{"results":[{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RB70","uniProtkbId":"A0ABV9RB70_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830814.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"RecBCD enzyme subunit RecB"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"3.1.11.5"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"5.6.2.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"DNA 3'-5' helicase subunit RecB"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Exonuclease V subunit RecB"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"ExoV subunit RecB"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Helicase/nuclease RecBCD subunit RecB"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"recB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830814.1"}],"value":"ACFPEL_00205"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"A helicase/nuclease that prepares dsDNA breaks (DSB) for recombinational DNA repair. Binds to DSBs and unwinds DNA via a highly rapid and processive ATP-dependent bidirectional helicase activity. Unwinds dsDNA until it encounters a Chi (crossover hotspot instigator) sequence from the 3' direction. Cuts ssDNA a few nucleotides 3' to the Chi site. The properties and activities of the enzyme are changed at Chi. The Chi-altered holoenzyme produces a long 3'-ssDNA overhang and facilitates RecA-binding to the ssDNA for homologous DNA recombination and repair. Holoenzyme degrades any linearized DNA that is unable to undergo homologous recombination. In the holoenzyme this subunit contributes ATPase, 3'-5' helicase, exonuclease activity and loads RecA onto ssDNA"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048988"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA by translocating in the 3'-5' direction.","ecNumber":"5.6.2.4","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.","ecNumber":"3.1.11.5","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Heterotrimer of RecB, RecC and RecD. All subunits contribute to DNA-binding. Interacts with RecA"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The C-terminal domain has nuclease activity and interacts with RecD. It interacts with RecA, facilitating its loading onto ssDNA"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"The N-terminal DNA-binding domain is a ssDNA-dependent ATPase and has ATP-dependent 3'-5' helicase function. This domain interacts with RecC"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"In the RecBCD complex, RecB has a slow 3'-5' helicase, an exonuclease activity and loads RecA onto ssDNA, RecD has a fast 5'-3' helicase activity, while RecC stimulates the ATPase and processivity of the RecB helicase and contributes to recognition of the Chi site"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"value":"Belongs to the helicase family. UvrD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830814.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":339,"modifier":"EXACT"}},"description":"UvrD-like helicase ATP-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51198"}]},{"type":"Domain","location":{"start":{"value":340,"modifier":"EXACT"},"end":{"value":637,"modifier":"EXACT"}},"description":"UvrD-like helicase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51217"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":748,"modifier":"EXACT"}},"description":"DNA-binding and helicase activity, interacts with RecC","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":799,"modifier":"EXACT"},"end":{"value":1126,"modifier":"EXACT"}},"description":"Nuclease activity, interacts with RecD and RecA","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Region","location":{"start":{"value":810,"modifier":"EXACT"},"end":{"value":846,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":1014,"modifier":"EXACT"},"end":{"value":1014,"modifier":"EXACT"}},"description":"For nuclease activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}]},{"type":"Binding site","location":{"start":{"value":24,"modifier":"EXACT"},"end":{"value":31,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00560"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":864,"modifier":"EXACT"},"end":{"value":864,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1000,"modifier":"EXACT"},"end":{"value":1000,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1014,"modifier":"EXACT"},"end":{"value":1014,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01485"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000001","properties":[{"key":"ProteinId","value":"MFC4830814.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274188880.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000001.1"}]},{"database":"Proteomes","id":"UP001595909","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:0009338","properties":[{"key":"GoTerm","value":"C:exodeoxyribonuclease V complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043138","properties":[{"key":"GoTerm","value":"F:3'-5' DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003677","properties":[{"key":"GoTerm","value":"F:DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008854","properties":[{"key":"GoTerm","value":"F:exodeoxyribonuclease V 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-UniRule"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd22352","properties":[{"key":"EntryName","value":"RecB_C-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.320.10","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":"2"}]},{"database":"Gene3D","id":"1.10.486.10","properties":[{"key":"EntryName","value":"PCRA, domain 4"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01485","properties":[{"key":"EntryName","value":"RecB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR011604","properties":[{"key":"EntryName","value":"PDDEXK-like_dom_sf"}]},{"database":"InterPro","id":"IPR038726","properties":[{"key":"EntryName","value":"PDDEXK_AddAB-type"}]},{"database":"InterPro","id":"IPR004586","properties":[{"key":"EntryName","value":"RecB"}]},{"database":"InterPro","id":"IPR011335","properties":[{"key":"EntryName","value":"Restrct_endonuc-II-like"}]},{"database":"InterPro","id":"IPR000212","properties":[{"key":"EntryName","value":"UvrD-like"}]},{"database":"InterPro","id":"IPR014016","properties":[{"key":"EntryName","value":"UvrD-like_ATP-bd"}]},{"database":"InterPro","id":"IPR014017","properties":[{"key":"EntryName","value":"UvrD-like_C"}]},{"database":"PANTHER","id":"PTHR11070:SF23","properties":[{"key":"EntryName","value":"RECBCD ENZYME SUBUNIT RECB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11070","properties":[{"key":"EntryName","value":"UVRD / RECB / PCRA DNA HELICASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12705","properties":[{"key":"EntryName","value":"PDDEXK_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00580","properties":[{"key":"EntryName","value":"UvrD-helicase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13361","properties":[{"key":"EntryName","value":"UvrD_C"},{"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":"SSF52980","properties":[{"key":"EntryName","value":"Restriction endonuclease-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51198","properties":[{"key":"EntryName","value":"UVRD_HELICASE_ATP_BIND"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51217","properties":[{"key":"EntryName","value":"UVRD_HELICASE_CTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTATLTRPFDVCGDLPSGTTVLEASAGTGKTYTIAALAARYVAEGHATLPQVMLVTFGREATRELRERVRGRFVATERALADPAGARRHDDPVIRLLAEGDDAVVALRRARLGAALAGFDAATIATTHQFCQDMLTGLGIVGDTDPDGTFVERIDDVVTEVVDDFYLRKYAVPGAKPPDFDRATALAIGQAVVNDPGARIEPGRDAPDAAGARAGFAEAVRAEVERRKRGRRLFTFDDMLLRLHRALRHPQLGAAARARLRARFSVVLVDEFQDTDPIQWDILRAAFHEESAERPTALTFIGDPKQAIYAFRGADVVSYLQAVETAGTREGLTTNWRSDEPLVRALDTVFGGAALGDEKIVVPRVGSAHPARRLVGAPRPAPFRLRVLPRAGLRAHWKTGLPMVGPVRERIAADLAADIAELVAADSRWEDGRDDPSLGPGDVAVLVRTNAQAGLVREALAAAGVPSVLAGATSVFATESAEEWLTLLEAVEQPGRTGRVRAAALTVFLGHAATDLDAHADAVLPEVGAMLRRWGAALHDRGVAAFLEAVAAETGLAARVLARVDGERRITDIRHIGQVLHAAAVESRLGVVALVEWLRVRMAEAAAGTGELRPERSRRLESDASAVQVLTVHKCKGLEFPVVYVPFGWDRWVSDTPTVVTHHDEHGHRVRAVGGQDDPAWPEHVAAARAEDDGEDLRLLYVALTRAQGQVVCWWAPATTTANSAVQRLFLGRPAPGTSPDGAYPVVEDERVLAELSVLAGDDIAVERVEPRTAVPFVPSAGHAHALAAAPFDRPLDLAWRRSSYSSLTAGAHAGAPVSEPEERTIVDEDDPDDAAAPTPDDVEPVPSPMADLPVGAAFGTLVHSVLETVDTATGDLHAALAAAATEELRHHPHADVDATTLADALLPVMRTPLPRGGPASLADVTPADRLAELDFELPLAGGDRAGADTPLVTLAAVAALLRRHLPADDPLAAYPDALEHQAHGLGDQVLRGYLTGSIDGVLRGPDGRFVVVDYKTNWLGPVGPTGREPLTAAHYGPTAMATAMIGAHYPLQAVLYAVALHRFLRWRLRGYDPATHLGGVLYLFLRGMCGPDTPVVGGTTCGVFAWSPPPALVVELGSLLDGGPR","length":1126,"molWeight":119807,"crc64":"44B21F039450E230","md5":"B8924ACA8B7C1A405138F8F06B1727FD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"DOMAIN":2,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":4},"uniParcId":"UPI002364FC5A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RBD3","uniProtkbId":"A0ABV9RBD3_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831085.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"Riboflavin biosynthesis protein RibBA"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3,4-dihydroxy-2-butanone 4-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"DHBP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"4.1.99.12"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase-2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"3.5.4.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"GTP cyclohydrolase II"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"value":"ribBA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831085.1"}],"value":"ACFPEL_01570"}]}],"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":"MFC4831085.1"}],"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":212,"modifier":"EXACT"},"end":{"value":376,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00925"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"DHBP synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"GTP cyclohydrolase II","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Region","location":{"start":{"value":398,"modifier":"EXACT"},"end":{"value":427,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":333,"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":335,"modifier":"EXACT"},"end":{"value":335,"modifier":"EXACT"}},"description":"Nucleophile; for GTP cyclohydrolase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Binding site","location":{"start":{"value":28,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":33,"modifier":"EXACT"},"end":{"value":33,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58121"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"D-ribulose 5-phosphate","id":"ChEBI:CHEBI:58121"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":145,"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":144,"modifier":"EXACT"},"end":{"value":144,"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":165,"modifier":"EXACT"},"end":{"value":165,"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":255,"modifier":"EXACT"},"end":{"value":259,"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":260,"modifier":"EXACT"},"end":{"value":260,"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":271,"modifier":"EXACT"},"end":{"value":271,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI: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":276,"modifier":"EXACT"},"end":{"value":276,"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":299,"modifier":"EXACT"},"end":{"value":301,"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":321,"modifier":"EXACT"},"end":{"value":321,"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":356,"modifier":"EXACT"},"end":{"value":356,"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":361,"modifier":"EXACT"},"end":{"value":361,"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":127,"modifier":"EXACT"},"end":{"value":127,"modifier":"EXACT"}},"description":"Essential for DHBP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01283"}]},{"type":"Site","location":{"start":{"value":165,"modifier":"EXACT"},"end":{"value":165,"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":"UP001595909"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000003","properties":[{"key":"ProteinId","value":"MFC4831085.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274186718.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000003.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008686","properties":[{"key":"GoTerm","value":"F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003935","properties":[{"key":"GoTerm","value":"F:GTP cyclohydrolase II activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009231","properties":[{"key":"GoTerm","value":"P:riboflavin biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00641","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.10990:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.870.10:FF:000001","properties":[{"key":"EntryName","value":"Riboflavin biosynthesis protein RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.870.10","properties":[{"key":"EntryName","value":"DHBP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10990","properties":[{"key":"EntryName","value":"GTP cyclohydrolase II"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00179","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00180","properties":[{"key":"EntryName","value":"RibB"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01283","properties":[{"key":"EntryName","value":"RibBA"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017945","properties":[{"key":"EntryName","value":"DHBP_synth_RibB-like_a/b_dom"}]},{"database":"InterPro","id":"IPR000422","properties":[{"key":"EntryName","value":"DHBP_synthase_RibB"}]},{"database":"InterPro","id":"IPR032677","properties":[{"key":"EntryName","value":"GTP_cyclohydro_II"}]},{"database":"InterPro","id":"IPR000926","properties":[{"key":"EntryName","value":"RibA"}]},{"database":"InterPro","id":"IPR036144","properties":[{"key":"EntryName","value":"RibA-like_sf"}]},{"database":"InterPro","id":"IPR016299","properties":[{"key":"EntryName","value":"Riboflavin_synth_RibBA"}]},{"database":"NCBIfam","id":"NF006803","properties":[{"key":"EntryName","value":"PRK09311.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001591","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00505","properties":[{"key":"EntryName","value":"ribA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00506","properties":[{"key":"EntryName","value":"ribB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327:SF18","properties":[{"key":"EntryName","value":"3,4-DIHYDROXY-2-BUTANONE 4-PHOSPHATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21327","properties":[{"key":"EntryName","value":"GTP CYCLOHYDROLASE II-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00926","properties":[{"key":"EntryName","value":"DHBP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00925","properties":[{"key":"EntryName","value":"GTP_cyclohydro2"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001259","properties":[{"key":"EntryName","value":"RibA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF142695","properties":[{"key":"EntryName","value":"RibA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55821","properties":[{"key":"EntryName","value":"YrdC/RibB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDGFEHIERAIADIAAGKAVVVVDDEDRENEGDLVFAAQHATPELVSFMVRYTSGYICVPLTGEACDRLDLPPAHSINQDRHGTAYTVSVDAREGIGTGISGTDRAHTIRVLADPESGPTDLARPGHLVPLRARDGGVLRRPGHTEAAVDLARLAGLEPAGAICEIVSQKDDGDMARFEELQVFADEHELSLITIKDLIAYRRRSEKQVVQVAHANIPTDHGEFVAYGYDSLLDGIEHVALVHGDLGDGEDVLVRVHSECLTGDVLRSRRCDCGPQLDAAMAAVVAEGRGVVLYVRGHEGRGIGLIHKLQAYQLQDAGADTVDANLALGMPADARDYGTGAQILADLGITSMRLLTNNPEKRAGLEGYGLQILGRVSLPSRATPENLRYLRTKRDRMGHDLEGLDGEEDGVVAQPADTDRPAVGGRS","length":427,"molWeight":45829,"crc64":"4B672A53C3971501","md5":"86C5AFA23298DF04C6BB0B105DBB4092"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":3,"PATHWAY":2,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":3,"Active site":2,"Binding site":16,"Site":2},"uniParcId":"UPI002366765A"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RBF5","uniProtkbId":"A0ABV9RBF5_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831100.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"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":"MFC4831100.1"}],"value":"carB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831100.1"}],"value":"ACFPEL_01645"}]}],"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":"MFC4831100.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":688,"modifier":"EXACT"},"end":{"value":880,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":962,"modifier":"EXACT"},"end":{"value":1106,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":402,"modifier":"EXACT"}},"description":"Carboxyphosphate synthetic domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Region","location":{"start":{"value":962,"modifier":"EXACT"},"end":{"value":1127,"modifier":"EXACT"}},"description":"Allosteric domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}]},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":129,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":208,"modifier":"EXACT"},"end":{"value":208,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":210,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":215,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":241,"modifier":"EXACT"},"end":{"value":241,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":242,"modifier":"EXACT"},"end":{"value":242,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":243,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":299,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":724,"modifier":"EXACT"},"end":{"value":724,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":763,"modifier":"EXACT"},"end":{"value":763,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":765,"modifier":"EXACT"},"end":{"value":765,"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":770,"modifier":"EXACT"},"end":{"value":770,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":796,"modifier":"EXACT"},"end":{"value":796,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":797,"modifier":"EXACT"},"end":{"value":797,"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":798,"modifier":"EXACT"},"end":{"value":798,"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":799,"modifier":"EXACT"},"end":{"value":799,"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":839,"modifier":"EXACT"},"end":{"value":839,"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":839,"modifier":"EXACT"},"end":{"value":839,"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":839,"modifier":"EXACT"},"end":{"value":839,"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":851,"modifier":"EXACT"},"end":{"value":851,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01210"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616","label":"2"}},{"type":"Binding site","location":{"start":{"value":851,"modifier":"EXACT"},"end":{"value":851,"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":851,"modifier":"EXACT"},"end":{"value":851,"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":851,"modifier":"EXACT"},"end":{"value":851,"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":851,"modifier":"EXACT"},"end":{"value":851,"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":853,"modifier":"EXACT"},"end":{"value":853,"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":853,"modifier":"EXACT"},"end":{"value":853,"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":"UP001595909"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000003","properties":[{"key":"ProteinId","value":"MFC4831100.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274186727.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000003.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004087","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (ammonia) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004088","properties":[{"key":"GoTerm","value":"F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0044205","properties":[{"key":"GoTerm","value":"P:'de novo' UMP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006526","properties":[{"key":"GoTerm","value":"P:L-arginine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01424","properties":[{"key":"EntryName","value":"MGS_CPS_II"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000007","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000014","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000003","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.1490.