","properties":[{"key":"EntryName","value":"S26_SPase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.10.109.10","properties":[{"key":"EntryName","value":"Umud Fragment, subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036286","properties":[{"key":"EntryName","value":"LexA/Signal_pep-like_sf"}]},{"database":"InterPro","id":"IPR000223","properties":[{"key":"EntryName","value":"Pept_S26A_signal_pept_1"}]},{"database":"InterPro","id":"IPR019758","properties":[{"key":"EntryName","value":"Pept_S26A_signal_pept_1_CS"}]},{"database":"InterPro","id":"IPR019533","properties":[{"key":"EntryName","value":"Peptidase_S26"}]},{"database":"NCBIfam","id":"TIGR02227","properties":[{"key":"EntryName","value":"sigpep_I_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43390:SF1","properties":[{"key":"EntryName","value":"CHLOROPLAST PROCESSING PEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43390","properties":[{"key":"EntryName","value":"SIGNAL PEPTIDASE I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10502","properties":[{"key":"EntryName","value":"Peptidase_S26"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00727","properties":[{"key":"EntryName","value":"LEADERPTASE"}]},{"database":"SUPFAM","id":"SSF51306","properties":[{"key":"EntryName","value":"LexA/Signal peptidase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00761","properties":[{"key":"EntryName","value":"SPASE_I_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MENDQPRLPERDRDPAPDRGRDPRSRFVRTGVLAALLLLAYATFSGLVAQPYAVPTGSMENTLRPGDRLLVNKLAYRFGNDPARGDVVVFDGGDTFGATGRESDPLPRLLRSAGASVGLVPPAGSDYVKRVVGTGGDRVRCCDARGRIEVNGQPIEEPYLRPGPSGAPGRASSVPFDVVVRPGRLWVMGDHRDGSEDSRHFLGHPGGGTVPVERVIGRVETVLWPPGRAGGLEGPHG","length":237,"molWeight":25286,"crc64":"9E0A6C91B3A3B62B","md5":"270E855E97FA7B01D4ACEBE2C6C6BE0C"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":2,"Compositional bias":1,"Active site":2},"uniParcId":"UPI0016019604"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9R9","uniProtkbId":"A0ABR6E9R9_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242090.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00014679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"value":"tRNA (guanine-N(1)-)-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012807"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"value":"2.1.1.228"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029736"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"value":"M1G-methyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033392"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"value":"tRNA [GM37] methyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242090.1"}],"value":"trmD"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242090.1"}],"value":"GL263_00630"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002634"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003464"}],"value":"Specifically methylates guanosine-37 in various tRNAs"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"guanosine(37) in tRNA + S-adenosyl-L-methionine = N(1)-methylguanosine(37) in tRNA + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:36899"},{"database":"Rhea","id":"RHEA-COMP:10145"},{"database":"Rhea","id":"RHEA-COMP:10147"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:73542"},{"database":"ChEBI","id":"CHEBI:74269"}],"ecNumber":"2.1.1.228","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047783"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003464"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003464"}],"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_00605"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003464"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007630"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003464"}],"value":"Belongs to the RNA methyltransferase TrmD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242090.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"tRNA methyltransferase TRMD/TRM10-type","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01746"}]},{"type":"Binding site","location":{"start":{"value":136,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000386-1"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"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_00605"}],"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_00605"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00605"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000004","properties":[{"key":"ProteinId","value":"MBB1242090.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853523.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000004.1"}]},{"database":"Proteomes","id":"UP000766698","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:0052906","properties":[{"key":"GoTerm","value":"F:tRNA (guanine(37)-N1)-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002939","properties":[{"key":"GoTerm","value":"P:tRNA N1-guanine methylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd18080","properties":[{"key":"EntryName","value":"TrmD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1270.20:FF:000002","properties":[{"key":"EntryName","value":"tRNA (guanine-N(1)-)-methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1280.10:FF:000001","properties":[{"key":"EntryName","value":"tRNA (guanine-N(1)-)-methyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1280.