{"results":[{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"Q8HG55","uniProtkbId":"CYB_AKAMU","entryAudit":{"firstPublicDate":"2005-12-06","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2003-03-01","entryVersion":97,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"value":"Cytochrome b"}},"alternativeNames":[{"fullName":{"value":"Complex III subunit 3"}},{"fullName":{"value":"Complex III subunit III"}},{"fullName":{"value":"Cytochrome b-c1 complex subunit 3"}},{"fullName":{"value":"Ubiquinol-cytochrome-c reductase complex cytochrome b subunit"}}]},"genes":[{"geneName":{"value":"cob"},"synonyms":[{"value":"cytB"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}],"value":"Component of the ubiquinol-cytochrome c reductase complex (complex III or cytochrome b-c1 complex) that is part of the mitochondrial respiratory chain. The b-c1 complex mediates electron transfer from ubiquinol to cytochrome c. Contributes to the generation of a proton gradient across the mitochondrial membrane that is then used for ATP synthesis"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"heme b","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}],"value":"Binds 2 heme b groups non-covalently."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}],"value":"Fungal cytochrome b-c1 complex contains 10 subunits; 3 respiratory subunits, 2 core proteins and 5 low-molecular weight proteins. Cytochrome b-c1 complex is a homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250"}],"value":"Heme 1 (or BL or b562) is low-potential and absorbs at about 562 nm, and heme 2 (or BH or b566) is high-potential and absorbs at about 566 nm"}],"commentType":"MISCELLANEOUS"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00967"},{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00968"}],"value":"Belongs to the cytochrome b family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}],"value":"The protein contains only eight transmembrane helices, not nine as predicted by bioinformatics tools"}],"commentType":"CAUTION"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Cytochrome b","featureId":"PRO_0000061746"},{"type":"Transmembrane","location":{"start":{"value":32,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Transmembrane","location":{"start":{"value":76,"modifier":"EXACT"},"end":{"value":98,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Transmembrane","location":{"start":{"value":113,"modifier":"EXACT"},"end":{"value":133,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Transmembrane","location":{"start":{"value":179,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Transmembrane","location":{"start":{"value":226,"modifier":"EXACT"},"end":{"value":246,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Transmembrane","location":{"start":{"value":290,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Transmembrane","location":{"start":{"value":322,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Transmembrane","location":{"start":{"value":349,"modifier":"EXACT"},"end":{"value":369,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00163"}]},{"type":"Binding site","location":{"start":{"value":82,"modifier":"EXACT"},"end":{"value":82,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"b562"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":96,"modifier":"EXACT"},"end":{"value":96,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"b566"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"b562"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":197,"modifier":"EXACT"},"end":{"value":197,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00968"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344","label":"b566"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":202,"modifier":"EXACT"},"end":{"value":202,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16389"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P00157"}],"ligand":{"name":"a ubiquinone","id":"ChEBI:CHEBI:16389"}}],"geneLocations":[{"geneEncodingType":"Mitochondrion"}],"keywords":[{"id":"KW-0249","category":"Biological process","name":"Electron transport"},{"id":"KW-0349","category":"Ligand","name":"Heme"},{"id":"KW-0408","category":"Ligand","name":"Iron"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"id":"KW-0679","category":"Biological process","name":"Respiratory chain"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"id":"KW-0813","category":"Biological process","name":"Transport"},{"id":"KW-0830","category":"Ligand","name":"Ubiquinone"}],"references":[{"referenceNumber":1,"citation":{"id":"15341915","citationType":"journal article","authors":["Kouvelis V.N.","Ghikas D.V.","Typas M.A."],"citationCrossReferences":[{"database":"PubMed","id":"15341915"},{"database":"DOI","id":"10.1016/j.fgb.2004.07.003"}],"title":"The analysis of the complete mitochondrial genome of Lecanicillium muscarium (synonym Verticillium lecanii) suggests a minimum common gene organization in mtDNAs of Sordariomycetes: phylogenetic implications.","publicationDate":"2004","journal":"Fungal Genet. Biol.","firstPage":"930","lastPage":"940","volume":"41"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"AF487277","properties":[{"key":"ProteinId","value":"AAO14664.