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.470.20","properties":[{"key":"EntryName","value":"ATP-grasp fold, B domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.1030.10","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthetase, large subunit oligomerisation domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1380","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01210_B","properties":[{"key":"EntryName","value":"CPSase_L_chain_B"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR011761","properties":[{"key":"EntryName","value":"ATP-grasp"}]},{"database":"InterPro","id":"IPR013815","properties":[{"key":"EntryName","value":"ATP_grasp_subdomain_1"}]},{"database":"InterPro","id":"IPR036897","properties":[{"key":"EntryName","value":"CarbamoylP_synth_lsu_oligo_sf"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR006275","properties":[{"key":"EntryName","value":"CPSase_lsu"}]},{"database":"InterPro","id":"IPR005480","properties":[{"key":"EntryName","value":"CPSase_lsu_oligo"}]},{"database":"InterPro","id":"IPR058047","properties":[{"key":"EntryName","value":"CPSase_preATP-grasp"}]},{"database":"InterPro","id":"IPR011607","properties":[{"key":"EntryName","value":"MGS-like_dom"}]},{"database":"InterPro","id":"IPR036914","properties":[{"key":"EntryName","value":"MGS-like_dom_sf"}]},{"database":"InterPro","id":"IPR033937","properties":[{"key":"EntryName","value":"MGS_CPS_CarB"}]},{"database":"InterPro","id":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"NF003671","properties":[{"key":"EntryName","value":"carB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01369","properties":[{"key":"EntryName","value":"CPSaseII_lrg"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF53","properties":[{"key":"EntryName","value":"CARBAMOYL-PHOSPHATE SYNTHASE [AMMONIA], MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF25596","properties":[{"key":"EntryName","value":"CPSase_L_D1"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02786","properties":[{"key":"EntryName","value":"CPSase_L_D2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02787","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48108","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, large subunit connection domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56059","properties":[{"key":"EntryName","value":"Glutathione synthetase ATP-binding domain-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF52335","properties":[{"key":"EntryName","value":"Methylglyoxal synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52440","properties":[{"key":"EntryName","value":"PreATP-grasp domain"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50975","properties":[{"key":"EntryName","value":"ATP_GRASP"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPRREDIHHVLVIGSGPIVIGQAAEFDYSGTQACRVLREEGLRVSLVNSNPATIMTDPEIADATYVEPITVEYLTKVIEVERPDALLATLGGQTALNAAIALHDAGVLERYGVELIGADIDAIQRGEDRLKFKDIVRSLGGDVPRSEVCHSMAEVRATVAEVGLPVVIRPSFTMGGLGSGLAYTHDELERLAGTGLSASPVHEVLIEESVLGWKEYELELMRDRSDNVVVVCSIENVDPMGVHTGDSVTVAPAMTLTDREYQVMRDTGIAVLRAVGVETGGCNIQFAVHPTTGRLVVIEMNPRVSRSSALASKATGFPIAKIAARLAVGYTLDEITNDITGETPASFEPTLDYVVVKVPRFAFEKFPGADPTLTTTMKSVGEAMALGRSFPEALNKALRSAETTAGGFWTLPDPDEDVKEALHQASLPRDGRLYAVERALRLGASVEEVTEASGIDGWFVEQIEGLVGLRDEIADAPVLDEALLRRAKRAGLSDAQVAAVRPELAGETGVRALRHRLGVRPVYKTVDTCAAEFEARTPYHYSAYESDPAAETEVVAQTERPKVIILGSGPNRIGQGIEFDYSCVHAAFALRAAGFETVMLNCNPETVSTDYDTSDRLYFEPLTEEDVLEVVHAEQVSGLGGAGLVGVVVQLGGQTPLKLAAGLEAAGVPVVGTPPAAIDLAESRGAFGRVLDDAGLPAPPYGMATSFDGAREIAASIGYPVLVRPSYVLGGRGMEIVYDDATLADYIARATEVTPDHPVLVDRFLDDAIEIDVDALCDADGEVYLGGVMEHIEEAGVHSGDSSCALPPITLGGAELATVRESTVALARRLGVRGLMNVQYALKDDVLFVLEANPRASRTVPFVSKATGVALAGAASRIMLGATIAGLREEGQLPAVGDGTDLPREHPVAVKEAVLPFHRFRRPDGRGVDSLLGPEMKSTGEVMGIDRAFSIAFAKAQAAAAGPLPVSGHVFVSVANRDKRSLIFPVKRLADLGFAILATAGTASVLERNGIPCEVVRKHFEGGDGLPTIVDRIVAGEVDLVVNTPVGHSGPRIDGYEIRAACLDVGVPCVTTVQGAAAAVQAVEAAIRGEVGVTSLQVLHARLAEARARDAATLTVEVPQPAGVAGS","length":1127,"molWeight":119063,"crc64":"F7E98DD27BA9FF05","md5":"7B59B5E2F13A0373029ED647CFCA4B94"},"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":"UPI00236573AE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RFH4","uniProtkbId":"A0ABV9RFH4_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831095.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"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":"MFC4831095.1"}],"value":"coaBC"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831095.1"}],"value":"ACFPEL_01620"}]}],"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":"MFC4831095.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":3,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Flavoprotein","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02441"}]},{"type":"Domain","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":412,"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":201,"modifier":"EXACT"}},"description":"Phosphopantothenoylcysteine decarboxylase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Region","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":415,"modifier":"EXACT"}},"description":"Phosphopantothenate--cysteine ligase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}]},{"type":"Binding site","location":{"start":{"value":291,"modifier":"EXACT"},"end":{"value":291,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":301,"modifier":"EXACT"},"end":{"value":301,"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":318,"modifier":"EXACT"},"end":{"value":321,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02225"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563"}},{"type":"Binding site","location":{"start":{"value":337,"modifier":"EXACT"},"end":{"value":337,"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":355,"modifier":"EXACT"},"end":{"value":355,"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":359,"modifier":"EXACT"},"end":{"value":359,"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":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000003","properties":[{"key":"ProteinId","value":"MFC4831095.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274186725.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000003.1"}]},{"database":"Proteomes","id":"UP001595909","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":"MTEESTRPREIVLGVSGGIAAYKACEVLRRLREAGHHVQVVATRAALEFIGAATFEALSGRPVLTGVFENVAEVEHVALGRRADLVVLAPATADLLSRMTHGRADDLLTSTLLTARCPVLAVPAMHTEMWEHPATVDNVATLRRRGTVVLEPASGRLTGADSGPGRLPEPAEIAEFARLLLEWGLTDDQPFPLPRDLEGRRVVVSAGGTAEPLDPVRTLGNRSSGRQGYALARVAAQRGADVTLVAGTIADLDPPAAVDVRRVQTTREMREAVLDAAKAADVVVMAAAVADFRPTDLATAKIKKGDGEPTSVPLTRNPDILRDLVAQDVPGRLVVGFAAETGDEHSSVLDLGRAKLERKGCDLLVVNAVGAGRAFEMEDNEGWLLGADGTSEPLPMGSKAALSARVWDAVAQRLR","length":415,"molWeight":43994,"crc64":"39A9ED0A4E091F7B","md5":"985FC085FAF0FDB078F7A47DFEDED27D"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":2,"PATHWAY":2,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Binding site":6},"uniParcId":"UPI0023655D39"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RGR6","uniProtkbId":"A0ABV9RGR6_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832779.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"S-adenosylmethionine decarboxylase proenzyme"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"AdoMetDC"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"SAMDC"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"4.1.1.50"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"S-adenosylmethionine decarboxylase beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"S-adenosylmethionine decarboxylase alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832779.1"}],"value":"speD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"value":"speE"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"speH"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832779.1"}],"value":"ACFPEL_10180"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Catalyzes the decarboxylation of S-adenosylmethionine to S-adenosylmethioninamine (dcAdoMet), the propylamine donor required for the synthesis of the polyamines spermine and spermidine from the diamine putrescine"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"value":"Catalyzes the irreversible transfer of a propylamine group from the amino donor S-adenosylmethioninamine (decarboxy-AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-adenosyl 3-(methylsulfanyl)propylamine + putrescine = S-methyl-5'-thioadenosine + spermidine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:12721"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17509"},{"database":"ChEBI","id":"CHEBI:57443"},{"database":"ChEBI","id":"CHEBI:57834"},{"database":"ChEBI","id":"CHEBI:326268"}],"ecNumber":"2.5.1.16","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-adenosyl-L-methionine + H(+) = S-adenosyl 3-(methylsulfanyl)propylamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15981"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57443"},{"database":"ChEBI","id":"CHEBI:59789"}],"ecNumber":"4.1.1.50","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Amine and polyamine biosynthesis; S-adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from S-adenosyl-L-methionine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"value":"Amine and polyamine biosynthesis; spermidine biosynthesis; spermidine from putrescine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl group blocking the N-terminus of the alpha chain"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"value":"Belongs to the prokaryotic AdoMetDC family. Type 1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007867"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"value":"Belongs to the spermidine/spermine synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832779.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":75,"modifier":"EXACT"}},"description":"S-adenosylmethionine decarboxylase beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"featureId":"PRO_5044931421"},{"type":"Chain","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":423,"modifier":"EXACT"}},"description":"S-adenosylmethionine decarboxylase alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"featureId":"PRO_5044931420"},{"type":"Domain","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"PABS","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51006"}]},{"type":"Active site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Active site","location":{"start":{"value":81,"modifier":"EXACT"},"end":{"value":81,"modifier":"EXACT"}},"description":"Proton acceptor; for processing activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Active site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"Proton donor; for catalytic activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Active site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00354"}]},{"type":"Binding site","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":164,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Binding site","location":{"start":{"value":194,"modifier":"EXACT"},"end":{"value":194,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57834"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"ligand":{"name":"spermidine","id":"ChEBI:CHEBI:57834"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57834"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"ligand":{"name":"spermidine","id":"ChEBI:CHEBI:57834"}},{"type":"Binding site","location":{"start":{"value":237,"modifier":"EXACT"},"end":{"value":237,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":276,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Binding site","location":{"start":{"value":307,"modifier":"EXACT"},"end":{"value":307,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:17509"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"ligand":{"name":"S-methyl-5'-thioadenosine","id":"ChEBI:CHEBI:17509"}},{"type":"Site","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]},{"type":"Modified residue","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022813"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0068","category":"PTM","name":"Autocatalytic cleavage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023115"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0620","category":"Biological process","name":"Polyamine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023270"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0704","category":"Ligand","name":"Schiff base"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023066"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0745","category":"Biological process","name":"Spermidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00198"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00464"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000020","properties":[{"key":"ProteinId","value":"MFC4832779.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_337994139.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000020.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0004014","properties":[{"key":"GoTerm","value":"F:adenosylmethionine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004766","properties":[{"key":"GoTerm","value":"F:spermidine synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008295","properties":[{"key":"GoTerm","value":"P:spermidine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.90.10","properties":[{"key":"EntryName","value":"S-adenosylmethionine decarboxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00464","properties":[{"key":"EntryName","value":"AdoMetDC_1"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00198","properties":[{"key":"EntryName","value":"Spermidine_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003826","properties":[{"key":"EntryName","value":"AdoMetDC_fam_prok"}]},{"database":"InterPro","id":"IPR030374","properties":[{"key":"EntryName","value":"PABS"}]},{"database":"InterPro","id":"IPR016067","properties":[{"key":"EntryName","value":"S-AdoMet_deCO2ase_core"}]},{"database":"InterPro","id":"IPR017716","properties":[{"key":"EntryName","value":"S-AdoMet_deCOase_pro-enz"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR001045","properties":[{"key":"EntryName","value":"Spermi_synthase"}]},{"database":"NCBIfam","id":"TIGR03330","properties":[{"key":"EntryName","value":"SAM_DCase_Bsu"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11558:SF11","properties":[{"key":"EntryName","value":"SPERMIDINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11558","properties":[{"key":"EntryName","value":"SPERMIDINE/SPERMINE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02675","properties":[{"key":"EntryName","value":"AdoMet_dc"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01564","properties":[{"key":"EntryName","value":"Spermine_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56276","properties":[{"key":"EntryName","value":"S-adenosylmethionine decarboxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51006","properties":[{"key":"EntryName","value":"PABS_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTTTTPTTHPTDPASFAGRHVLAELRGVDPALLGDEHAVADALRRALDEGGARVLDVVTHRFEPQGTTVMALLAESHASVHAYPEASAAFVDVFTCGVEADPELVVDALGRGLGAAEVRAQVVARGAGLAPAGGGREVDEPLAAGMRRRWRLDEVLWRGRTEWQDMMVARTAQGVSLFCDGERQSTEQSQLVYHEALAVPPMLLADELRSVLVVGSSEGVVSQLAVAAGARWVDHVDIDTECVRRCAELLPYGYTPAELAAAEVGDGPVRMHYTDGWRFLADAAARGDRWDVVIVDLPDEPVEVTDPAQHARLYGAEFLRRCADVLTPGGVVCSQAGCPTLWRNDTLQRMTDRFDDVFAAVLPYCSDEHEWAYLSGRVQPVPDPVALAISRLDRFPELTSIDADALRRGAILPFALRARTPVS","length":423,"molWeight":45759,"crc64":"3E16464EB927FB27","md5":"DB8428CED881FCC748180EE260C81C41"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":2,"PTM":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Chain":2,"Domain":1,"Active site":4,"Binding site":6,"Site":1,"Modified residue":1},"uniParcId":"UPI00308237A7"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RH76","uniProtkbId":"A0ABV9RH76_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833050.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"6.3.4.2"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine 5'-triphosphate synthase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Cytidine triphosphate synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTP synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPS"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"UTP--ammonia ligase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"pyrG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833050.1"}],"value":"ACFPEL_11590"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-glutamine + H2O = L-glutamate + NH4(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15889"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + L-glutamine + ATP + H2O = CTP + L-glutamate + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:26426"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"6.3.4.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047781"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"UTP + NH4(+) + ATP = CTP + ADP + phosphate + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16597"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:28938"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:37563"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005171"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Belongs to the CTP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833050.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"CTP synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF06418"}]},{"type":"Domain","location":{"start":{"value":310,"modifier":"EXACT"},"end":{"value":541,"modifier":"EXACT"}},"description":"Glutamine amidotransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00117"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"Amidoligase domain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Region","location":{"start":{"value":561,"modifier":"EXACT"},"end":{"value":585,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"Nucleophile; for glutamine hydrolysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}]},{"type":"Active site","location":{"start":{"value":522,"modifier":"EXACT"},"end":{"value":522,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":524,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":26,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":78,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":149,"modifier":"EXACT"},"end":{"value":149,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":196,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37563"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"CTP","id":"ChEBI:CHEBI:37563","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":232,"modifier":"EXACT"},"end":{"value":232,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:46398"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"UTP","id":"ChEBI:CHEBI:46398"}},{"type":"Binding site","location":{"start":{"value":250,"modifier":"EXACT"},"end":{"value":250,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":363,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":414,"modifier":"EXACT"},"end":{"value":414,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022962"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01227"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000022","properties":[{"key":"ProteinId","value":"MFC4833050.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274192406.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000022.