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1270.20","properties":[{"key":"EntryName","value":"tRNA(m1g37)methyltransferase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00605","properties":[{"key":"EntryName","value":"TrmD"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029028","properties":[{"key":"EntryName","value":"Alpha/beta_knot_MTases"}]},{"database":"InterPro","id":"IPR023148","properties":[{"key":"EntryName","value":"tRNA_m1G_MeTrfase_C_sf"}]},{"database":"InterPro","id":"IPR002649","properties":[{"key":"EntryName","value":"tRNA_m1G_MeTrfase_TrmD"}]},{"database":"InterPro","id":"IPR029026","properties":[{"key":"EntryName","value":"tRNA_m1G_MTases_N"}]},{"database":"InterPro","id":"IPR016009","properties":[{"key":"EntryName","value":"tRNA_MeTrfase_TRMD/TRM10"}]},{"database":"NCBIfam","id":"NF000648","properties":[{"key":"EntryName","value":"trmD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00088","properties":[{"key":"EntryName","value":"trmD"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46417","properties":[{"key":"EntryName","value":"TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46417:SF1","properties":[{"key":"EntryName","value":"TRNA (GUANINE-N(1)-)-METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01746","properties":[{"key":"EntryName","value":"tRNA_m1G_MT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000386","properties":[{"key":"EntryName","value":"tRNA_mtase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF75217","properties":[{"key":"EntryName","value":"alpha/beta knot"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRIDVVTIFPEYLEPLNVSLVGKARARGLLDVRLHDLRNWTHDRHHTVDDTPYGGGPGMVMKPEPWGEALDEIAASGEDKPVIVVPTPSGRPFTQRLAEELSTRPWLVFTPARYEGIDRRVVEEYAERYEVREVSIGDYVLAGGEAPVLVMVEAVARLLPGVLGNAESHRDDSFADGAMANLLEGPVYTKPPLWRGRDVPDVLLSGHHGRVERWRRDQALTRTAANRPDLLRSCDPETLDKHDRAMLAALGWHQGPDGRFGPPGETVEE","length":269,"molWeight":29971,"crc64":"1D7CE1FEAA048DBF","md5":"06A38463C9F05A66C416D4D23AEDEF37"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Binding site":1},"uniParcId":"UPI0015FEE12C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9S4","uniProtkbId":"A0ABR6E9S4_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242086.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Signal peptidase I"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013208"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"3.4.21.89"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242086.1"}],"value":"lepB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242086.1"}],"value":"GL263_00610"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Cleavage of hydrophobic, N-terminal signal or leader sequences from secreted and periplasmic proteins.","ecNumber":"3.4.21.89","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000677"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004401"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004401"}],"value":"Single-pass type II membrane protein","id":"SL-9906"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Single-pass type II membrane protein","id":"SL-9906"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009370"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"value":"Belongs to the peptidase S26 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242086.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Transmembrane","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":84,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}]},{"type":"Domain","location":{"start":{"value":60,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"Peptidase S26","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF10502"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":53,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":90,"modifier":"EXACT"},"end":{"value":90,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600223-1"}]},{"type":"Active site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR600223-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362042"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000004","properties":[{"key":"ProteinId","value":"MBB1242086.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853533.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000004.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009003","properties":[{"key":"GoTerm","value":"F:signal peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0051604","properties":[{"key":"GoTerm","value":"P:protein maturation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd06530","properties":[{"key":"EntryName","value":"S26_SPase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.10.109.10","properties":[{"key":"EntryName","value":"Umud Fragment, subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR036286","properties":[{"key":"EntryName","value":"LexA/Signal_pep-like_sf"}]},{"database":"InterPro","id":"IPR000223","properties":[{"key":"EntryName","value":"Pept_S26A_signal_pept_1"}]},{"database":"InterPro","id":"IPR019758","properties":[{"key":"EntryName","value":"Pept_S26A_signal_pept_1_CS"}]},{"database":"InterPro","id":"IPR019533","properties":[{"key":"EntryName","value":"Peptidase_S26"}]},{"database":"NCBIfam","id":"TIGR02227","properties":[{"key":"EntryName","value":"sigpep_I_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43390:SF1","properties":[{"key":"EntryName","value":"CHLOROPLAST