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"NP_775403.1","properties":[{"key":"NucleotideSequenceId","value":"NC_004514.1"}]},{"database":"AlphaFoldDB","id":"Q8HG55","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"Q8HG55","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"806193","properties":[{"key":"Description","value":"-"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"ISS:UniProtKB"}]},{"database":"GO","id":"GO:0045275","properties":[{"key":"GoTerm","value":"C:respiratory chain complex III"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008121","properties":[{"key":"GoTerm","value":"F:quinol-cytochrome-c reductase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006122","properties":[{"key":"GoTerm","value":"P:mitochondrial electron transport, ubiquinol to cytochrome c"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00290","properties":[{"key":"EntryName","value":"cytochrome_b_C"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00284","properties":[{"key":"EntryName","value":"Cytochrome_b_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.810.10:FF:000002","properties":[{"key":"EntryName","value":"Cytochrome b"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.810.10","properties":[{"key":"EntryName","value":"Cytochrome Bc1 Complex, Chain C"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR005798","properties":[{"key":"EntryName","value":"Cyt_b/b6_C"}]},{"database":"InterPro","id":"IPR036150","properties":[{"key":"EntryName","value":"Cyt_b/b6_C_sf"}]},{"database":"InterPro","id":"IPR005797","properties":[{"key":"EntryName","value":"Cyt_b/b6_N"}]},{"database":"InterPro","id":"IPR027387","properties":[{"key":"EntryName","value":"Cytb/b6-like_sf"}]},{"database":"InterPro","id":"IPR030689","properties":[{"key":"EntryName","value":"Cytochrome_b"}]},{"database":"InterPro","id":"IPR048260","properties":[{"key":"EntryName","value":"Cytochrome_b_C_euk/bac"}]},{"database":"InterPro","id":"IPR048259","properties":[{"key":"EntryName","value":"Cytochrome_b_N_euk/bac"}]},{"database":"InterPro","id":"IPR016174","properties":[{"key":"EntryName","value":"Di-haem_cyt_TM"}]},{"database":"PANTHER","id":"PTHR19271","properties":[{"key":"EntryName","value":"CYTOCHROME B"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR19271:SF16","properties":[{"key":"EntryName","value":"CYTOCHROME B"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00032","properties":[{"key":"EntryName","value":"Cytochrom_B_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00033","properties":[{"key":"EntryName","value":"Cytochrome_B"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF038885","properties":[{"key":"EntryName","value":"COB"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81648","properties":[{"key":"EntryName","value":"a domain/subunit of cytochrome bc1 complex (Ubiquinol-cytochrome c reductase)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81342","properties":[{"key":"EntryName","value":"Transmembrane di-heme cytochromes"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51003","properties":[{"key":"EntryName","value":"CYTB_CTER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51002","properties":[{"key":"EntryName","value":"CYTB_NTER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRILKSHPLLKLLNAYIIDHSQPTNINYLWNFGSLLGLCLGIQIITGVTLAMHYNPSVAEAFNSVEHIMRDVNNGWLIRYLHSNTASAFFFLVYLHIGRGFYYGSYRSPRTLAWILGVIILILMMGIGFLGYVLPYGQMSLWGATVITNLISAIPWIGQDIVEFIWGGFSVNNATLNRFFALHFVLPFVLAALVIMHLIAVHETAGASNPLGTPAYYDRIPFAPYYLFKDLITIFLFMFGLSIFVFFMPNVLGDSENYIMANPMQTPAAIVPEWYLLPFYAILRSIPNKLLGVIAMFASLVILMVLPKTDLGITKGLQFRPLSKIAFYLFVTNFLLLLQLGAKHVESPFIEFGQISTALYFAYYLIIMPGVSILENTLIDLSQKG","length":385,"molWeight":43339,"crc64":"505CD68116E40545","md5":"CB428922CF5334F18070073F4D47622D"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"MISCELLANEOUS":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":1,"Transmembrane":8,"Binding site":5},"uniParcId":"UPI000009A8B4"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QN91","uniProtkbId":"A0A9W8QN91_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":14,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165048.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00081752"}],"value":"Pyrimidine-specific carbamoyl phosphate synthase-aspartate carbamoyl transferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013008"}],"value":"2.1.3.