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0097268","properties":[{"key":"GoTerm","value":"C:cytoophidium"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003883","properties":[{"key":"GoTerm","value":"F:CTP synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0044210","properties":[{"key":"GoTerm","value":"P:'de novo' CTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019856","properties":[{"key":"GoTerm","value":"P:pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd03113","properties":[{"key":"EntryName","value":"CTPS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01746","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000009","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000002","properties":[{"key":"EntryName","value":"CTP synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01227","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR004468","properties":[{"key":"EntryName","value":"CTP_synthase"}]},{"database":"InterPro","id":"IPR017456","properties":[{"key":"EntryName","value":"CTP_synthase_N"}]},{"database":"InterPro","id":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR033828","properties":[{"key":"EntryName","value":"GATase1_CTP_Synthase"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"NCBIfam","id":"NF003792","properties":[{"key":"EntryName","value":"PRK05380.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00337","properties":[{"key":"EntryName","value":"PyrG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550","properties":[{"key":"EntryName","value":"CTP SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11550:SF0","properties":[{"key":"EntryName","value":"CTP SYNTHASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06418","properties":[{"key":"EntryName","value":"CTP_synth_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTVQPSRTTKHVFVTGGVASSLGKGLTASSLGQLLTARGLRVTMQKLDPYLNVDPGTMNPFQHGEVFVTEDGAETDLDIGHYERFLDRDLSARANVTTGQVYSTVIAKERRGEYLGDTVQVIPHITDEIKSRVLAMRTADPAPDVVITEVGGTVGDIESLPFLEAARQLRHEVGRDNCFFLHVSLVPFLAPSGELKTKPTQHSVAALRNIGIQPDGLVLRADRAIPEDMTRKISLMCDVEEDGVVACPDAPSIYDIPKVLHGEGLDAYVVRRLGLPFRDVDWTVWGDLLDRVHHPTETVEIAIVGKYVDLPDAYLSVTEAVRAGGFAHRARVTVRWVPSDSCETPAGAAAALKGVSGVLVPGGFGIRGIEGKLGALAHAHRNGIPTLGLCLGLQCMVIHAARSMAGLEGANSAEFDESTPHPVISTMAGQHDVVAGERDMGGTMRLGSWPAVLAPETVVRAAYGTGKVTERHRHRYEVNNAYRDRLVEAGLVISGTSPDGSLVEFVELPREKHPFFVGTQAHPELKSRPTRAHPLFRAFVAASLRHVASERLDLETNGDLISDAGSGNDGDARVDGVDVPAAASS","length":585,"molWeight":62775,"crc64":"0C9F5FA19D84A4B6","md5":"71737A96A211784019C864CCE310572C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":2,"Region":2,"Active site":4,"Binding site":16},"uniParcId":"UPI002366D3A5"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RHX1","uniProtkbId":"A0ABV9RHX1_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832787.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"dITP/XTP pyrophosphatase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"3.6.1.66"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Non-canonical purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Non-standard purine NTP pyrophosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Nucleoside-triphosphate diphosphatase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Nucleoside-triphosphate pyrophosphatase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"NTPase"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832787.1"}],"value":"rdgB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832787.1"}],"value":"ACFPEL_10225"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Pyrophosphatase that catalyzes the hydrolysis of nucleoside triphosphates to their monophosphate derivatives, with a high preference for the non-canonical purine nucleotides XTP (xanthosine triphosphate), dITP (deoxyinosine triphosphate) and ITP. Seems to function as a house-cleaning enzyme that removes non-canonical purine nucleotides from the nucleotide pool, thus preventing their incorporation into DNA/RNA and avoiding chromosomal lesions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ITP + H2O = IMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29399"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58053"},{"database":"ChEBI","id":"CHEBI:61402"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"XTP + H2O = XMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28610"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57464"},{"database":"ChEBI","id":"CHEBI:61314"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052017"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"dITP + H2O = dIMP + diphosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:28342"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:61194"},{"database":"ChEBI","id":"CHEBI:61382"}],"ecNumber":"3.6.1.66","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051875"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008023"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003781"}],"value":"Belongs to the HAM1 NTPase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4832787.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Region","location":{"start":{"value":167,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":186,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}]},{"type":"Binding site","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":12,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":72,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":73,"modifier":"EXACT"},"end":{"value":73,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"ligand":{"name":"substrate"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023080"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"id":"KW-0546","category":"Biological process","name":"Nucleotide metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01405"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000020","properties":[{"key":"ProteinId","value":"MFC4832787.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274188305.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000020.1"}]},{"database":"Proteomes","id":"UP001595909","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:0035870","properties":[{"key":"GoTerm","value":"F:dITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0036220","properties":[{"key":"GoTerm","value":"F:ITP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0017111","properties":[{"key":"GoTerm","value":"F:ribonucleoside triphosphate phosphatase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0036222","properties":[{"key":"GoTerm","value":"F:XTP diphosphatase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009146","properties":[{"key":"GoTerm","value":"P:purine nucleoside triphosphate catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00515","properties":[{"key":"EntryName","value":"HAM1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.950.10:FF:000001","properties":[{"key":"EntryName","value":"dITP/XTP pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.950.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01405","properties":[{"key":"EntryName","value":"Non_canon_purine_NTPase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR020922","properties":[{"key":"EntryName","value":"dITP/XTP_pyrophosphatase"}]},{"database":"InterPro","id":"IPR029001","properties":[{"key":"EntryName","value":"ITPase-like_fam"}]},{"database":"InterPro","id":"IPR002637","properties":[{"key":"EntryName","value":"RdgB/HAM1"}]},{"database":"NCBIfam","id":"TIGR00042","properties":[{"key":"EntryName","value":"RdgB/HAM1 family non-canonical purine NTP pyrophosphatase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067:SF9","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11067","properties":[{"key":"EntryName","value":"INOSINE TRIPHOSPHATE PYROPHOSPHATASE/HAM1 PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01725","properties":[{"key":"EntryName","value":"Ham1p_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52972","properties":[{"key":"EntryName","value":"ITPase-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MKVLLATRNDAKLAELRRLVEGRGLEGLEIRGLDDVPEFPEAPETGATFEENALAKARDAAAATGLVAVADDSGLAVDALNGMPGVLSARWSGRGGARTERDAANLALVLDQMADVPEDRRGAAFVCAAAAAHPDGREVVVVERWPGRLVRSPRGLNGFGYDPAFVPEGESRTSAEMAPEEKDAVSHRSRALRALLPRLSELG","length":203,"molWeight":21489,"crc64":"9A0AF0ED53074E26","md5":"B53E2D009A900BE0F335EDC8A8214966"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Region":1,"Compositional bias":1,"Active site":1,"Binding site":6},"uniParcId":"UPI0023670629"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RIF0","uniProtkbId":"A0ABV9RIF0_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833121.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Lysine--tRNA ligase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"6.1.1.6"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Lysyl-tRNA synthetase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"LysRS"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833121.1"}],"value":"lysS"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833121.1"}],"value":"ACFPEL_11965"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024681"}],"value":"Catalyzes the production of L-lysyl-tRNA(Lys)transfer and the transfer of a lysyl group from L-lysyl-tRNA(Lys) to membrane-bound phosphatidylglycerol (PG), which produces lysylphosphatidylglycerol (LPG), one of the components of the bacterial membrane with a positive net charge. LPG synthesis contributes to the resistance to cationic antimicrobial peptides (CAMPs) and likely protects M.tuberculosis against the CAMPs produced by competiting microorganisms (bacteriocins). In fact, the modification of anionic phosphatidylglycerol with positively charged L-lysine results in repulsion of the peptides"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-tRNA(Lys) + a 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a 1,2-diacyl-sn-glycero-3-phospho-1'-(3'-O-L-lysyl)-sn-glycerol + tRNA(Lys)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10668"},{"database":"Rhea","id":"RHEA-COMP:9696"},{"database":"Rhea","id":"RHEA-COMP:9697"},{"database":"ChEBI","id":"CHEBI:64716"},{"database":"ChEBI","id":"CHEBI:75792"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78529"}],"ecNumber":"2.3.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047540"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"tRNA(Lys) + L-lysine + ATP = L-lysyl-tRNA(Lys) + AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20792"},{"database":"Rhea","id":"RHEA-COMP:9696"},{"database":"Rhea","id":"RHEA-COMP:9697"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32551"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:78442"},{"database":"ChEBI","id":"CHEBI:78529"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.1.1.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048573"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Binds 3 Mg(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"}],"value":"Multi-pass membrane protein","id":"SL-9909"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"value":"Belongs to the class-II aminoacyl-tRNA synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009968"}],"value":"In the C-terminal section; belongs to the class-II aminoacyl-tRNA synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005270"}],"value":"In the N-terminal section; belongs to the LPG synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833121.1"}],"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":580,"modifier":"EXACT"},"end":{"value":599,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":619,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":649,"modifier":"EXACT"},"end":{"value":667,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":673,"modifier":"EXACT"},"end":{"value":692,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":704,"modifier":"EXACT"},"end":{"value":725,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Transmembrane","location":{"start":{"value":765,"modifier":"EXACT"},"end":{"value":785,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}]},{"type":"Domain","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"Aminoacyl-transfer RNA synthetases class-II family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50862"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1147,"modifier":"EXACT"},"end":{"value":1166,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1147,"modifier":"EXACT"},"end":{"value":1166,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":436,"modifier":"EXACT"},"end":{"value":436,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":443,"modifier":"EXACT"},"end":{"value":443,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023146"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0030","category":"Molecular function","name":"Aminoacyl-tRNA synthetase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023251"}],"id":"KW-0046","category":"Biological process","name":"Antibiotic resistance"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"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":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00252"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"SAM","id":"Phobius"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000023","properties":[{"key":"ProteinId","value":"MFC4833121.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274187239.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000023.1"}]},{"database":"Proteomes","id":"UP001595909","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:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"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:0004824","properties":[{"key":"GoTerm","value":"F:lysine-tRNA ligase 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:0050071","properties":[{"key":"GoTerm","value":"F:phosphatidylglycerol lysyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0000049","properties":[{"key":"GoTerm","value":"F:tRNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006430","properties":[{"key":"GoTerm","value":"P:lysyl-tRNA aminoacylation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00775","properties":[{"key":"EntryName","value":"LysRS_core"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04322","properties":[{"key":"EntryName","value":"LysRS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.50.140","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00252","properties":[{"key":"EntryName","value":"Lys_tRNA_synth_class2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004364","properties":[{"key":"EntryName","value":"Aa-tRNA-synt_II"}]},{"database":"InterPro","id":"IPR006195","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR024320","properties":[{"key":"EntryName","value":"LPG_synthase_C"}]},{"database":"InterPro","id":"IPR002313","properties":[{"key":"EntryName","value":"Lys-tRNA-ligase_II"}]},{"database":"InterPro","id":"IPR044136","properties":[{"key":"EntryName","value":"Lys-tRNA-ligase_II_N"}]},{"database":"InterPro","id":"IPR018149","properties":[{"key":"EntryName","value":"Lys-tRNA-synth_II_C"}]},{"database":"InterPro","id":"IPR012340","properties":[{"key":"EntryName","value":"NA-bd_OB-fold"}]},{"database":"InterPro","id":"IPR004365","properties":[{"key":"EntryName","value":"NA-bd_OB_tRNA"}]},{"database":"InterPro","id":"IPR031553","properties":[{"key":"EntryName","value":"tRNA-synt_2_TM"}]},{"database":"NCBIfam","id":"TIGR00499","properties":[{"key":"EntryName","value":"lysS_bact"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF001756","properties":[{"key":"EntryName","value":"PRK00484.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42918:SF15","properties":[{"key":"EntryName","value":"LYSINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42918","properties":[{"key":"EntryName","value":"LYSYL-TRNA SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09924","properties":[{"key":"EntryName","value":"LPG_synthase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00152","properties":[{"key":"EntryName","value":"tRNA-synt_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16995","properties":[{"key":"EntryName","value":"tRNA-synt_2_TM"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01336","properties":[{"key":"EntryName","value":"tRNA_anti-codon"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00982","properties":[{"key":"EntryName","value":"TRNASYNTHLYS"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50249","properties":[{"key":"EntryName","value":"Nucleic acid-binding proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50862","properties":[{"key":"EntryName","value":"AA_TRNA_LIGASE_II"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDAHTDAHTDAPTDAHGEAPPDVPDSAAGPDASNGPDAHLGQQDIRTAKLAARRAAGETEPYRWPVDHSLADLRAAHGDLAPDTLTGEEVHVAGRLMGLRRQGGLSFGTLRDRSGTIQLFVDTAVVGHDAHVAIDDLDRGDWVGVRGTVMTTRRGELSIRVDECALLAKALRPPAGGHHGLADVETRYRQRYADLEVNERTREIFRIRHAAVHAIRNHLAEKGFTEVEGPVLQSIQGGASARPFVTHHNALDLDMYLRIALELHLKRLIVGGMERVFELGRVFRNEGVDTRHNPEFTMLEAYQAFADYHDMMDLTEGMVTAAAHAALGDDLTVRYQGQEIDLRPPWPRRRFADMIAEKTGEVMHPDMPIADARAALDRLGIAWEQGWGPGRLMKEVYDERVQHDVVGPVFCIDYPREVSPLARAHRDDPAYSERFELIVAGFELCNAYSEQNDPVVQMAAFEEEAQAKRDGDPEAGDIDLDYVRALEYGMPPTGGLGIGIDRLVMLLASVDSIREVILFPTLRPEFAPPPGGGPGGAHRPVLPPTPMPAAALAAATPPASVTAVPARASATDDGPPGRPWVVTVIAGLTALAGLLHLMVHVPIVHERLGDRINVDLVPPWFAVTGHVLSAAIGLLLLLLADQLAKRKQAAWRVAVVLSALAVVAHVLKGPHQVGLGISVALLVLLLVARKSFRAPADPPSLLRLVRFVPIYLTAVLAFGFVSLGLQSGRMTPELTFLGGLETIFGGLVGIDGPYTFSRRLFAETFPAALLTLGVVGLVVFLILLFRPLTARDPHTRDDWSRARLLVQTYGWDTLAAFALRDDKSFFFGSDGRAMIAYTYLGGYALAAGDPIGDEASLPAVVDEFLAMCAQRAWTPAFLAAREEDTQEGGLLASRGFRSFYLGDEAIIDCPSFTLEGRERKSVRAAVRRVERTYRFQMIAESAASPKLVAALNAISEKWRGKDPERGFTMSLSQDITGSDANRDFLLCVALDADGVPGGFLRLVPAYGGPATGTTFGYTLDLMRHDPGAPNGMTEFLIAKSASALDERGVTRLSMNFAMWGRLFADDVPFTPTQKLARRAVGVLNPFFQVRSLHDFNEKFGPQWLPRVLAYRSPADLPRVGLLYAGAEGFLAVPGLGPLFVPAAVGGAPSPSSTAPEASAPPGATAA","length":1166,"molWeight":126056,"crc64":"C232A39D4996AF4C","md5":"51B1DEDB0B3D6D3FC395CF0975ECB459"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Transmembrane":6,"Domain":1,"Region":2,"Compositional bias":2,"Binding site":3},"uniParcId":"UPI0023669474"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RJ74","uniProtkbId":"A0ABV9RJ74_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4833338.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"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":"MFC4833338.1"}],"value":"ACFPEL_13075"}]}],"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":"MFC4833338.1"}],"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":28,"modifier":"EXACT"},"end":{"value":106,"modifier":"EXACT"}},"description":"Mur ligase N-terminal catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01225"}]},{"type":"Domain","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":320,"modifier":"EXACT"}},"description":"Mur ligase central","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08245"}]},{"type":"Domain","location":{"start":{"value":342,"modifier":"EXACT"},"end":{"value":473,"modifier":"EXACT"}},"description":"Mur ligase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02875"}]},{"type":"Motif","location":{"start":{"value":418,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"Meso-diaminopimelate recognition motif","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00208"}]},{"type":"Binding site","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":31,"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":122,"modifier":"EXACT"},"end":{"value":128,"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":164,"modifier":"EXACT"},"end":{"value":165,"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":191,"modifier":"EXACT"},"end":{"value":191,"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":199,"modifier":"EXACT"},"end":{"value":199,"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":394,"modifier":"EXACT"},"end":{"value":394,"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":418,"modifier":"EXACT"},"end":{"value":421,"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":471,"modifier":"EXACT"},"end":{"value":471,"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":475,"modifier":"EXACT"},"end":{"value":475,"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":231,"modifier":"EXACT"},"end":{"value":231,"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":"MFC4833338.1"}],"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":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000027","properties":[{"key":"ProteinId","value":"MFC4833338.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_378014955.