PROCESSING PEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43390","properties":[{"key":"EntryName","value":"SIGNAL PEPTIDASE I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF10502","properties":[{"key":"EntryName","value":"Peptidase_S26"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00727","properties":[{"key":"EntryName","value":"LEADERPTASE"}]},{"database":"SUPFAM","id":"SSF51306","properties":[{"key":"EntryName","value":"LexA/Signal peptidase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00761","properties":[{"key":"EntryName","value":"SPASE_I_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAVGARSGSGEDGPEERSGDRHREQPAGADDRQGATADEPAAGGSGGRRSKARKPRSFWKELPLLIGIALVLALVIKTFLLQAFSIPSNSMQNTLQKGDRVLVDKLTPWFGSTPDRGEVIVFNDPGGWLDNPHVQENFLQKGLSFIGLMPSANEQDLIKRVIAVGGDTIECKPGASVTINGKPLDETSYLFPGNVPCERDGFGPVEVPEGRLWVMGDHRQDSLDSRYHQELPGGGTISEDDVVGRAVAIGWPPNRWGTLPVPDAFGKDFGAVAGAAPAALGVLGALPVVLWRRRRLLSEARPTD","length":304,"molWeight":32571,"crc64":"9BAEF216144F6CF5","md5":"ECDDCC134BF116DDD7BE8B208BBC4514"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":1,"Domain":1,"Region":1,"Compositional bias":1,"Active site":2},"uniParcId":"UPI0016041684"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9S8","uniProtkbId":"A0ABR6E9S8_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242096.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"Signal recognition particle protein"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"3.6.5.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"Fifty-four homolog"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242096.1"}],"value":"ffh"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242096.1"}],"value":"GL263_00665"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"Involved in targeting and insertion of nascent membrane proteins into the cytoplasmic membrane. Binds to the hydrophobic signal sequence of the ribosome-nascent chain (RNC) as it emerges from the ribosomes. The SRP-RNC complex is then targeted to the cytoplasmic membrane where it interacts with the SRP receptor FtsY"}],"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_00306"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"Part of the signal recognition particle protein translocation system, which is composed of SRP and FtsY"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"The SRP-RNC complex is targeted to the cytoplasmic membrane"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"Composed of three domains: the N-terminal N domain, which is responsible for interactions with the ribosome, the central G domain, which binds GTP, and the C-terminal M domain, which binds the RNA and the signal sequence of the RNC"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005450"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"value":"Belongs to the GTP-binding SRP family. SRP54 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242096.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"Signal recognition particle SRP54 helical bundle","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00963"}]},{"type":"Domain","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"Domain","location":{"start":{"value":100,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"SRP54-type proteins GTP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00962"}]},{"type":"Region","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":453,"modifier":"EXACT"},"end":{"value":469,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":474,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":488,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":506,"modifier":"EXACT"},"end":{"value":518,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":196,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023274"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"id":"KW-0687","category":"Molecular function","name":"Ribonucleoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023135"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00306"}],"id":"KW-0733","category":"Cellular component","name":"Signal recognition particle"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000004","properties":[{"key":"ProteinId","value":"MBB1242096.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853528.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000004.