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012918"}],"value":"3.5.1.2"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044063"}],"value":"6.3.4.16"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012738"}],"value":"6.3.5.5"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165048.1"}],"value":"LMH87_006695"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058513"}],"value":"Multifunctional protein that encodes the first 2 enzymatic activities of the de novo pyrimidine pathway: carbamoylphosphate synthetase (CPSase; EC 6.3.5.5) and aspartate transcarbamylase (ATCase; EC 2.1.3.2). The CPSase-function is accomplished in 2 steps, by a glutamine-dependent amidotransferase activity (GATase) that binds and cleaves glutamine to produce ammonia, followed by an ammonium-dependent carbamoyl phosphate synthetase, which reacts with the ammonia, hydrogencarbonate and ATP to form carbamoyl phosphate. The endogenously produced carbamoyl phosphate is sequestered and channeled to the ATCase active site. ATCase then catalyzes the formation of carbamoyl-L-aspartate from L-aspartate and carbamoyl phosphate"}],"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"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"carbamoyl phosphate + L-aspartate = N-carbamoyl-L-aspartate + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20013"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29991"},{"database":"ChEBI","id":"CHEBI:32814"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58228"}],"ecNumber":"2.1.3.2","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048859"}]}},{"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"}]}},{"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"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001947"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004812"}],"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":"ARBA00004852"}],"value":"Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043998"}],"value":"In the 2nd section; belongs to the CarB family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043968"}],"value":"In the 3rd section; belongs to the metallo-dependent hydrolases superfamily. DHOase family. CAD subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043979"}],"value":"In the C-terminal section; belongs to the aspartate/ornithine carbamoyltransferase superfamily. ATCase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043984"}],"value":"In the N-terminal section; belongs to the CarA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165048.1"}],"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":567,"modifier":"EXACT"},"end":{"value":759,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1104,"modifier":"EXACT"},"end":{"value":1295,"modifier":"EXACT"}},"description":"ATP-grasp","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50975"}]},{"type":"Domain","location":{"start":{"value":1361,"modifier":"EXACT"},"end":{"value":1509,"modifier":"EXACT"}},"description":"MGS-like","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51855"}]},{"type":"Region","location":{"start":{"value":1861,"modifier":"EXACT"},"end":{"value":1883,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":305,"modifier":"EXACT"},"end":{"value":305,"modifier":"EXACT"}},"description":"Nucleophile","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]},{"type":"Active site","location":{"start":{"value":391,"modifier":"EXACT"},"end":{"value":391,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00605"}],"id":"KW-0315","category":"Domain","name":"Glutamine amidotransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022598"}],"id":"KW-0436","category":"Molecular function","name":"Ligase"},{"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":"PROSITE-ProRule","id":"PRU00409"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022975"}],"id":"KW-0665","category":"Biological process","name":"Pyrimidine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165048.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165048.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000001","properties":[{"key":"ProteinId","value":"KAJ4165048.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056059963.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056204625.1"}]},{"database":"GeneID","id":"80893854","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_006695","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 1"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016597","properties":[{"key":"GoTerm","value":"F:amino acid binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004070","properties":[{"key":"GoTerm","value":"F:aspartate carbamoyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"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-EC"}]},{"database":"GO","id":"GO:0004151","properties":[{"key":"GoTerm","value":"F:dihydroorotase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004359","properties":[{"key":"GoTerm","value":"F:glutaminase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046872","properties":[{"key":"GoTerm","value":"F:metal ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006207","properties":[{"key":"GoTerm","value":"P:'de novo' pyrimidine nucleobase biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0019240","properties":[{"key":"GoTerm","value":"P:L-citrulline biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006541","properties":[{"key":"GoTerm","value":"P:L-glutamine metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006228","properties":[{"key":"GoTerm","value":"P:UTP biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd01744","properties":[{"key":"EntryName","value":"GATase1_CPSase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01423","properties":[{"key":"EntryName","value":"MGS_CPS_I_III"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000002","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000036","properties":[{"key":"EntryName","value":"Aspartate carbamoyltransferase catalytic subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.880:FF:000025","properties":[{"key":"EntryName","value":"Bifunctional pyrimidine biosynthesis protein"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1370:FF:000005","properties":[{"key":"EntryName","value":"CAD protein-like isoform X1"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000004","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase (glutamine-hydrolyzing)"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.50.30.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase 1, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1030.10:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.140:FF:000036","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.470.20:FF:000001","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.20:FF:000002","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase large chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1380:FF:000009","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase, large subunit"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.20","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.880","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1370","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"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":"3.50.30.20","properties":[{"key":"EntryName","value":"Carbamoyl-phosphate synthase small subunit, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"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":"3.20.20.140","properties":[{"key":"EntryName","value":"Metal-dependent hydrolases"},{"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_01209","properties":[{"key":"EntryName","value":"CPSase_S_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006132","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoyltranf_P-bd"}]},{"database":"InterPro","id":"IPR006130","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase"}]},{"database":"InterPro","id":"IPR036901","properties":[{"key":"EntryName","value":"Asp/Orn_carbamoylTrfase_sf"}]},{"database":"InterPro","id":"IPR002082","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf"}]},{"database":"InterPro","id":"IPR006131","properties":[{"key":"EntryName","value":"Asp_carbamoyltransf_Asp/Orn-bd"}]},{"database":"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":"IPR006274","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu"}]},{"database":"InterPro","id":"IPR002474","properties":[{"key":"EntryName","value":"CarbamoylP_synth_ssu_N"}]},{"database":"InterPro","id":"IPR036480","properties":[{"key":"EntryName","value":"CarbP_synth_ssu_N_sf"}]},{"database":"InterPro","id":"IPR029062","properties":[{"key":"EntryName","value":"Class_I_gatase-like"}]},{"database":"InterPro","id":"IPR005479","properties":[{"key":"EntryName","value":"CPAse_ATP-bd"}]},{"database":"InterPro","id":"IPR005483","properties":[{"key":"EntryName","value":"CPSase_dom"}]},{"database":"InterPro","id":"IPR035686","properties":[{"key":"EntryName","value":"CPSase_GATase1"}]},{"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":"IPR017926","properties":[{"key":"EntryName","value":"GATASE"}]},{"database":"InterPro","id":"IPR032466","properties":[{"key":"EntryName","value":"Metal_Hydrolase"}]},{"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":"IPR016185","properties":[{"key":"EntryName","value":"PreATP-grasp_dom_sf"}]},{"database":"NCBIfam","id":"TIGR00670","properties":[{"key":"EntryName","value":"asp_carb_tr"},{"key":"MatchStatus","value":"1"}]},{"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":"TIGR01368","properties":[{"key":"EntryName","value":"CPSaseIIsmall"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF002032","properties":[{"key":"EntryName","value":"PRK00856.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009455","properties":[{"key":"EntryName","value":"PRK12815.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF009475","properties":[{"key":"EntryName","value":"PRK12838.