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000027.1"}]},{"database":"Proteomes","id":"UP001595909","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":"MTVTEVVARLRETGSVEIVGEADARLTGATLRAHEVRPGDLFAALPGSRAHGADFVGDALARGAAAVLTDADGAARPVLREAALEAAVPVLVHPDPRAAIGPAAARIYGDPSTRLDVLGVTGTSGKTTTVYLLEAALAAAGARTGLIGTVETRLGGRRLPSSFTTPEAPDLQALLATMVDEGATHVAMEVSSHALSLGRVAGTRFAVGAFTNLSAEHLDFHADMEDYFAAKARLFDGRSAAEVVCIDSAWGQRLVREGAGEKKTVTVGTPEADWHAADVVALPDGTQRFTAHGPDGLALPVTLRLPGAFNVTNALLALACGHAAGEDPAALARGLAEVRVPGRMQRVEAGQPFLAVVDYAHKPAAVGALLETLRAQATETGGRVLTVLGCGGDRDRAKRPVMGRLGAQLSDHLWVTDDNPRTEDPAAIRAAVLDGAREVPGAVVDEIGDRRAAIAAAVAEARPGDVVVVAGKGHETGQQVGAEKLPFSDVEELERALRAGGPR","length":503,"molWeight":51903,"crc64":"BE00CAC911EADDCA","md5":"CD925E10F61DE763CC09C10A4A373C65"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":3,"Motif":1,"Binding site":9,"Modified residue":1},"uniParcId":"UPI003371AB75"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RMN4","uniProtkbId":"A0ABV9RMN4_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4834538.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"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":"MFC4834538.1"}],"value":"glmU"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4834538.1"}],"value":"ACFPEL_19145"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049628"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-N-acetylglucosamine (UDP-GlcNAc). The C-terminal domain catalyzes the transfer of acetyl group from acetyl coenzyme A to glucosamine-1-phosphate (GlcN-1-P) to produce N-acetylglucosamine-1-phosphate (GlcNAc-1-P), which is converted into UDP-GlcNAc by the transfer of uridine 5-monophosphate (from uridine 5-triphosphate), a reaction catalyzed by the N-terminal domain"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N-acetyl-alpha-D-glucosamine 1-phosphate + UTP + H(+) = UDP-N-acetyl-alpha-D-glucosamine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13509"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46398"},{"database":"ChEBI","id":"CHEBI:57705"},{"database":"ChEBI","id":"CHEBI:57776"}],"ecNumber":"2.7.7.23","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048493"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"alpha-D-glucosamine 1-phosphate + acetyl-CoA = N-acetyl-alpha-D-glucosamine 1-phosphate + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13725"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:57776"},{"database":"ChEBI","id":"CHEBI:58516"}],"ecNumber":"2.3.1.157","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048247"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Binds 1 Mg(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Bacterial outer membrane biogenesis; LPS lipid A biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate from alpha-D-glucosamine 6-phosphate (route II): step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D-glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N-acetyl-alpha-D-glucosamine 1-phosphate: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Homotrimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007707"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the C-terminal section; belongs to the transferase hexapeptide repeat family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007947"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"In the N-terminal section; belongs to the N-acetylglucosamine-1-phosphate uridyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4834538.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":8,"modifier":"EXACT"},"end":{"value":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":494,"modifier":"EXACT"}},"description":"N-acetyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}]},{"type":"Region","location":{"start":{"value":447,"modifier":"EXACT"},"end":{"value":494,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":466,"modifier":"EXACT"},"end":{"value":484,"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":11,"modifier":"EXACT"},"end":{"value":14,"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":25,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57705"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"ligand":{"name":"UDP-N-acetyl-alpha-D-glucosamine","id":"ChEBI:CHEBI:57705"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":88,"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":111,"modifier":"EXACT"},"end":{"value":113,"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"}}],"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":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01631"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000039","properties":[{"key":"ProteinId","value":"MFC4834538.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274190629.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000039.1"}]},{"database":"Proteomes","id":"UP001595909","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":"IPR025877","properties":[{"key":"EntryName","value":"MobA-like_NTP_Trfase"}]},{"database":"InterPro","id":"IPR029044","properties":[{"key":"EntryName","value":"Nucleotide-diphossugar_trans"}]},{"database":"InterPro","id":"IPR011004","properties":[{"key":"EntryName","value":"Trimer_LpxA-like_sf"}]},{"database":"NCBIfam","id":"NF010932","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01173","properties":[{"key":"EntryName","value":"glmU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584:SF3","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN GLMU"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43584","properties":[{"key":"EntryName","value":"NUCLEOTIDYL TRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12804","properties":[{"key":"EntryName","value":"NTP_transf_3"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53448","properties":[{"key":"EntryName","value":"Nucleotide-diphospho-sugar transferases"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51161","properties":[{"key":"EntryName","value":"Trimeric LpxA-like enzymes"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPPSPTAVVVLAAGEGTRMHSATPKVLHPVGGRSLLGHAVHAAAGTTPEHLVVVVGHEREQVGTHTIGLAAELDREVVTAVQDRRRGTGHAVSCGIARLPADLEGTVLVSYGDVPLLDAATMRALLAEHVDGGYAVTLLTAELDDPRGYGRVVRDEANQVSAIVEHRDATLEQLAINEVNSGVYAFDLAFLREALGHLTTHNSQGELYLTDVVAIAADSGRGAGAVETADPWLVAGVNDRVQMASLGAELNRRLLERWMRAGVTVVDPTSTWVDVGVRLERDVTLHPGTQLHGGTTVAEGATVGPDTTLTDVVVGARAAVVRTHGSSSRIGPETSVGPFAYLRPGVELDARGKIGTFVEVKNAHIGEGSKVPHLTYVGDATIGEGSNIGASSVFVNYDGVTKHRTTVGSHVRTGSDNTFVAPVSIGDGAYTGAGTVVREDVPPGALAVSSGPQRNVEGWVGRKRPGTAAAQAAEQAGKAATRAAGSDDHEQEDP","length":494,"molWeight":51276,"crc64":"BD4C28A1DC8D8D2D","md5":"68F3C93E3BFDBEDA79D3D74349E98282"},"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":"UPI0023654AC2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RMR2","uniProtkbId":"A0ABV9RMR2_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4835489.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"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":"MFC4835489.1"}],"value":"rlmN"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4835489.1"}],"value":"ACFPEL_23970"}]}],"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":"MFC4835489.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":372,"modifier":"EXACT"}},"description":"Radical SAM core","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51918"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":34,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Active site","location":{"start":{"value":378,"modifier":"EXACT"},"end":{"value":378,"modifier":"EXACT"}},"description":"S-methylcysteine intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"}]},{"type":"Binding site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":148,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":151,"modifier":"EXACT"},"end":{"value":151,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01849"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01266"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883","note":"4Fe-4S-S-AdoMet"}},{"type":"Binding site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":200,"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":233,"modifier":"EXACT"},"end":{"value":233,"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":256,"modifier":"EXACT"},"end":{"value":258,"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":335,"modifier":"EXACT"},"end":{"value":335,"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":"UP001595909"}],"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":"HAMAP-Rule","id":"MF_01849"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000050","properties":[{"key":"ProteinId","value":"MFC4835489.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274189083.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000050.1"}]},{"database":"Proteomes","id":"UP001595909","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":"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":"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":"MTEPAVTPETPDPGTAPGPVLTLSPRGSRRTRPAQHLADLDTEGRRAAVAELGMPAFRADQLSRHYFTRLESDPATMTDLPAAARETLGPALLPSLLTPTWEQDCDGGTTRKTLWRANDGALVESVLMGYTDRATVCISSQAGCGMACPFCATGQNGLERNLSTAEIVEQVRSAAAVVRSGGLGANLSRLSNVVFMGMGEPLANYRRVVDAVHRLCDAPPAGLGLSQRSVTVSTVGLVPAIHRLAEENLQVTLAVSLHTPDDELRDTLVPVNTRWPVADVFAAARHYADVTGRRVSIEYALIRDVNDQPWRADLLAKLASKHLGRLVHVNLIPLNPTPGSKWDASPAPVQAEFLRRVREGGVACTVRDTRGREIAAACGQLAATARP","length":387,"molWeight":41404,"crc64":"A9B24239E7E0FFB5","md5":"D99CAD4EE6B757EAC0917A912E725176"},"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":"UPI002365735C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RP81","uniProtkbId":"A0ABV9RP81_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4835314.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate--fructose 6-phosphate 1-phosphotransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"2.7.1.90"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"6-phosphofructokinase, pyrophosphate dependent"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-dependent phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"PPi-PFK"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Pyrophosphate-dependent 6-phosphofructose-1-kinase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"pfp"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4835314.1"}],"value":"ACFPEL_23090"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate, the first committing step of glycolysis. Uses inorganic phosphate (PPi) as phosphoryl donor instead of ATP like common ATP-dependent phosphofructokinases (ATP-PFKs), which renders the reaction reversible, and can thus function both in glycolysis and gluconeogenesis. Consistently, PPi-PFK can replace the enzymes of both the forward (ATP-PFK) and reverse (fructose-bisphosphatase (FBPase)) reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + diphosphate = beta-D-fructose 1,6-bisphosphate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13613"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57634"}],"ecNumber":"2.7.1.90","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":"HAMAP-Rule","id":"MF_01976"}],"value":"Non-allosteric"}],"commentType":"ACTIVITY REGULATION"},{"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":"MFC4835314.1"}],"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":296,"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:33019"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}],"ligand":{"name":"diphosphate","id":"ChEBI:CHEBI:33019"}},{"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":221,"modifier":"EXACT"},"end":{"value":221,"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":265,"modifier":"EXACT"},"end":{"value":265,"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":271,"modifier":"EXACT"},"end":{"value":274,"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 catalytic activity and substrate specificity; stabilizes the transition state when the phosphoryl donor is PPi; prevents ATP from binding by mimicking the alpha-phosphate group of ATP","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]},{"type":"Site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"Important for catalytic activity; stabilizes the transition state when the phosphoryl donor is PPi","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01976"}]}],"keywords":[{"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:0000313","source":"Proteomes","id":"UP001595909"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000049","properties":[{"key":"ProteinId","value":"MFC4835314.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274187018.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000049.1"}]},{"database":"Proteomes","id":"UP001595909","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:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070095","properties":[{"key":"GoTerm","value":"F:fructose-6-phosphate binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042802","properties":[{"key":"GoTerm","value":"F:identical protein binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0048029","properties":[{"key":"GoTerm","value":"F:monosaccharide binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061621","properties":[{"key":"GoTerm","value":"P:canonical glycolysis"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0030388","properties":[{"key":"GoTerm","value":"P:fructose 1,6-bisphosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006002","properties":[{"key":"GoTerm","value":"P:fructose 6-phosphate metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01976","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR012003","properties":[{"key":"EntryName","value":"ATP_PFK_prok-type"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR012829","properties":[{"key":"EntryName","value":"Phosphofructokinase_III"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02483","properties":[{"key":"EntryName","value":"PFK_mixed"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002872","properties":[{"key":"EntryName","value":"PRK03202.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF52","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE 3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000532","properties":[{"key":"EntryName","value":"ATP_PFK_prok"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00476","properties":[{"key":"EntryName","value":"PHFRCTKINASE"}]},{"database":"SUPFAM","id":"SSF53784","properties":[{"key":"EntryName","value":"Phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRIGMLTGGGDCPGLNAVIRAVVHRADAAGDEVIGFRDGWRGPLKGASRPLNVADVAGILARGGTILGSSRTNPYAQGEGGADAVRATMAAQGVDALVAIGGEDTLGAAARLAADGVRVVGVPKTIDNDLAATDYTFGFDTAVHIATEAIDRLRTTAESHRRALVCEVMGRHAGWIALHAGMAGGANAIIIPERPFTVGRVCDWVNSCFRNEYAPVIVVSEGAVPDGGDELLAAGGTDAFGHRRLGGVGTWLADEIERETGAESRAVVLGHIQRGGTPTAYDRVLATRFGVQAMAALHDGESGVMVALRGTDIVRVSLDEATAELKTVPTTRLDEAEVFFG","length":341,"molWeight":35332,"crc64":"9F10E16935C1B758","md5":"01743A5CA7A8AF9074CA92D6288CDAF2"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":8,"Site":2},"uniParcId":"UPI0023671104"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RQE8","uniProtkbId":"A0ABV9RQE8_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2025-10-08","entryVersion":3,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4834432.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional NAD(P)H-hydrate repair enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Nicotinamide nucleotide repair protein"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent (S)-NAD(P)H-hydrate dehydratase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"4.2.1.136"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"ADP-dependent NAD(P)HX dehydratase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"NAD(P)H-hydrate epimerase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"5.1.99.6"}]}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"nnrD"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"nnrE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4834432.1"}],"value":"ACFPEL_18610"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00025153"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Bifunctional enzyme that catalyzes the epimerization of the S- and R-forms of NAD(P)HX and the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. This allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Catalyzes the dehydration of the S-form of NAD(P)HX at the expense of ADP, which is converted to AMP. Together with NAD(P)HX epimerase, which catalyzes the epimerization of the S- and R-forms, the enzyme allows the repair of both epimers of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Catalyzes the epimerization of the S- and R-forms of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADHX = (6S)-NADHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32215"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:64075"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000013"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6R)-NADPHX = (6S)-NADPHX","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32227"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:64077"}],"ecNumber":"5.1.99.6","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000909"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADHX + ADP = AMP + phosphate + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32223"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:64074"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048238"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:32235"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:64076"},{"database":"ChEBI","id":"CHEBI:456215"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"4.2.1.136","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"K(+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29103"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"Binds 1 potassium ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"value":"Belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009524"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the C-terminal section; belongs to the NnrD/CARKD family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006001"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR017184"}],"value":"In the N-terminal section; belongs to the NnrE/AIBP family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4834432.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":10,"modifier":"EXACT"},"end":{"value":213,"modifier":"EXACT"}},"description":"YjeF N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51385"}]},{"type":"Domain","location":{"start":{"value":220,"modifier":"EXACT"},"end":{"value":482,"modifier":"EXACT"}},"description":"YjeF C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51383"}]},{"type":"Binding site","location":{"start":{"value":62,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":63,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":129,"modifier":"EXACT"},"end":{"value":135,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":161,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29103"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"ligand":{"name":"K(+)","id":"ChEBI:CHEBI:29103"}},{"type":"Binding site","location":{"start":{"value":255,"modifier":"EXACT"},"end":{"value":255,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":308,"modifier":"EXACT"},"end":{"value":308,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":359,"modifier":"EXACT"},"end":{"value":359,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}},{"type":"Binding site","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":395,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":420,"modifier":"EXACT"},"end":{"value":420,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:456215"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"AMP","id":"ChEBI:CHEBI:456215"}},{"type":"Binding site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:64076"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"ligand":{"name":"(6S)-NADPHX","id":"ChEBI:CHEBI:64076"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01965"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022958"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01966"}],"id":"KW-0630","category":"Ligand","name":"Potassium"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000039","properties":[{"key":"ProteinId","value":"MFC4834432.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274190724.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000039.