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0048500","properties":[{"key":"GoTerm","value":"C:signal recognition particle"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008312","properties":[{"key":"GoTerm","value":"F:7S RNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"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:0006614","properties":[{"key":"GoTerm","value":"P:SRP-dependent cotranslational protein targeting to membrane"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18539","properties":[{"key":"EntryName","value":"SRP_G"},{"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":"Gene3D","id":"1.10.260.30","properties":[{"key":"EntryName","value":"Signal recognition particle, SRP54 subunit, M-domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00306","properties":[{"key":"EntryName","value":"SRP54"},{"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":"IPR036891","properties":[{"key":"EntryName","value":"Signal_recog_part_SRP54_M_sf"}]},{"database":"InterPro","id":"IPR013822","properties":[{"key":"EntryName","value":"Signal_recog_particl_SRP54_hlx"}]},{"database":"InterPro","id":"IPR004125","properties":[{"key":"EntryName","value":"Signal_recog_particle_SRP54_M"}]},{"database":"InterPro","id":"IPR004780","properties":[{"key":"EntryName","value":"SRP"}]},{"database":"InterPro","id":"IPR022941","properties":[{"key":"EntryName","value":"SRP54"}]},{"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":"TIGR00959","properties":[{"key":"EntryName","value":"ffh"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11564","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE 54K PROTEIN SRP54"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11564:SF5","properties":[{"key":"EntryName","value":"SIGNAL RECOGNITION PARTICLE SUBUNIT SRP54"},{"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":"Pfam","id":"PF02978","properties":[{"key":"EntryName","value":"SRP_SPB"},{"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":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF47446","properties":[{"key":"EntryName","value":"Signal peptide-binding domain"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MFDTLSDRLAATFKNLRGKGRLSEADIDATAREIRIALLEADVALPVVRSFIKQVKERAAGAEVSKALNPAQQVIKIVNEELVGILGGETRQLRFAKRPPTVIMLAGLQGAGKTTLAGKLGQWLKSKGHSPLLVACDLQRPNAVNQLSVVAERAGVGVYAPEPGNGVGDPVRVAEDSVEYARSKQYDVVVVDTAGRLGIDEEMMRQAADIRDAVSPDEILFVVDAMIGQDAVNTAEAFRDGVGFDGVVLSKLDGDARGGAALSIAHITGRQIMFASNGEKLDDFDAFHPDRMASRILGMGDVLSLIEKAEQTFSQQEAEKMAAKLAKGPKEFTLDDFLAQMEQVRKMGSLSKLLGMMPGMGQMKDQINNLDERDVDRTAAIIKSMTPAERHDPTIINGSRRARVARGSGVDVSAVKNLVERFFEARKMMSRMAQGGGIPGMPGMPGMPGMGGGKKKGKPQKKAKGKRRSGNPMKRREEEQAAAERRAAGGGAFGLPGAGEADESFELPKEFKDMLPPK","length":518,"molWeight":55634,"crc64":"E21484BE6F80EC24","md5":"72208849627743E629D4E82386D44CEE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":1,"Compositional bias":4,"Binding site":3},"uniParcId":"UPI0016046A9C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9U3","uniProtkbId":"A0ABR6E9U3_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242111.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"Hydrogenobyrinate a,c-diamide synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"6.3.5.9"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"Hydrogenobyrinic acid a,c-diamide synthase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"cobB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242111.1"}],"value":"GL263_00740"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"Catalyzes the ATP-dependent amidation of the two carboxylate groups at positions a and c of hydrogenobyrinate, using either L-glutamine or ammonia as the nitrogen source"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogenobyrinate + 2 L-glutamine + 2 ATP + 2 H2O = hydrogenobyrinate a,c-diamide + 2 L-glutamate + 2 ADP + 2 phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12544"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:77873"},{"database":"ChEBI","id":"CHEBI:77874"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.5.9","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"Cofactor biosynthesis; adenosylcobalamin biosynthesis; cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step 9/10"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"Comprises of two domains. The C-terminal domain contains the binding site for glutamine and catalyzes the hydrolysis of this substrate to glutamate and ammonia. The N-terminal domain is anticipated to bind ATP and hydrogenobyrinate and catalyzes the ultimate synthesis of the diamide product. The ammonia produced via the glutaminase domain is probably translocated to the adjacent domain via a molecular tunnel, where it reacts with an activated intermediate"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"The a and c carboxylates of hydrogenobyrinate are activated for nucleophilic attack via formation of a phosphorylated intermediate by ATP. CobB catalyzes first the amidation of the c-carboxylate, and then that of the a-carboxylate"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"value":"Belongs to the CobB/CbiA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242111.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"CobQ/CobB/MinD/ParA nucleotide binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01656"}]},{"type":"Domain","location":{"start":{"value":260,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"CobB/CobQ-like glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07685"}]},{"type":"Active site","location":{"start":{"value":339,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}]},{"type":"Site","location":{"start":{"value":433,"modifier":"EXACT"},"end":{"value":433,"modifier":"EXACT"}},"description":"Increases nucleophilicity of active site Cys","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"id":"KW-0169","category":"Biological process","name":"Cobalamin biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00027"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000005","properties":[{"key":"ProteinId","value":"MBB1242111.