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR11405:SF5","properties":[{"key":"EntryName","value":"CAD PROTEIN"},{"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":"PF00988","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00117","properties":[{"key":"EntryName","value":"GATase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02142","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00185","properties":[{"key":"EntryName","value":"OTCace"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02729","properties":[{"key":"EntryName","value":"OTCace_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00100","properties":[{"key":"EntryName","value":"AOTCASE"}]},{"database":"PRINTS","id":"PR00101","properties":[{"key":"EntryName","value":"ATCASE"}]},{"database":"PRINTS","id":"PR00098","properties":[{"key":"EntryName","value":"CPSASE"}]},{"database":"PRINTS","id":"PR00099","properties":[{"key":"EntryName","value":"CPSGATASE"}]},{"database":"SMART","id":"SM01096","properties":[{"key":"EntryName","value":"CPSase_L_D3"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01097","properties":[{"key":"EntryName","value":"CPSase_sm_chain"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00851","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53671","properties":[{"key":"EntryName","value":"Aspartate/ornithine carbamoyltransferase"},{"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":"SSF52021","properties":[{"key":"EntryName","value":"Carbamoyl phosphate synthetase, small subunit N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52317","properties":[{"key":"EntryName","value":"Class I glutamine amidotransferase-like"},{"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":"SSF51556","properties":[{"key":"EntryName","value":"Metallo-dependent hydrolases"},{"key":"MatchStatus","value":"1"}]},{"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":"PS00097","properties":[{"key":"EntryName","value":"CARBAMOYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00866","properties":[{"key":"EntryName","value":"CPSASE_1"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00867","properties":[{"key":"EntryName","value":"CPSASE_2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS51273","properties":[{"key":"EntryName","value":"GATASE_TYPE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51855","properties":[{"key":"EntryName","value":"MGS"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSVKITAPATARFRGCEDDGLVCLEIEDGSAYQGYSFGAKKTIAGELVFQTGMVGYPESVTDPSYRGQILVITFPLVGNYGVPSRETVDELLGDLPAHFESSQIHVAGLVVASYCGEDYSHFLAQSSLGSWLKEQGVPAMYGVDTRALTKKIREKGSMLGKMRLELPGTANGTASDERTHTTLDSFEKIEWSNPNADNLVAQVSVKTPKLYKPPASCVRKHPSGRAIRVLCVDVGMKYNQLRCFLKRGVEVMVCPWDYDLTKAAGEEYDGLFISNGPGDPAVLETTVQNISAVMQKNKTPVFGICLGHQLLARASGAATKKMKFGNRGHNIPCTSLVSGKCHITSQNHGFAVDAETLPANWKELFVNANDGSNEGIMHVSKPYFSVQFHPESTPGPRDTEFLFDVFINTMASCAENPSLLQSPVSFPGGAIEENERLHPRVSVKKVLVLGSGGLSIGQAGEFDYSGSQAIKALKEEGIYTVLINPNIATIQTSKGLADKVYFLPVNAEFVRKVIKYEHPDAIYCTFGGQTALQVGIQLKDEFEALGVKVLGTPIDTIITTEDRELFARSMESIGEKCAKSASANNIDEAMNAVKDIGFPVIVRAAYALGGLGSGFANNEQELLDLCNKAFAASPQVLVERSMKGWKEIEYEVVRDAQDNCITVCNMENFDPLGIHTGDSIVVAPSQTLSDEDYNMLRTTAVNVIRHLGVVGECNIQYALNPFSREYCIIEVNARLSRSSALASKATGYPLAFIAAKLGLGIPLKEIKNSVTKVTCACFEPSLDYVVVKMPRWDLKKFTRVSTQLGSSMKSVGEVMSIGRTFEEAIQKAIRSIDFHNLGFNETPALMAIDDELQTPSDQRLFAIANAMHQGYTVDKIWELTNIDKWFLRKLKGLSDFGKHMSQLTASDVANSPSLLLQAKRLGFSDSQVAKFVSSNEMAIRRLRLDAGIHPFVKQIDTVAAEFPAFTNYLYLTYNASEHDISFDDHGIMVLGSGVYRIGSSVEFDWCSVRAIRTLRATGFKTVMVNYNPETVSTDYDEADKLYFENINQETVLDIYSLENASGVLGAMGGQTPNNIALPLYRAGVKVLGTSPEMIDNAENRYKFSRMLDRIGVDQPTWKELTSFKEAKSFCDKVSYPVLVRPSYVLSGAAMNTVYSEKDLEAYLAQAAEVSREHPVVITKYIENAKEIEMDAVAKDGIVVGHFISEHVENAGVHSGDATLILPPQDLEATTIARIEDATRKIGAALNVTGPFNIQFIAKDNDIKVIECNVRASRSFPFVSKVMGVDLIEMATKAITGQPFQEYPPTNLAPNCVGVKVPQFSFSRLSGADPVLGVEMASTGEVACFGVDKNEAYLKALLSTGFKIPKRNILLSVGSYKDKKEMLPSVQKLQRLGYKLFATAGTADFLQENGVPVQYLEVLGSDEDRNSEFSLSQHLANNMIDLYINLPSSNKYRRPANYVSKGYQTRRMAVDYQVPLVTNVKNAKILIEAIARHFELAVSGRDFQTSHQTVVFPGLINIAAFVPGIVSPHSADIQTVTKASIAAGFSMIRLMPLGVEGSITDAISLKAAQQNSAAGGHCDYNFSISATSNNAEQISTVTGEVGSLFIPFNHLSGSGNISKVAAVTAHFEAWPTNKPMVTDAKFTDLASILLLASLHSRRIHVTSVSTKDDIRLIALSKAKGLQVTCDVSIYSLFLSQKDFPKADFLPTAEDQAALWQNLETIDVFSIGSLPYQLATSLGHKGDPSMGIAEALPLLLSAVTEGKLTIDDIKDRLYTNPMDIFELHEQTGTSVEVEVDRAFEVAKGSFWSPLEGRRLHGSVRRVTFQNATLCLDDEGITGSPTGKDMSSHMVAPQTPAMKPTTAATSLESPKARQQAGFTPRPMGRLRGITSPQALPAQGPRGAIEDLGLPLQLQPATSTSLHKLLSQPSSFRNAHVLSVKQYSRADLHLLFTVAQEMRLGVQREGVLNVLPGRVLCNLFYEPSTRTSASFDAAMQRLGGRTINIDTAHSSVKKGESLQDTLRTLACYGDAVVLRHPEETSVNVAEKFCPVPVVNGGNGSKEHPTQAFLDLFTIREELGTVQGLTITFVGDLLYGRPVHSLVYLLRHYQVQVQLVAPKGLELPSQVREQLAASGQLLRESETLTPEILAHSDVLYCTRVQRERFDSEEKYQQVKNSYRVDNATLKSAKSSTVVLHPLPRNEEVAEEVDFDQRAAYFRQMRYGLYCRMALLALVMASS","length":2233,"molWeight":244304,"crc64":"E4309CCEC56557D4","md5":"D8CA362C5B62DD55744944AF7E81B729"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"PATHWAY":2,"SIMILARITY":4,"CAUTION":1},"countByFeatureType":{"Domain":3,"Region":1,"Active site":3},"uniParcId":"UPI0023104F7F"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QPV0","uniProtkbId":"A0A9W8QPV0_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":14,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165300.