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0052855","properties":[{"key":"GoTerm","value":"F:ADP-dependent NAD(P)H-hydrate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0052856","properties":[{"key":"GoTerm","value":"F:NAD(P)HX epimerase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0110051","properties":[{"key":"GoTerm","value":"P:metabolite repair"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0046496","properties":[{"key":"GoTerm","value":"P:nicotinamide nucleotide metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd01171","properties":[{"key":"EntryName","value":"YXKO-related"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.10260","properties":[{"key":"EntryName","value":"YjeF N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01965","properties":[{"key":"EntryName","value":"NADHX_dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01966","properties":[{"key":"EntryName","value":"NADHX_epimerase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR017953","properties":[{"key":"EntryName","value":"Carbohydrate_kinase_pred_CS"}]},{"database":"InterPro","id":"IPR000631","properties":[{"key":"EntryName","value":"CARKD"}]},{"database":"InterPro","id":"IPR030677","properties":[{"key":"EntryName","value":"Nnr"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR004443","properties":[{"key":"EntryName","value":"YjeF_N_dom"}]},{"database":"InterPro","id":"IPR036652","properties":[{"key":"EntryName","value":"YjeF_N_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00196","properties":[{"key":"EntryName","value":"yjeF_cterm"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00197","properties":[{"key":"EntryName","value":"yjeF_nterm"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592:SF0","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12592","properties":[{"key":"EntryName","value":"ATP-DEPENDENT (S)-NAD(P)H-HYDRATE DEHYDRATASE FAMILY MEMBER"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01256","properties":[{"key":"EntryName","value":"Carb_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03853","properties":[{"key":"EntryName","value":"YjeF_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF017184","properties":[{"key":"EntryName","value":"Nnr"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF64153","properties":[{"key":"EntryName","value":"YjeF N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01049","properties":[{"key":"EntryName","value":"YJEF_C_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51383","properties":[{"key":"EntryName","value":"YJEF_C_3"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51385","properties":[{"key":"EntryName","value":"YJEF_N"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MYGVWTPEQVGAAEEPVLARTPEGALMRRAAHGVAQVALAELRRRTGGVAGRRVVVLVGAGNNGGDGLWAGDELRRRGVAVTAVLLSPDRAHPAGLAALRKQRGRIVTDVEHGVVAVDHADLVLDAIVGTGARGGLRPEAATLVDAARTTDVPILAVDTPSGVDPLTGVPGEHHVRAAATVTFGARKPVHVLAAPLCGPVTLIDIGLGPELPPAPVDVLDAADVGARWPVPGPGDDKYSQGVVGIAAGSRTYPGAAVLASGAAALSTSGMVRYAGSAADEVRAAWPEIVATDTVGEAGRVQAWVVGPGLGTDDAGAQTLADVLDTGLPVLADADAVTLLGQHAGLREKAAGAPVLITPHAGEFARVAELTDDRVDSARRAAADLGVTLLLKGNATVVAAPDGRVLVHPAGSAWLATAGSGDVLSGVAGALLAAGLEPWWAGGCAAFVHARAADIGAGADIGPGSPVPASHVQAALSTAIRQVREARG","length":487,"molWeight":48704,"crc64":"5E981327E28B2B65","md5":"79B004C4969EE07B3E4975577D04033E"},"extraAttributes":{"countByCommentType":{"FUNCTION":3,"CATALYTIC ACTIVITY":4,"COFACTOR":2,"SUBUNIT":1,"SIMILARITY":4,"CAUTION":2},"countByFeatureType":{"Domain":2,"Binding site":12},"uniParcId":"UPI0023666755"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RR23","uniProtkbId":"A0ABV9RR23_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836673.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"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":"MFC4836673.1"}],"value":"pdxT"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836673.1"}],"value":"ACFPEL_30015"}]}],"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":"MFC4836673.1"}],"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":80,"modifier":"EXACT"},"end":{"value":80,"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":182,"modifier":"EXACT"},"end":{"value":182,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":182,"modifier":"EXACT"},"end":{"value":182,"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":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"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":48,"modifier":"EXACT"},"end":{"value":50,"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":109,"modifier":"EXACT"},"end":{"value":109,"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":138,"modifier":"EXACT"},"end":{"value":139,"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":"UP001595909"}],"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":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000069","properties":[{"key":"ProteinId","value":"MFC4836673.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274191832.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000069.1"}]},{"database":"Proteomes","id":"UP001595909","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":"MSAPVGVLALQGNIPEHLDALRACGAEAVPVRRPSELAEVAGLVLPGGESTTLSKLLEAVELLEPLRERLRAGMPAFGSCAGMILLAREAIDARPDQHQLGALDITVRRNAFGRQVASFESDLAVTGVAGGPVRAVFIRAPWVESTGRGVEVLARVPGSVAGPASGKVVAVRQGPVMATAFHPEQTGDARLHDLFLRRVRDSVAAG","length":206,"molWeight":21504,"crc64":"4CC91BBDD18D7EF7","md5":"6897843FA9A78AA18B5F1790EC793936"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Active site":5,"Binding site":3},"uniParcId":"UPI002366330C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RRH1","uniProtkbId":"A0ABV9RRH1_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836114.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Bifunctional protein HldE"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 7-phosphate kinase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"2.7.1.167"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 7-phosphotransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-glycero-beta-D-manno-heptose-7-phosphate kinase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-beta-D-heptose 1-phosphate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"2.7.7.70"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836114.1"}],"value":"rfaE2"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"hldE"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836114.1"}],"value":"ACFPEL_27150"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Catalyzes the phosphorylation of D-glycero-D-manno-heptose 7-phosphate at the C-1 position to selectively form D-glycero-beta-D-manno-heptose-1,7-bisphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glycero-beta-D-manno-heptose 1-phosphate + ATP + H(+) = ADP-D-glycero-beta-D-manno-heptose + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27465"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:59967"},{"database":"ChEBI","id":"CHEBI:61593"}],"ecNumber":"2.7.7.70","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047428"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"D-glycero-beta-D-manno-heptose 7-phosphate + ATP = D-glycero-beta-D-manno-heptose 1,7-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:27473"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:60204"},{"database":"ChEBI","id":"CHEBI:60208"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.167","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004713"}],"value":"Bacterial outer membrane biogenesis; LPS core biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 1/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Nucleotide-sugar biosynthesis; ADP-L-glycero-beta-D-manno-heptose biosynthesis; ADP-L-glycero-beta-D-manno-heptose from D-glycero-beta-D-manno-heptose 7-phosphate: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"In the C-terminal section; belongs to the cytidylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"value":"In the N-terminal section; belongs to the carbohydrate kinase PfkB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836114.1"}],"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":342,"modifier":"EXACT"}},"description":"Carbohydrate kinase PfkB","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00294"}]},{"type":"Domain","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":479,"modifier":"EXACT"}},"description":"Cytidyltransferase-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01467"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":358,"modifier":"EXACT"}},"description":"Ribokinase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Region","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":512,"modifier":"EXACT"}},"description":"Cytidylyltransferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Active site","location":{"start":{"value":304,"modifier":"EXACT"},"end":{"value":304,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}]},{"type":"Binding site","location":{"start":{"value":230,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023277"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0119","category":"Biological process","name":"Carbohydrate metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"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_01603"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01603"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"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_01603"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000056","properties":[{"key":"ProteinId","value":"MFC4836114.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274191632.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000056.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033785","properties":[{"key":"GoTerm","value":"F:heptose 7-phosphate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033786","properties":[{"key":"GoTerm","value":"F:heptose-1-phosphate adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016773","properties":[{"key":"GoTerm","value":"F:phosphotransferase activity, alcohol group as acceptor"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005975","properties":[{"key":"GoTerm","value":"P:carbohydrate metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.40.1190.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01603","properties":[{"key":"EntryName","value":"HldE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023030","properties":[{"key":"EntryName","value":"Bifunc_HldE"}]},{"database":"InterPro","id":"IPR002173","properties":[{"key":"EntryName","value":"Carboh/pur_kinase_PfkB_CS"}]},{"database":"InterPro","id":"IPR004821","properties":[{"key":"EntryName","value":"Cyt_trans-like"}]},{"database":"InterPro","id":"IPR011611","properties":[{"key":"EntryName","value":"PfkB_dom"}]},{"database":"InterPro","id":"IPR011914","properties":[{"key":"EntryName","value":"RfaE_dom_II"}]},{"database":"InterPro","id":"IPR029056","properties":[{"key":"EntryName","value":"Ribokinase-like"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"TIGR00125","properties":[{"key":"EntryName","value":"cyt_tran_rel"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR02199","properties":[{"key":"EntryName","value":"rfaE_dom_II"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46969","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN HLDE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR46969:SF1","properties":[{"key":"EntryName","value":"BIFUNCTIONAL PROTEIN HLDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01467","properties":[{"key":"EntryName","value":"CTP_transf_like"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00294","properties":[{"key":"EntryName","value":"PfkB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53613","properties":[{"key":"EntryName","value":"Ribokinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00584","properties":[{"key":"EntryName","value":"PFKB_KINASES_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAAPEMSRLEAWSRPESPDLALAPLAADLPARLAAVAPRVVVVGDAVLDQWLTGPSRRLSREAPVPVVEVDHTHGSPGAAANTAANLAALGARTEFVSVLGDDADGATVREVLAGFGVGTAGVVTDPSRPTAAKRRVLADEALVARFDTSSREPLDADRRAAVHDALRAAVEGADAVVVCDYGGGIVDDETVALVGSLLDAPGERSCRLVVDAHDPARWAPARPEVVTPNAGEAKLLLGRELGGPDRVAAAEAAGPELRERSGAASVVVTLDRDGALLLPDDGSPTHRTFARPAPEANTCGAGDTFTAALALALAAGTPAATAVELAQAAADVVVGRPGTSVCGTGELAERVAAAEGPLLDAASLATIVHDQRVAGRRVVFTNGCFDVVHRGHVASLNQAKRLGDVLVVALNSDESVSRLKGPERPLNPLADRAAVIGALSCVDHVTAFDADTPAELLDLLRPDVYAKGGDYTPEMLRETATVTAYGGRVVILDYLPDRSTTSLVDRIRSGS","length":512,"molWeight":52693,"crc64":"0EAA394743B5A672","md5":"56C42ABA94CBAC59EA9EFEDCC129E7F1"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"PATHWAY":3,"SUBUNIT":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Active site":1,"Binding site":1},"uniParcId":"UPI002366C399"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RS70","uniProtkbId":"A0ABV9RS70_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836379.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067012"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Peroxidase/catalase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836379.1"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836379.1"}],"value":"ACFPEL_28500"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00056989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2 H2O2 = O2 + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20309"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"AH2 + H2O2 = A + 2 H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:30275"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:17499"}],"ecNumber":"1.11.1.21","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADH + O2 + H(+) = H2O2 + NAD(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11264"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"NADPH + O2 + H(+) = H2O2 + NADP(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11260"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:15379"},{"database":"ChEBI","id":"CHEBI:16240"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.6.3.1","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per dimer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Homodimer or homotetramer"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Formation of the three residue Trp-Tyr-Met cross-link is important for the catalase, but not the peroxidase activity of the enzyme"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00060838"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Belongs to the peroxidase family. Peroxidase/catalase subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836379.1"}],"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":149,"modifier":"EXACT"},"end":{"value":419,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Active site","location":{"start":{"value":98,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":262,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":94,"modifier":"EXACT"},"end":{"value":94,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]},{"type":"Cross-link","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":247,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-97)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0376","category":"Biological process","name":"Hydrogen peroxide"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01961"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000061","properties":[{"key":"ProteinId","value":"MFC4836379.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274191219.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000061.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0004096","properties":[{"key":"GoTerm","value":"F:catalase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016174","properties":[{"key":"GoTerm","value":"F:NAD(P)H oxidase H2O2-forming activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0070301","properties":[{"key":"GoTerm","value":"P:cellular response to hydrogen peroxide"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042744","properties":[{"key":"GoTerm","value":"P:hydrogen peroxide catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00649","properties":[{"key":"EntryName","value":"catalase_peroxidase_1"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.520.10:FF:000002","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF0","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNTEEAGGCPVDHGRLAHPTEGGGNVDWWPHQLNLRVLRSHTSVSNPMDPDFDYAKEFATVDLDALAADVDEVLTTSQDWWPADFGHYGGLMIRLAWHSAGTYRLADGRGGAGMGMQRFAPLNSWPDNGNLDKARRLLWPVKQKWGKKVSWADLLILAGNRSLDTMGLTTFGFAGGRPDVFEPDNETYWGPENYWLGGDQRYTGDRQLEKPLGASQMGLIYVNPEGPDGNPDPLAAARDIRETFGRMAMNDEETVALIAGGHTFGKTHGAADPDQYVGPEPEGASIEENGLGWKQSFGKGKGRDTITSGLEVTWTSTPVQWSNGYFDNLFGYEWELHKSPAGAWQYRPVDGGGANTVPDPETGELTRQPTMLVTDVSLKVDPVYKEISKRFHENPDEFADAFARAWFKLTHRDMGPIQRYVGPWVPQETLIWQDPVPAHEGALIGSTEIAELKKQILDTDLTVSQLVKAAWASASTFRIGDKRGGANGARVRLDPQIDWEVNDPQELRRTLSALEGVQSSFNASGTQVSLADLIVLGGCAAVEKAARDAGFDVSVPFTPGRTDASLEWTDVDSFTHLEPAADGFRNYLGKGHQLPAEYLLVDRANLLNLSAPQMTALVGGLRVLGANTGGSQHGVFTERVGQLTNDFFTNLLDMNTSWSKVAEEEGLYESRGADGEVRWTGTRNDLVFSSNSELRALAEIYAENGSEEKFVRDFVAAWDKVMMLDRYDVK","length":730,"molWeight":80277,"crc64":"BDF72C08ECF57D9F","md5":"43592DDC8113889B3E59D0DBAE721CEB"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":1,"Site":1,"Cross-link":1},"uniParcId":"UPI002366733C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RSH3","uniProtkbId":"A0ABV9RSH3_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836226.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024082"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Phosphatidylinositol phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"PIP synthase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"2.7.8.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033137"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"CDP-diacylglycerol--D-myo-inositol-3-phosphate 3-phosphatidyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836226.1"}],"value":"pgsA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836226.1"}],"value":"ACFPEL_27710"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Catalyzes the conjugation of the 1'-hydroxyl group of D-myo-inositol-3-phosphate (also named L-myo-inositol-1-phosphate) with a lipid tail of cytidine diphosphate diacylglycerol (CDP-DAG), forming phosphatidylinositol phosphate (PIP) and CMP. PIP is a precursor of phosphatidylinositol (PI) which is an essential lipid required for cell wall formation"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"1,2-di-(9Z-octadecenoyl)-sn-glycero-3-cytidine-5'-diphosphate + 1D-myo-inositol 3-phosphate = 1,2-di-(9Z-octadecenoyl)-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + CMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:61216"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58401"},{"database":"ChEBI","id":"CHEBI:60377"},{"database":"ChEBI","id":"CHEBI:85356"},{"database":"ChEBI","id":"CHEBI:144472"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023935"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a CDP-1,2-diacyl-sn-glycerol + 1D-myo-inositol 3-phosphate = a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol-3-phosphate) + CMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:60504"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:58088"},{"database":"ChEBI","id":"CHEBI:58332"},{"database":"ChEBI","id":"CHEBI:58401"},{"database":"ChEBI","id":"CHEBI:60377"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048865"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Contains a di-nuclear catalytic Mg(2+) center."