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853565.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000005.1"}]},{"database":"Proteomes","id":"UP000766698","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:0042242","properties":[{"key":"GoTerm","value":"F:cobyrinic acid a,c-diamide synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0043802","properties":[{"key":"GoTerm","value":"F:hydrogenobyrinic acid a,c-diamide synthase (glutamine-hydrolysing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009236","properties":[{"key":"GoTerm","value":"P:cobalamin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05388","properties":[{"key":"EntryName","value":"CobB_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd03130","properties":[{"key":"EntryName","value":"GATase1_CobB"},{"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_00027","properties":[{"key":"EntryName","value":"CobB_CbiA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004484","properties":[{"key":"EntryName","value":"CbiA/CobB_synth"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR002586","properties":[{"key":"EntryName","value":"CobQ/CobB/MinD/ParA_Nub-bd_dom"}]},{"database":"InterPro","id":"IPR011698","properties":[{"key":"EntryName","value":"GATase_3"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"TIGR00379","properties":[{"key":"EntryName","value":"cobB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002204","properties":[{"key":"EntryName","value":"PRK01077.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43873","properties":[{"key":"EntryName","value":"COBYRINATE A,C-DIAMIDE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43873:SF1","properties":[{"key":"EntryName","value":"COBYRINATE A,C-DIAMIDE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01656","properties":[{"key":"EntryName","value":"CbiA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07685","properties":[{"key":"EntryName","value":"GATase_3"},{"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":"PS51274","properties":[{"key":"EntryName","value":"GATASE_COBBQ"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPRLVIAAPSSGSGKTTVATGLMAALTESGLDVSPHKVGPDYIDPGYHTLAVSLEGRPGRPPRPGRNLDAYLCGPERVAPLFLHGAAGADLAVVEGVMGLYDGAAGQGELASTAQVAKLLRAPVVLVVDGSSQSRSVAALVHGFATFDPEVRLAGVILNKVGSPRHEELLREALEIVGVPVLGALHRSRQVRTPSRHLGLVPAAERHAEAVEAVRAMAAQVRESVDLTALLALAHSAPPLPDEPWSPEGEGPVAGGEPVVAVAGGPAFTFSYAEHAELLAGAGARVVSFDPLRDERLPEGARALVVGGGFPEVYAAELSANEPLRAAVAAFEGPVVAECAGLLYLCRELDGSPMCGLLDARARMTDRLTLGYREAVAVADNVLAAAGTRVRGHEFHRTAVDPPAGTAPAWGVVRPERRTEGFATGRVHASYLHVHWAAEPELPRRLVAACLEGRGGR","length":457,"molWeight":47574,"crc64":"EDBAA9A4F18D4B11","md5":"4245623BC835B4EFBDB29F8A0F465FF2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"DOMAIN":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Site":1},"uniParcId":"UPI00160477AA"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABR6E9X4","uniProtkbId":"A0ABR6E9X4_9ACTN","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Streptomyces durbertensis","taxonId":2448886,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242149.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Kitasatosporales","Streptomycetaceae","Streptomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"L-Cys:GlcN-Ins ligase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"6.3.1.13"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"Mycothiol ligase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"MSH ligase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"mshC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242149.1"}],"value":"GL263_00935"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"Catalyzes the ATP-dependent condensation of GlcN-Ins and L-cysteine to form L-Cys-GlcN-Ins"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside + L-cysteine + ATP = 1D-myo-inositol 2-(L-cysteinylamino)-2-deoxy-alpha-D-glucopyranoside + AMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26176"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:35235"},{"database":"ChEBI","id":"CHEBI:58886"},{"database":"ChEBI","id":"CHEBI:58887"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.1.13","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048350"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"value":"Belongs to the class-I aminoacyl-tRNA synthetase family. MshC subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MBB1242149.1"}],"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":39,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"tRNA synthetases class I catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01406"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":30,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Motif","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"'HIGH' region","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}]},{"type":"Motif","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"'ERGGDP' region","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}]},{"type":"Motif","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":290,"modifier":"EXACT"}},"description":"'KMSKS' region","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}]},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":46,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:144924"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"L-cysteinyl-5'-AMP","id":"ChEBI:CHEBI:144924"}},{"type":"Binding