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004805"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Phospholipid metabolism; phosphatidylinositol phosphate biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011738"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Cell membrane","id":"SL-0039"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004651"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010441"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003750"}],"value":"Belongs to the CDP-alcohol phosphatidyltransferase class-I family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836226.1"}],"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":43,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}]},{"type":"Transmembrane","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}]},{"type":"Transmembrane","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}]},{"type":"Region","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":233,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}]},{"type":"Binding site","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":32,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58332"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"a CDP-1,2-diacyl-sn-glycerol","id":"ChEBI:CHEBI:58332"}},{"type":"Binding site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":66,"modifier":"EXACT"},"end":{"value":66,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":69,"modifier":"EXACT"},"end":{"value":69,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":70,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58332"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"a CDP-1,2-diacyl-sn-glycerol","id":"ChEBI:CHEBI:58332"}},{"type":"Binding site","location":{"start":{"value":74,"modifier":"EXACT"},"end":{"value":74,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58332"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"a CDP-1,2-diacyl-sn-glycerol","id":"ChEBI:CHEBI:58332"}},{"type":"Binding site","location":{"start":{"value":80,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58332"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"a CDP-1,2-diacyl-sn-glycerol","id":"ChEBI:CHEBI:58332"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"1"}},{"type":"Binding site","location":{"start":{"value":87,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}},{"type":"Binding site","location":{"start":{"value":91,"modifier":"EXACT"},"end":{"value":91,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022475"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-1003","category":"Cellular component","name":"Cell membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"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_02241"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02241"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000059","properties":[{"key":"ProteinId","value":"MFC4836226.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274192268.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000059.1"}]},{"database":"Proteomes","id":"UP001595909","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:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016780","properties":[{"key":"GoTerm","value":"F:phosphotransferase activity, for other substituted phosphate groups"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008654","properties":[{"key":"GoTerm","value":"P:phospholipid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"1.20.120.1760","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02241","properties":[{"key":"EntryName","value":"PIP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR050324","properties":[{"key":"EntryName","value":"CDP-alcohol_PTase-I"}]},{"database":"InterPro","id":"IPR000462","properties":[{"key":"EntryName","value":"CDP-OH_P_trans"}]},{"database":"InterPro","id":"IPR043130","properties":[{"key":"EntryName","value":"CDP-OH_PTrfase_TM_dom"}]},{"database":"InterPro","id":"IPR048254","properties":[{"key":"EntryName","value":"CDP_ALCOHOL_P_TRANSF_CS"}]},{"database":"InterPro","id":"IPR044268","properties":[{"key":"EntryName","value":"PIP_synthase_PgsA1"}]},{"database":"NCBIfam","id":"NF045883","properties":[{"key":"EntryName","value":"PIPSynth"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14269:SF11","properties":[{"key":"EntryName","value":"CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14269","properties":[{"key":"EntryName","value":"CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01066","properties":[{"key":"EntryName","value":"CDP-OH_P_transf"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00379","properties":[{"key":"EntryName","value":"CDP_ALCOHOL_P_TRANSF"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MINQWARAAIKGGVEPTAAWLVRRGVHPDAVTVFGTVASTASALWLIPTGHLLAASIVVAVFALLDVLDGAMARARGVTSPFGGVLDSVGDRLVDGAVFAGITWWAFTQDRPLLAGLALACLITGQLISYIKARAEAAGLRADGGLVERAERLILGLAGVGLTEVGVPYALDVALWLLTIGSVITVGQRIVAVWHSAREQYGAATGVTDHADPSENIGRPENADHPESSEGTA","length":233,"molWeight":24178,"crc64":"BD0F78EBEE48FDEE","md5":"A6A408D55A3971A99616554462638A44"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Transmembrane":3,"Region":1,"Compositional bias":1,"Active site":1,"Binding site":10},"uniParcId":"UPI0023657C3F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RSJ8","uniProtkbId":"A0ABV9RSJ8_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4836147.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"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":"MFC4836147.1"}],"value":"ACFPEL_27315"}]}],"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":"MFC4836147.1"}],"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":288,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]},{"type":"Domain","location":{"start":{"value":482,"modifier":"EXACT"},"end":{"value":615,"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":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000057","properties":[{"key":"ProteinId","value":"MFC4836147.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274192153.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000057.1"}]},{"database":"Proteomes","id":"UP001595909","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":"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":"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":"MGHYRANVRDIEFNLFEVFRVQDRFGSGPFADADEETARALLGEVAAMAEGPLADSYESGDRNPVRFDPQTHTAHLDEGIKKSFHTLWDGEWWRLSADNEIGGMGVPPTVQWAAGEMILGANAPVFMYMAGPNFASVVYRNGTEQQKHWAQLMVDRGWGATMVLTEPDAGSDVGAGRTKARDNGDGTWSIEGVKRFITSGDAGDLNENIMHLVLARPEGARAGTKGLSLFLVPKFHFDPETGEPGERNGAFVTNVEHKMGLNASATCEVTFGGNGVPATGWLLGEVHDGIAQMFQVIEYARMMVGTKAIGTLSTGYLRALEYAKERIQGADLTRQTDKTAPRVPITNHPDVRRSLMLQKAYAEGLRAVYTFTSTYQDVVRFGEAPEADRGAVSAEDITLAEKVNDLLLPIVKGVGSERASEQLIQSLQTLGGSGYLQDYPIEQYIRDAKIDSLYEGTTAIQAQDFFFRKIVRDNGQALMHVAGQVQAFLDAEGGNGRLKEERQLLATALGDVQAMLGSMVGYLTSSQEDATNLYKVGQHAVRFLMSVGDMLIGWLLLRQAEVAGEVLDAGTAGRDRNFYEGKIAVARFFARNVLPELSSRRTIVEGAENSIMELDVASL","length":619,"molWeight":67592,"crc64":"6331E28E24364A95","md5":"2FA5CA2F766ADCCAB60253028E32382B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":9,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI0023658A60"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9R9C5","uniProtkbId":"A0ABV9R9C5_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830778.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"NAD-dependent protein deacetylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"2.3.1.286"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"Regulatory protein SIR2 homolog"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"cobB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830778.1"}],"value":"ACFPEL_00025"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"NAD-dependent protein deacetylase which modulates the activities of several enzymes which are inactive in their acetylated form"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"N(6)-acetyl-L-lysyl-[protein] + NAD(+) + H2O = 2''-O-acetyl-ADP-D-ribose + nicotinamide + L-lysyl-[protein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43636"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:17154"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:61930"},{"database":"ChEBI","id":"CHEBI:83767"}],"ecNumber":"2.3.1.286","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"Binds 1 zinc ion per subunit."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"Belongs to the sirtuin family. Class II subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830778.1"}],"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":291,"modifier":"EXACT"}},"description":"Deacetylase sirtuin-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50305"}]},{"type":"Active site","location":{"start":{"value":133,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00236"}]},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":141,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00236"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":144,"modifier":"EXACT"},"end":{"value":144,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00236"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":192,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00236"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":195,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00236"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":233,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":277,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"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_01967"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_01967"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000001","properties":[{"key":"ProteinId","value":"MFC4830778.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274189047.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000001.1"}]},{"database":"Proteomes","id":"UP001595909","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:0070403","properties":[{"key":"GoTerm","value":"F:NAD+ binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0034979","properties":[{"key":"GoTerm","value":"F:NAD-dependent protein lysine deacetylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008270","properties":[{"key":"GoTerm","value":"F:zinc ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.1600.10","properties":[{"key":"EntryName","value":"SIR2/SIRT2 'Small Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1220","properties":[{"key":"EntryName","value":"TPP-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01967","properties":[{"key":"EntryName","value":"Sirtuin_ClassII"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029035","properties":[{"key":"EntryName","value":"DHS-like_NAD/FAD-binding_dom"}]},{"database":"InterPro","id":"IPR050134","properties":[{"key":"EntryName","value":"NAD-dep_sirtuin_deacylases"}]},{"database":"InterPro","id":"IPR003000","properties":[{"key":"EntryName","value":"Sirtuin"}]},{"database":"InterPro","id":"IPR026591","properties":[{"key":"EntryName","value":"Sirtuin_cat_small_dom_sf"}]},{"database":"InterPro","id":"IPR026587","properties":[{"key":"EntryName","value":"Sirtuin_class_II"}]},{"database":"InterPro","id":"IPR026590","properties":[{"key":"EntryName","value":"Ssirtuin_cat_dom"}]},{"database":"NCBIfam","id":"NF003738","properties":[{"key":"EntryName","value":"PRK05333.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11085","properties":[{"key":"EntryName","value":"NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11085:SF10","properties":[{"key":"EntryName","value":"NAD-DEPENDENT PROTEIN DEACYLASE SIRTUIN-5, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02146","properties":[{"key":"EntryName","value":"SIR2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52467","properties":[{"key":"EntryName","value":"DHS-like NAD/FAD-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50305","properties":[{"key":"EntryName","value":"SIRTUIN"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRYTAPQTAWEAEVPVRGDVAALATLLAEGGAVVLTGAGISTDSGIPDYRGPTSAQRRHAPMTYDAFVGDPVARHRYWARSHVGWPQIAGARPNDGHRAVASLQRAGLLHGVITQNVDGLHQKAGARDVVELHGALGRVVCLGCRVALGRARVQEDLASLNPDFDTRATEINPDGDAELPDAELDRFTMTGCPSCGDGPLKPDVVFFGESVPRPRVDHCFELVERARSLVVLGSSLTVMSGLRFVRAAARRDLPVAVVTAGPSRADDVAAVRLTEALGEVLPATLATLGLGERP","length":294,"molWeight":31128,"crc64":"54E38DFBD11605AF","md5":"ADD125E5F9A5F1669CD5FDC1B21F2D14"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":7},"uniParcId":"UPI002366F523"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9R9E4","uniProtkbId":"A0ABV9R9E4_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830791.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012353"}],"value":"assimilatory sulfite reductase (ferredoxin)"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012353"}],"value":"1.8.7.1"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830791.1"}],"value":"nirB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830791.1"}],"value":"ACFPEL_00090"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003247"}],"value":"Catalyzes the reduction of sulfite to sulfide, a step in the biosynthesis of sulfur-containing amino acids and cofactors"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"hydrogen sulfide + 6 oxidized [2Fe-2S]-[ferredoxin] + 3 H2O = sulfite + 6 reduced [2Fe-2S]-[ferredoxin] + 7 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:23132"},{"database":"Rhea","id":"RHEA-COMP:10000"},{"database":"Rhea","id":"RHEA-COMP:10001"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17359"},{"database":"ChEBI","id":"CHEBI:29919"},{"database":"ChEBI","id":"CHEBI:33737"},{"database":"ChEBI","id":"CHEBI:33738"}],"ecNumber":"1.8.7.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049518"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"FAD","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001974"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR037149"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:57692"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"[2Fe-2S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034078"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:190135"}}]},{"commentType":"COFACTOR","cofactors":[{"name":"[4Fe-4S] cluster","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:49883"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"value":"Binds 1 [4Fe-4S] cluster per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"siroheme","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60052"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"value":"Binds 1 siroheme per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005096"}],"value":"Nitrogen metabolism; nitrate reduction (assimilation)"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010429"}],"value":"Belongs to the nitrite and sulfite reductase 4Fe-4S domain family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830791.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":328,"modifier":"EXACT"}},"description":"FAD/NAD(P)-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF07992"}]},{"type":"Domain","location":{"start":{"value":363,"modifier":"EXACT"},"end":{"value":430,"modifier":"EXACT"}},"description":"NADH-rubredoxin oxidoreductase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18267"}]},{"type":"Domain","location":{"start":{"value":463,"modifier":"EXACT"},"end":{"value":510,"modifier":"EXACT"}},"description":"BFD-like [2Fe-2S]-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF04324"}]},{"type":"Domain","location":{"start":{"value":599,"modifier":"EXACT"},"end":{"value":662,"modifier":"EXACT"}},"description":"Nitrite/Sulfite reductase ferredoxin-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03460"}]},{"type":"Domain","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":805,"modifier":"EXACT"}},"description":"Nitrite/sulphite reductase 4Fe-4S","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01077"}]},{"type":"Binding site","location":{"start":{"value":679,"modifier":"EXACT"},"end":{"value":679,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":685,"modifier":"EXACT"},"end":{"value":685,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":719,"modifier":"EXACT"},"end":{"value":719,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":723,"modifier":"EXACT"},"end":{"value":723,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:49883"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"ligand":{"name":"[4Fe-4S] cluster","id":"ChEBI:CHEBI:49883"}},{"type":"Binding site","location":{"start":{"value":723,"modifier":"EXACT"},"end":{"value":723,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60052"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"ligand":{"name":"siroheme","id":"ChEBI:CHEBI:60052"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022714"}],"id":"KW-0001","category":"Ligand","name":"2Fe-2S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022485"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"id":"KW-0004","category":"Ligand","name":"4Fe-4S"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022827"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR037149"}],"id":"KW-0274","category":"Ligand","name":"FAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022630"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR037149"}],"id":"KW-0285","category":"Ligand","name":"Flavoprotein"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023004"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023014"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"id":"KW-0411","category":"Ligand","name":"Iron-sulfur"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR037149-1"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023063"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR037149"}],"id":"KW-0534","category":"Biological process","name":"Nitrate assimilation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022784"}],"id":"KW-0883","category":"PTM","name":"Thioether bond"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000001","properties":[{"key":"ProteinId","value":"MFC4830791.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274188857.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000001.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0020037","properties":[{"key":"GoTerm","value":"F:heme binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0051536","properties":[{"key":"GoTerm","value":"F:iron-sulfur cluster binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050661","properties":[{"key":"GoTerm","value":"F:NADP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0098809","properties":[{"key":"GoTerm","value":"F:nitrite reductase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0050311","properties":[{"key":"GoTerm","value":"F:sulfite reductase (ferredoxin) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0042128","properties":[{"key":"GoTerm","value":"P:nitrate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"Gene3D","id":"3.30.390.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.480.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.1100","properties":[{"key":"EntryName","value":"BFD-like [2Fe-2S]-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.50.50.60","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.413.10","properties":[{"key":"EntryName","value":"Sulfite Reductase Hemoprotein, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR007419","properties":[{"key":"EntryName","value":"BFD-like_2Fe2S-bd_dom"}]},{"database":"InterPro","id":"IPR041854","properties":[{"key":"EntryName","value":"BFD-like_2Fe2S-bd_dom_sf"}]},{"database":"InterPro","id":"IPR036188","properties":[{"key":"EntryName","value":"FAD/NAD-bd_sf"}]},{"database":"InterPro","id":"IPR023753","properties":[{"key":"EntryName","value":"FAD/NAD-binding_dom"}]},{"database":"InterPro","id":"IPR016156","properties":[{"key":"EntryName","value":"FAD/NAD-linked_Rdtase_dimer_sf"}]},{"database":"InterPro","id":"IPR052034","properties":[{"key":"EntryName","value":"NasD-like"}]},{"database":"InterPro","id":"IPR005117","properties":[{"key":"EntryName","value":"NiRdtase/SiRdtase_haem-b_fer"}]},{"database":"InterPro","id":"IPR036136","properties":[{"key":"EntryName","value":"Nit/Sulf_reduc_fer-like_dom_sf"}]},{"database":"InterPro","id":"IPR012744","properties":[{"key":"EntryName","value":"Nitri_red_NirB"}]},{"database":"InterPro","id":"IPR017121","properties":[{"key":"EntryName","value":"Nitrite_Rdtase_lsu"}]},{"database":"InterPro","id":"IPR006067","properties":[{"key":"EntryName","value":"NO2/SO3_Rdtase_4Fe4S_dom"}]},{"database":"InterPro","id":"IPR045854","properties":[{"key":"EntryName","value":"NO2/SO3_Rdtase_4Fe4S_sf"}]},{"database":"InterPro","id":"IPR006066","properties":[{"key":"EntryName","value":"NO2/SO3_Rdtase_FeS/sirohaem_BS"}]},{"database":"InterPro","id":"IPR041575","properties":[{"key":"EntryName","value":"NROR_C"}]},{"database":"NCBIfam","id":"TIGR02374","properties":[{"key":"EntryName","value":"nitri_red_nirB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43809","properties":[{"key":"EntryName","value":"NITRITE REDUCTASE (NADH) LARGE SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43809:SF1","properties":[{"key":"EntryName","value":"NITRITE REDUCTASE (NADH) LARGE SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04324","properties":[{"key":"EntryName","value":"Fer2_BFD"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01077","properties":[{"key":"EntryName","value":"NIR_SIR"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03460","properties":[{"key":"EntryName","value":"NIR_SIR_ferr"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF07992","properties":[{"key":"EntryName","value":"Pyr_redox_2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18267","properties":[{"key":"EntryName","value":"Rubredoxin_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF037149","properties":[{"key":"EntryName","value":"NirB"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00368","properties":[{"key":"EntryName","value":"FADPNR"}]},{"database":"PRINTS","id":"PR00411","properties":[{"key":"EntryName","value":"PNDRDTASEI"}]},{"database":"PRINTS","id":"PR00397","properties":[{"key":"EntryName","value":"SIROHAEM"}]},{"database":"SUPFAM","id":"SSF51905","properties":[{"key":"EntryName","value":"FAD/NAD(P)-binding domain"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF56014","properties":[{"key":"EntryName","value":"Nitrite and sulphite reductase 4Fe-4S domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55124","properties":[{"key":"EntryName","value":"Nitrite/Sulfite reductase N-terminal domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00365","properties":[{"key":"EntryName","value":"NIR_SIR"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTQTAERPETEQENPSKTRLVVVGNGMSGARALEEILARGGGDTFAIEVFGDEPYGNYNRILLSEVLANAAGEAVDNEDADGEDELYLNPLDWYDENGITLHAGVRIVRIDRHAKVVYGDDGSVTPYDTLVLATGSRSFFPPMEGMWASKTELTPGVFGFRSLDDATSMLAHIAGDAAQRSSTLEKEHRTAVVIGGGLLGLEAAAGLQAHGVAVHVVHPTEVLMNQQLEAEASKVLRSKLEDMGMHLHLGVKTNEILTDEGRVSGVRFTDGSDLACDMVVVTAGIRPNIGLAMVSGLETQRAIVVDDKLRSVDDDSIFVVGECAQHRGEVYGVVGPLWEQAAVLADVVTGSNPHAEYHGSRLATKLKVAGVDVAQMGVKVPERSSDEFVQFSETGRGVYQTVVIRDGTLIGATLVGDVSKVAALTQAFDSRSALPEERIKLLFDLGSAADAASAADLPDDTQICNCNGVSKGDLVACVHDGAESVSACMAATRAGKGCGSCKGLVKEVVEAALGGAGAEDPAEHYYVPGIPLDKPTLMAEIRSRGLKSVSSVFAELAPDGKDHVGSKMGLTALLRMMWPDDHVDERDGRFINDRVHANIQRDGTFSVVPRMSGGVTSPDQLRRIADVADKHEIPMVKLTGGQRIDLLGVPKEKLQEVWADLDMPSGWAYGKSFRTVKTCVGTDFCRFGLGDSTTLGIDMEERYKGIEGPAKMKLAVSGCPRNCAESMVKDVGLVAIEGGQWQIYVGGAAGATIRKGDILATVDSHDEALRITGRFLQYYRENANWLERTYDFVPRMGLDHLIGVIVDDAEGIADELDARMQETVDRYADPWATDQTEATPGQFHDALPLVPLPQVPIRTSSSREGVSS","length":868,"molWeight":93031,"crc64":"65BCCC4C1F45F47E","md5":"DFB00C31D41522CDE825A5E92A8E3C2D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":4,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":5,"Binding site":5},"uniParcId":"UPI002365E437"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9R9P1","uniProtkbId":"A0ABV9R9P1_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830779.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Phosphoenolpyruvate carboxykinase [GTP]"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"PEP carboxykinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"PEPCK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"4.1.1.32"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"GTP-dependent phosphoenolpyruvate carboxykinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"GTP-PEPCK"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"pckG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830779.1"}],"value":"ACFPEL_00030"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Catalyzes the conversion of oxaloacetate (OAA) to phosphoenolpyruvate (PEP), the rate-limiting step in the metabolic pathway that produces glucose from lactate and other precursors derived from the citric acid cycle"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"oxaloacetate + GTP = phosphoenolpyruvate + GDP + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10388"},{"database":"ChEBI","id":"CHEBI:16452"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:37565"},{"database":"ChEBI","id":"CHEBI:58189"},{"database":"ChEBI","id":"CHEBI:58702"}],"ecNumber":"4.1.1.32","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10113"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Binds 1 Mn(2+) ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004742"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Carbohydrate biosynthesis; gluconeogenesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011245"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005796"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"value":"Belongs to the phosphoenolpyruvate carboxykinase [GTP] family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830779.1"}],"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":22,"modifier":"EXACT"},"end":{"value":243,"modifier":"EXACT"}},"description":"Phosphoenolpyruvate carboxykinase GTP-utilising N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF17297"}]},{"type":"Domain","location":{"start":{"value":247,"modifier":"EXACT"},"end":{"value":605,"modifier":"EXACT"}},"description":"Phosphoenolpyruvate carboxykinase C-terminal P-loop","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00821"}]},{"type":"Active site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10113"}]},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":222,"modifier":"EXACT"},"end":{"value":224,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":251,"modifier":"EXACT"},"end":{"value":251,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":274,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":298,"modifier":"EXACT"},"end":{"value":298,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035"}},{"type":"Binding site","location":{"start":{"value":388,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":390,"modifier":"EXACT"},"end":{"value":390,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":421,"modifier":"EXACT"},"end":{"value":421,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}},{"type":"Binding site","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":519,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:37565"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"ligand":{"name":"GTP","id":"ChEBI:CHEBI:37565"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022432"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0312","category":"Biological process","name":"Gluconeogenesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023134"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0342","category":"Ligand","name":"GTP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00452"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000001","properties":[{"key":"ProteinId","value":"MFC4830779.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274188845.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000001.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005525","properties":[{"key":"GoTerm","value":"F:GTP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004613","properties":[{"key":"GoTerm","value":"F:phosphoenolpyruvate carboxykinase (GTP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071333","properties":[{"key":"GoTerm","value":"P:cellular response to glucose stimulus"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006094","properties":[{"key":"GoTerm","value":"P:gluconeogenesis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006107","properties":[{"key":"GoTerm","value":"P:oxaloacetate metabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0019543","properties":[{"key":"GoTerm","value":"P:propionate catabolic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0033993","properties":[{"key":"GoTerm","value":"P:response to lipid"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042594","properties":[{"key":"GoTerm","value":"P:response to starvation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00819","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.449.10:FF:000005","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate carboxykinase [GTP]"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.228.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.449.10","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate Carboxykinase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.170.8.10","properties":[{"key":"EntryName","value":"Phosphoenolpyruvate Carboxykinase, domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00452","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018091","properties":[{"key":"EntryName","value":"PEP_carboxykin_GTP_CS"}]},{"database":"InterPro","id":"IPR013035","properties":[{"key":"EntryName","value":"PEP_carboxykinase_C"}]},{"database":"InterPro","id":"IPR008209","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP"}]},{"database":"InterPro","id":"IPR035077","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP_C"}]},{"database":"InterPro","id":"IPR035078","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP_N"}]},{"database":"InterPro","id":"IPR008210","properties":[{"key":"EntryName","value":"PEP_carboxykinase_N"}]},{"database":"NCBIfam","id":"NF003253","properties":[{"key":"EntryName","value":"PRK04210.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11561","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE CARBOXYKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11561:SF0","properties":[{"key":"EntryName","value":"PHOSPHOENOLPYRUVATE CARBOXYKINASE [GTP]-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00821","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17297","properties":[{"key":"EntryName","value":"PEPCK_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF001348","properties":[{"key":"EntryName","value":"PEP_carboxykinase_GTP"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF68923","properties":[{"key":"EntryName","value":"PEP carboxykinase N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53795","properties":[{"key":"EntryName","value":"PEP carboxykinase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00505","properties":[{"key":"EntryName","value":"PEPCK_GTP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAVPTIQGLDNPPIRRREVLDWVNEVADLTTPDRVVWCDGSQDEWDRLTSELVEAGTYVRLDPAKKPNSFYAASDPDDVARVEERTFICSVNEADAGVTNNWMDPAEMKATMRELYRGCMRGRTMYVIPFCMGPVNAEHPKLGVEISDSAYVVTSMHIMTRMGPEVQRRLDEGDTEWVPALHSVGAPLERGQQDVKWPCNDTKYISHFPDTREIWSFGSGYGGNALLGKKCYSLRIASAMARDEGWLAEHMLILKLISPEDKAYYIAAAFPSACGKTNLAMLQPTIPGWRAETVGDDIAWMRFGADGRLYAVNPEFGFFGVAPGTNWKTNPNAMRTIEQGNALFTNVALTDDGDVWWEGLEGDPEHLTAWTGDDWTPGSAKPAAHPNSRYTVPISQCPVVAPEWDDPQGVPISAILFGGRRKTTIPLVTESFDWQHGTFMGATMSSEMTAAAKGGKGQVRRDPMAMLPFLGYNVGDYFQHWVDVGKNADATKLPSIFYVNWFRRGEDNRFLWPGFGENSRVLKWIIERLEGKAAATETPIGHVPSADQIDVEGLSEPMEDIEASLRFDVDEWREELPLIEEWFAKIGDKLPTSMRDELDSLKQRLDAS","length":609,"molWeight":68061,"crc64":"F13D752E222E5FD8","md5":"0F22DD17CF8FD2540C0BCFB83F1A3B74"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":1,"Binding site":11},"uniParcId":"UPI002365F64D"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9R9V6","uniProtkbId":"A0ABV9R9V6_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830943.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"Glutamine-dependent NAD(+) synthetase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"6.3.5.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"NAD(+) synthase [glutamine-hydrolyzing]"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"value":"nadE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830943.1"}],"value":"ACFPEL_00855"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"value":"Catalyzes the ATP-dependent amidation of deamido-NAD to form NAD. Uses L-glutamine as a nitrogen source"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"deamido-NAD(+) + L-glutamine + ATP + H2O = L-glutamate + AMP + diphosphate + NAD(+) + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24384"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29985"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:58359"},{"database":"ChEBI","id":"CHEBI:58437"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"6.3.5.1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005188"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from deamido-NAD(+) (L-Gln route): step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR006630"}],"value":"In the C-terminal section; belongs to the NAD synthetase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4830943.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"CN hydrolase","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50263"}]},{"type":"Active site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":55,"modifier":"EXACT"},"end":{"value":55,"modifier":"EXACT"}},"description":"Proton acceptor; for glutaminase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}]},{"type":"Active site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":124,"modifier":"EXACT"},"end":{"value":124,"modifier":"EXACT"}},"description":"For glutaminase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}]},{"type":"Active site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}]},{"type":"Active site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Nucleophile; for glutaminase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}]},{"type":"Binding site","location":{"start":{"value":130,"modifier":"EXACT"},"end":{"value":130,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":206,"modifier":"EXACT"},"end":{"value":206,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":212,"modifier":"EXACT"},"end":{"value":212,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58359"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"L-glutamine","id":"ChEBI:CHEBI:58359"}},{"type":"Binding site","location":{"start":{"value":370,"modifier":"EXACT"},"end":{"value":377,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":460,"modifier":"EXACT"},"end":{"value":460,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":484,"modifier":"EXACT"},"end":{"value":484,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":489,"modifier":"EXACT"},"end":{"value":489,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":494,"modifier":"EXACT"},"end":{"value":497,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}},{"type":"Binding site","location":{"start":{"value":640,"modifier":"EXACT"},"end":{"value":640,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58437"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"ligand":{"name":"deamido-NAD(+)","id":"ChEBI:CHEBI:58437","note":"ligand shared between two neighboring subunits"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00054"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023027"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_02090"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000002","properties":[{"key":"ProteinId","value":"MFC4830943.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274190304.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000002.1"}]},{"database":"Proteomes","id":"UP001595909","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003952","properties":[{"key":"GoTerm","value":"F:NAD+ synthase (glutamine-hydrolyzing) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0008795","properties":[{"key":"GoTerm","value":"F:NAD+ synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009435","properties":[{"key":"GoTerm","value":"P:NAD+ biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd07570","properties":[{"key":"EntryName","value":"GAT_Gln-NAD-synth"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00553","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.1140:FF:000001","properties":[{"key":"EntryName","value":"Glutamine-dependent NAD(+) synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000155","properties":[{"key":"EntryName","value":"Glutamine-dependent NAD(+) synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.110.10:FF:000020","properties":[{"key":"EntryName","value":"Glutamine-dependent NAD(+) synthetase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.110.10","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.1140","properties":[{"key":"EntryName","value":"Glutamine-dependent NAD+ synthetase, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_02090","properties":[{"key":"EntryName","value":"NadE_glutamine_dep"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003010","properties":[{"key":"EntryName","value":"C-N_Hydrolase"}]},{"database":"InterPro","id":"IPR036526","properties":[{"key":"EntryName","value":"C-N_Hydrolase_sf"}]},{"database":"InterPro","id":"IPR014445","properties":[{"key":"EntryName","value":"Gln-dep_NAD_synthase"}]},{"database":"InterPro","id":"IPR041856","properties":[{"key":"EntryName","value":"NAD+_synth_C"}]},{"database":"InterPro","id":"IPR022310","properties":[{"key":"EntryName","value":"NAD/GMP_synthase"}]},{"database":"InterPro","id":"IPR003694","properties":[{"key":"EntryName","value":"NAD_synthase"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"NCBIfam","id":"NF002730","properties":[{"key":"EntryName","value":"PRK02628.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23090:SF9","properties":[{"key":"EntryName","value":"GLUTAMINE-DEPENDENT NAD(+) SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23090","properties":[{"key":"EntryName","value":"NH 3 /GLUTAMINE-DEPENDENT NAD + SYNTHETASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00795","properties":[{"key":"EntryName","value":"CN_hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02540","properties":[{"key":"EntryName","value":"NAD_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF006630","properties":[{"key":"EntryName","value":"NADS_GAT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52402","properties":[{"key":"EntryName","value":"Adenine nucleotide alpha hydrolases-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56317","properties":[{"key":"EntryName","value":"Carbon-nitrogen hydrolase"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50263","properties":[{"key":"EntryName","value":"CN_HYDROLASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPSPPFTSVYHQGFVRVAAATIRTTIAEPAANATSLLAVARECHDDGVGLVVFPELTLSGYSIEDLLMQDTLLDAAVDALGDVVAASAELTPVLVVGAPLRHRHRIYNCAVVVHRGRVLGVVPKTYLPNYREFYEPRQLAAGAGEGGTTRLLGEDVPFGSDLLFAATDVDGLVLHVEVCEDMFVPIPPSAEAALAGATVLANLSGSPITVGRADDRQLLARSASARCSAAYVYAAAGDGESTTEVSWDGQTSIHENGALLAETERFPAGERHAVADVDLRLLRSERLRMGTFDDNRRHREQTAGTTFRTVEFTLDPPTGDLGFRRDVERFPFVPTDPARLEQDCYEAYNIQVAGLLQRLRAIGDAKVVIGVSGGLDSTHALIVAARAMDRAGRPRSDILAFTLPGFATGERTKSNAERLSETLGVTFETIDITETARLMLRELGHPFSSGEPVYDVTFENVQAGLRTDYLFRAANQRGGIVVGTGDLSEAALGWSTYGVGDQMSHYTVNTGVPKTLVQHLIRWVISSEQFDDDVAEVLSDVLDTEISPELVPADSDQEIQSSEQRIGPYNLQDFTLYWVLRYGFRPSRIAFLAWHAWHDLDAGSWPPGFPDGDREAYDLAEIRQWLQVFAQRFFGFAQFKRSAMPNGPKVVAGGSLSPRGDWRAPSDSSATIWLEEIEAHVPES","length":684,"molWeight":74534,"crc64":"745D4522C637011B","md5":"7DA9D446344920D2F3353936E452D585"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":6,"Binding site":9},"uniParcId":"UPI0023667033"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RA10","uniProtkbId":"A0ABV9RA10_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831003.