site","location":{"start":{"value":43,"modifier":"EXACT"},"end":{"value":43,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":58,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:144924"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"L-cysteinyl-5'-AMP","id":"ChEBI:CHEBI:144924"}},{"type":"Binding site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:144924"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"L-cysteinyl-5'-AMP","id":"ChEBI:CHEBI:144924"}},{"type":"Binding site","location":{"start":{"value":224,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:144924"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"L-cysteinyl-5'-AMP","id":"ChEBI:CHEBI:144924"}},{"type":"Binding site","location":{"start":{"value":228,"modifier":"EXACT"},"end":{"value":228,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":246,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:144924"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"L-cysteinyl-5'-AMP","id":"ChEBI:CHEBI:144924"}},{"type":"Binding site","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":253,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":280,"modifier":"EXACT"},"end":{"value":280,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:144924"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"ligand":{"name":"L-cysteinyl-5'-AMP","id":"ChEBI:CHEBI:144924"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01697"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-B6HMQU4UM720J","citationType":"journal article","authors":["Swiecimska M.","Golinska P.","Nouioui I.","Wypij M.","Rai M.","Sangal V.","Goodfellow M."],"title":"Streptomyces alkaliterrae sp. nov., isolated from an alkaline soil, and emended descriptions of Streptomyces alkaliphilus, Streptomyces calidiresistens and Streptomyces durbertensis.","publicationDate":"2020","journal":"Syst. Appl. Microbiol.","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}],"value":"DSM 104538","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP000766698"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"WMLF01000006","properties":[{"key":"ProteinId","value":"MBB1242149.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_182853581.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_WMLF01000006.1"}]},{"database":"Proteomes","id":"UP000766698","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0035446","properties":[{"key":"GoTerm","value":"F:cysteine-glucosaminylinositol ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004817","properties":[{"key":"GoTerm","value":"F:cysteine-tRNA ligase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006423","properties":[{"key":"GoTerm","value":"P:cysteinyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0010125","properties":[{"key":"GoTerm","value":"P:mycothiol biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07955","properties":[{"key":"EntryName","value":"Anticodon_Ia_Cys_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000134","properties":[{"key":"EntryName","value":"L-cysteine:1D-myo-inositol 2-amino-2-deoxy-alpha-D-glucopyranoside ligase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.120.640","properties":[{"key":"EntryName","value":"Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01697","properties":[{"key":"EntryName","value":"MshC"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024909","properties":[{"key":"EntryName","value":"Cys-tRNA/MSH_ligase"}]},{"database":"InterPro","id":"IPR017812","properties":[{"key":"EntryName","value":"Mycothiol_ligase_MshC"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR032678","properties":[{"key":"EntryName","value":"tRNA-synt_1_cat_dom"}]},{"database":"NCBIfam","id":"TIGR03447","properties":[{"key":"EntryName","value":"mycothiol_MshC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10890:SF3","properties":[{"key":"EntryName","value":"CYSTEINE--TRNA LIGASE, CYTOPLASMIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10890","properties":[{"key":"EntryName","value":"CYSTEINYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01406","properties":[{"key":"EntryName","value":"tRNA-synt_1e"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00983","properties":[{"key":"EntryName","value":"TRNASYNTHCYS"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MHAWPASEVPALPGKGRDLRIHDSATGGRVTSAPGPVARIYVCGITPYDATHLGHAATYNAFDLVQRVWLDTKRQVHYVQNVTDVDDPLLERAQETGVPWEQLAERETALFREDMTALRMLPPQHYIGAVEAIPAIVPLVERLRDVGAAYELGGDVYFSVDADPHFGEVSRLDAEVMRRLSAERGGDPDRAGKKNPLDPLLWQAARDGEPHWDGASLGTGRPGWHIECVAIALEHLGMGFDVQGGGSDLAFPHHEMGASHAQALTGEYPFAKAYVHAGMVALHGEKMSKSKGNLVFVSALRRDGVDPAAVRLTLLAHHYRADWEYTDAVLDEATARLARWRSAVSRPDGPPAEELLAEVREALADDLDTPSALAAVDRWAERQHAEGGTDEGAPGLVSRTVDALLGVAL","length":409,"molWeight":44353,"crc64":"BDE4C41938E3B9DF","md5":"981151FAE4E93C7CFFB2D97BFD58CF70"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Motif":3,"Binding site":9},"uniParcId":"UPI0016010ACF"}}]}