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Bifunctional glutamine synthetase adenylyltransferase/adenylyl-removing enzyme"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"ATP:glutamine synthetase adenylyltransferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"ATase"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Glutamine synthetase adenylyl-L-tyrosine phosphorylase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"2.7.7.89"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Adenylyl removase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AR"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AT-N"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Glutamine synthetase adenylyl transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"2.7.7.42"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Adenylyl transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AT"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"AT-C"}]}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"glnE"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831003.1"}],"value":"ACFPEL_01160"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Involved in the regulation of glutamine synthetase GlnA, a key enzyme in the process to assimilate ammonia. When cellular nitrogen levels are high, the C-terminal adenylyl transferase (AT) inactivates GlnA by covalent transfer of an adenylyl group from ATP to specific tyrosine residue of GlnA, thus reducing its activity. Conversely, when nitrogen levels are low, the N-terminal adenylyl removase (AR) activates GlnA by removing the adenylyl group by phosphorolysis, increasing its activity. The regulatory region of GlnE binds the signal transduction protein PII (GlnB) which indicates the nitrogen status of the cell"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[glutamine synthetase]-L-tyrosine + ATP = [glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18589"},{"database":"Rhea","id":"RHEA-COMP:10660"},{"database":"Rhea","id":"RHEA-COMP:10661"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"}],"ecNumber":"2.7.7.42","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[glutamine synthetase]-O(4)-(5'-adenylyl)-L-tyrosine + phosphate = [glutamine synthetase]-L-tyrosine + ADP","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43716"},{"database":"Rhea","id":"RHEA-COMP:10660"},{"database":"Rhea","id":"RHEA-COMP:10661"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:46858"},{"database":"ChEBI","id":"CHEBI:83624"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.7.89","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"value":"Belongs to the GlnE family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831003.1"}],"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":172,"modifier":"EXACT"},"end":{"value":350,"modifier":"EXACT"}},"description":"Glutamate-ammonia ligase adenylyltransferase repeated","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03710"}]},{"type":"Domain","location":{"start":{"value":375,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08335"}]},{"type":"Domain","location":{"start":{"value":626,"modifier":"EXACT"},"end":{"value":864,"modifier":"EXACT"}},"description":"Glutamate-ammonia ligase adenylyltransferase repeated","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF03710"}]},{"type":"Domain","location":{"start":{"value":889,"modifier":"EXACT"},"end":{"value":1029,"modifier":"EXACT"}},"description":"PII-uridylyltransferase/Glutamine-synthetase adenylyltransferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08335"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":525,"modifier":"EXACT"}},"description":"Adenylyl removase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]},{"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":"Region","location":{"start":{"value":533,"modifier":"EXACT"},"end":{"value":1034,"modifier":"EXACT"}},"description":"Adenylyl transferase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}]},{"type":"Compositional bias","location":{"start":{"value":9,"modifier":"EXACT"},"end":{"value":23,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"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_00802"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00802"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"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_00802"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000002","properties":[{"key":"ProteinId","value":"MFC4831003.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274190246.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000002.1"}]},{"database":"Proteomes","id":"UP001595909","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:0008882","properties":[{"key":"GoTerm","value":"F:[glutamate-ammonia-ligase] adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0047388","properties":[{"key":"GoTerm","value":"F:[glutamine synthetase]-adenylyl-L-tyrosine phosphorylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0062132","properties":[{"key":"GoTerm","value":"P:regulation of L-glutamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd05401","properties":[{"key":"EntryName","value":"NT_GlnE_GlnD_like"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.30.460.10","properties":[{"key":"EntryName","value":"Beta Polymerase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.20.120.330","properties":[{"key":"EntryName","value":"Nucleotidyltransferases domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_00802","properties":[{"key":"EntryName","value":"GlnE"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023057","properties":[{"key":"EntryName","value":"GlnE"}]},{"database":"InterPro","id":"IPR005190","properties":[{"key":"EntryName","value":"GlnE_rpt_dom"}]},{"database":"InterPro","id":"IPR043519","properties":[{"key":"EntryName","value":"NT_sf"}]},{"database":"InterPro","id":"IPR013546","properties":[{"key":"EntryName","value":"PII_UdlTrfase/GS_AdlTrfase"}]},{"database":"NCBIfam","id":"NF010707","properties":[{"key":"EntryName","value":"PRK14109.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30621:SF0","properties":[{"key":"EntryName","value":"BIFUNCTIONAL GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE_ADENYLYL-REMOVING ENZYME"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30621","properties":[{"key":"EntryName","value":"GLUTAMINE SYNTHETASE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08335","properties":[{"key":"EntryName","value":"GlnD_UR_UTase"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF03710","properties":[{"key":"EntryName","value":"GlnE"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF81301","properties":[{"key":"EntryName","value":"Nucleotidyltransferase"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF81593","properties":[{"key":"EntryName","value":"Nucleotidyltransferase substrate binding subunit/domain"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MTESAPSSRPAGRTGRAPARLGLTDPDAGTRLADLGWWDGDAPVEGTELAVWALARSPDPDLALLALERLRESLGEAEWATLAEALRVDQSLRGRLFGVLGGSTALGDHLVAHPERWRSLQSESTPGRTYDPSELPDLAERTRTLLTAVGAAEAGEDGAATPRATVLEPAGIGVLRLAYRDEVLALAAADLQSVCEPELPVVPVEVVAAQLADLASAGLRAALAVADATVADALGTKDDRQPGDPLPCRLGVIGMGKCGGRELNYVSDIDVIFVSDGPTDVATRLASTMMRVATEAFLEVDANLRPEGRQGALVRTLDGHVSYYRRWAKTWEFQALLKARPVAGDEELAREYCEAVDPMVWSAADRDDFVADVRAMRRRVEDHIRADHADREIKLGRGGLRDVEFAVQMLQMVHGRGDETIRSQNTLEALAALADGGYVGRDDAANLAASYRFLRMLEHRVQLQKMRRTHLFPSDDDTAGLRWLARAAKLRADGSRDAVGVLAHERSRHTVRVRRLHEKLFYRPLLESVARVPGEDLVLTSESANRRLKALGWTSPQGALGHLQALTSGVSRASRIQRALLPVLLDELGHTADPDHGLLAYRKVSEALAGTPWFLGYLRDEGVAAERLMRVLGTSRWVAELMPRTPEVLRLLAGDGPRAELVARRPEEVAASLRNAVGRHTDPASAGQVGRSMRRIELVRVACADILGLIDVTAVCEALSSIWVAVLQAALAAAERGLADGGGPPPARIAVIGMGRLGGGELGYSSDADVLFVCEPAEGVDDAEAVRHTKAVAEAAIAALGAPSPDPPLEVDTKLRPEGRSGPLVRTLASYRDYYAKLASTWEYQALLRARPVAGDEALGAAFVEAIDPYRYPADGLPDAQAVEIRRIKARVDNERMPRRADKALHTKLGTGGLADVEWTVQLLQLQHAGSVPSLRTPSTLEALDAAAKAGLIDAGDAEELAAGWTMATRARGAATLVRGRPTDEVPHSGRDLAAVASALGHDPDADPGEFLDEYRRVTRRARAVVDRVFYLVD","length":1034,"molWeight":111222,"crc64":"C318991727C4A454","md5":"F150BD2AFC61B8149947ACC483A5ADD4"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":4,"Region":3,"Compositional bias":1},"uniParcId":"UPI002365DCAD"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RA16","uniProtkbId":"A0ABV9RA16_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":5,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831016.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Probable cytosol aminopeptidase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"3.4.11.1"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Leucine aminopeptidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"LAP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"3.4.11.10"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Leucyl aminopeptidase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"pepA"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831016.1"}],"value":"ACFPEL_01225"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049972"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.","ecNumber":"3.4.11.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000135"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.","ecNumber":"3.4.11.10","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000967"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Binds 2 manganese ions per subunit."}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009528"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"value":"Belongs to the peptidase M17 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831016.1"}],"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":46,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Peptidase M17 leucyl aminopeptidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02789"}]},{"type":"Domain","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":495,"modifier":"EXACT"}},"description":"Peptidase M17 leucyl aminopeptidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00883"}]},{"type":"Active site","location":{"start":{"value":282,"modifier":"EXACT"},"end":{"value":282,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]},{"type":"Active site","location":{"start":{"value":356,"modifier":"EXACT"},"end":{"value":356,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}]},{"type":"Binding site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":275,"modifier":"EXACT"},"end":{"value":275,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":293,"modifier":"EXACT"},"end":{"value":293,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}},{"type":"Binding site","location":{"start":{"value":352,"modifier":"EXACT"},"end":{"value":352,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"1"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29035"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"ligand":{"name":"Mn(2+)","id":"ChEBI:CHEBI:29035","label":"2"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022438"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0031","category":"Molecular function","name":"Aminopeptidase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00181"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000002","properties":[{"key":"ProteinId","value":"MFC4831016.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274190234.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000002.1"}]},{"database":"Proteomes","id":"UP001595909","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:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070006","properties":[{"key":"GoTerm","value":"F:metalloaminopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00433","properties":[{"key":"EntryName","value":"Peptidase_M17"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.220.10","properties":[{"key":"EntryName","value":"Leucine Aminopeptidase, subunit E, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.10","properties":[{"key":"EntryName","value":"Zn peptidases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00181","properties":[{"key":"EntryName","value":"Cytosol_peptidase_M17"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR064115","properties":[{"key":"EntryName","value":"LAP_cs"}]},{"database":"InterPro","id":"IPR011356","properties":[{"key":"EntryName","value":"Leucine_aapep/pepB"}]},{"database":"InterPro","id":"IPR043472","properties":[{"key":"EntryName","value":"Macro_dom-like"}]},{"database":"InterPro","id":"IPR000819","properties":[{"key":"EntryName","value":"Peptidase_M17_C"}]},{"database":"InterPro","id":"IPR023042","properties":[{"key":"EntryName","value":"Peptidase_M17_leu_NH2_pept"}]},{"database":"InterPro","id":"IPR008283","properties":[{"key":"EntryName","value":"Peptidase_M17_N"}]},{"database":"NCBIfam","id":"NF002073","properties":[{"key":"EntryName","value":"PRK00913.1-2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11963:SF23","properties":[{"key":"EntryName","value":"CYTOSOL AMINOPEPTIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11963","properties":[{"key":"EntryName","value":"LEUCINE AMINOPEPTIDASE-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00883","properties":[{"key":"EntryName","value":"Peptidase_M17"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02789","properties":[{"key":"EntryName","value":"Peptidase_M17_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00481","properties":[{"key":"EntryName","value":"LAMNOPPTDASE"}]},{"database":"SUPFAM","id":"SSF52949","properties":[{"key":"EntryName","value":"Macro domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53187","properties":[{"key":"EntryName","value":"Zn-dependent exopeptidases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00631","properties":[{"key":"EntryName","value":"CYTOSOL_AP"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSTPDLDLLGADPGADALAGVDAVVVGVRPGIDGADPAVAGPTSALGDLAGELPGLVALLGGTGKAEEVTRVPTRGTIGAPLVVAVGLGAEPGDTGAAGETPDLAEQVRRGAGAAARTLHGHAAHVVTTLSALDLAAAIEGTLLGDYAFTDYKKAPETAPTELTRVGLVGDGDEAAVTRAVAVVRAVRNARDLVNTPPNDLYPDAFAERARSLAEAAGVSVEILDESALAEHGYGGVLGVGGGSSRPPRLVRLTYSPANPRKKVALVGKGITFDTGGISIKPAANMDHMTSDMSGAAGVVAATCLAADLGLDVEVVATVPMAENMPSGTAYRPGDVLKMYGGTTVEVLNTDAEGRLVLGDAIARACEDSPDYLLETSTLTGAQLVALGSRTPGVMGTDEFRDRVAAHAVAAGDGGWAMPLPDELRSDLDSRVADLANVTNHRFGGMLVGGIFLREFVADGVPWVHLDIAGPAFNTGGPHGYTPKGGTGVPVRTIAAVLDDIARNG","length":506,"molWeight":51040,"crc64":"08E0F70EE11067C8","md5":"C6AA9C4C78D1A117EE5C999EC21368DD"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Active site":2,"Binding site":7},"uniParcId":"UPI0023662BA9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0ABV9RA18","uniProtkbId":"A0ABV9RA18_9PSEU","entryAudit":{"firstPublicDate":"2025-10-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2025-10-08","entryVersion":4,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Actinomycetospora chibensis","taxonId":663606,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831011.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"lineage":["Bacteria","Bacillati","Actinomycetota","Actinomycetes","Pseudonocardiales","Pseudonocardiaceae","Actinomycetospora"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Octanoyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"2.3.1.181"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Lipoate-protein ligase B"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Lipoyl/octanoyl transferase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Octanoyl-[acyl-carrier-protein]-protein N-octanoyltransferase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831011.1"}],"value":"lipB"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831011.1"}],"value":"ACFPEL_01200"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024732"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Catalyzes the transfer of endogenously produced octanoic acid from octanoyl-acyl-carrier-protein onto the lipoyl domains of lipoate-dependent enzymes. Lipoyl-ACP can also act as a substrate although octanoyl-ACP is likely to be the physiological substrate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"octanoyl-[ACP] + L-lysyl-[protein] = N(6)-octanoyl-L-lysyl-[protein] + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17665"},{"database":"Rhea","id":"RHEA-COMP:9636"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:9928"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78463"},{"database":"ChEBI","id":"CHEBI:78809"}],"ecNumber":"2.3.1.181","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004821"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Protein modification; protein lipoylation via endogenous pathway; protein N(6)-(lipoyl)lysine from octanoyl-[acyl-carrier-protein]: step 1/2"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"value":"In the reaction, the free carboxyl group of octanoic acid is attached via an amide linkage to the epsilon-amino group of a specific lysine residue of lipoyl domains of lipoate-dependent enzymes"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016262"}],"value":"Belongs to the LipB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"MFC4831011.1"}],"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":38,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"BPL/LPL catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51733"}]},{"type":"Active site","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Acyl-thioester intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-1"}]},{"type":"Binding site","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":83,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":148,"modifier":"EXACT"},"end":{"value":150,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Binding site","location":{"start":{"value":161,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-2"}],"ligand":{"name":"substrate"}},{"type":"Site","location":{"start":{"value":145,"modifier":"EXACT"},"end":{"value":145,"modifier":"EXACT"}},"description":"Lowers pKa of active site Cys","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR016262-3"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023315"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"id":"KW-0012","category":"Molecular function","name":"Acyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_00013"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"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_00013"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"30832757","citationType":"journal article","authoringGroup":["The Broad Institute Genomics Platform","The Broad Institute Genome Sequencing Center for Infectious Disease"],"authors":["Wu L.","Ma J."],"citationCrossReferences":[{"database":"PubMed","id":"30832757"},{"database":"DOI","id":"10.1099/ijsem.0.003276"}],"title":"The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing project: providing services to taxonomists for standard genome sequencing and annotation.","publicationDate":"2019","journal":"Int. J. Syst. Evol. Microbiol.","firstPage":"895","lastPage":"898","volume":"69"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}],"value":"CCUG 50347","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001595909"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JBHSIM010000002","properties":[{"key":"ProteinId","value":"MFC4831011.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"WP_274190239.1","properties":[{"key":"NucleotideSequenceId","value":"NZ_BAABHN010000002.1"}]},{"database":"Proteomes","id":"UP001595909","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:0033819","properties":[{"key":"GoTerm","value":"F:lipoyl(octanoyl) transferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0009249","properties":[{"key":"GoTerm","value":"P:protein lipoylation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16444","properties":[{"key":"EntryName","value":"LipB"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.930.10","properties":[{"key":"EntryName","value":"Bira Bifunctional Protein, Domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00013","properties":[{"key":"EntryName","value":"LipB"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045864","properties":[{"key":"EntryName","value":"aa-tRNA-synth_II/BPL/LPL"}]},{"database":"InterPro","id":"IPR004143","properties":[{"key":"EntryName","value":"BPL_LPL_catalytic"}]},{"database":"InterPro","id":"IPR000544","properties":[{"key":"EntryName","value":"Octanoyltransferase"}]},{"database":"InterPro","id":"IPR020605","properties":[{"key":"EntryName","value":"Octanoyltransferase_CS"}]},{"database":"NCBIfam","id":"NF010925","properties":[{"key":"EntryName","value":"lipB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00214","properties":[{"key":"EntryName","value":"lipB"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10993:SF7","properties":[{"key":"EntryName","value":"LIPOYLTRANSFERASE 2, MITOCHONDRIAL-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10993","properties":[{"key":"EntryName","value":"OCTANOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21948","properties":[{"key":"EntryName","value":"LplA-B_cat"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF016262","properties":[{"key":"EntryName","value":"LPLase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55681","properties":[{"key":"EntryName","value":"Class II aaRS and biotin synthetases"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51733","properties":[{"key":"EntryName","value":"BPL_LPL_CATALYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01313","properties":[{"key":"EntryName","value":"LIPB"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSRSSRAAAEPVEVHEIGTVDYQEAWDAQRAHADARVDGGPDVLLLLEHPSVYTAGKRTLPEERPADGTPVVDVDRGGKITWHGPGQLVGYPIIGLAQPFDVVDHVRRLEQALITVCDSYGLATGRIDGRSGVWLPADDRGPARKIAAIGVRVARGVTLHGFALNADPDLAAFGAIVPCGIRDAGVTSLTAELGRTVSVDEVRAATREAVLAALEGDLEVTDRTLAVDEPREVTVGGLTVRVGTPAGA","length":248,"molWeight":26057,"crc64":"B328FC6C7740D971","md5":"5E5E1C7CF5D44B0618172DF85CD339DE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Active site":1,"Binding site":3,"Site":1},"uniParcId":"UPI0023661B7A"}}]}