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068309"}],"value":"Fatty acid synthase subunit beta"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012996"}],"value":"1.3.1.9"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013256"}],"value":"2.3.1.38"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013258"}],"value":"2.3.1.39"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012878"}],"value":"2.3.1.86"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012480"}],"value":"3.1.2.14"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013167"}],"value":"4.2.1.59"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165300.1"}],"value":"LMH87_006937"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058855"}],"value":"Fatty acid synthetase catalyzes the formation of long-chain fatty acids from acetyl-CoA, malonyl-CoA and NADPH. The beta subunit contains domains for: [acyl-carrier-protein] acetyltransferase and malonyltransferase, S-acyl fatty acid synthase thioesterase, enoyl-[acyl-carrier-protein] reductase, and 3-hydroxypalmitoyl-[acyl-carrier-protein] dehydratase"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(9Z)-octadecenoyl-[ACP] + H2O = (9Z)-octadecenoate + holo-[ACP] + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:15057"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9924"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30823"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78783"}],"ecNumber":"3.1.2.14","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048536"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3R)-hydroxyacyl-[ACP] = a (2E)-enoyl-[ACP] + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13097"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9945"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78827"}],"ecNumber":"4.2.1.59","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001055"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 2,3-saturated acyl-[ACP] + NAD(+) = a (2E)-enoyl-[ACP] + NADH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10240"},{"database":"Rhea","id":"RHEA-COMP:9925"},{"database":"Rhea","id":"RHEA-COMP:9926"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57540"},{"database":"ChEBI","id":"CHEBI:57945"},{"database":"ChEBI","id":"CHEBI:78784"},{"database":"ChEBI","id":"CHEBI:78785"}],"ecNumber":"1.3.1.9","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048572"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).","ecNumber":"2.3.1.86","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048237"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"holo-[ACP] + acetyl-CoA = acetyl-[ACP] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41788"},{"database":"Rhea","id":"RHEA-COMP:9621"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78446"}],"ecNumber":"2.3.1.38","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048835"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"holo-[ACP] + malonyl-CoA = malonyl-[ACP] + CoA","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:41792"},{"database":"Rhea","id":"RHEA-COMP:9623"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57384"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78449"}],"ecNumber":"2.3.1.39","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048462"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00033756"}],"value":"[Alpha(6)beta(6)] hexamers of two multifunctional subunits (alpha and beta)"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010009"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR005562"}],"value":"Belongs to the fungal fatty acid synthetase subunit beta family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165300.1"}],"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":1695,"modifier":"EXACT"},"end":{"value":2047,"modifier":"EXACT"}},"description":"Malonyl-CoA:ACP transacylase (MAT)","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00827"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":2078,"modifier":"EXACT"},"end":{"value":2103,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":1948,"modifier":"EXACT"},"end":{"value":1975,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":14,"modifier":"EXACT"},"end":{"value":24,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"For acetyltransferase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005562-1"}]},{"type":"Active site","location":{"start":{"value":1839,"modifier":"EXACT"},"end":{"value":1839,"modifier":"EXACT"}},"description":"For malonyltransferase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR005562-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"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":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR005562"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"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":"PIRNR","id":"PIRNR005562"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR005562"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR005562"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR005562"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165300.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165300.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000001","properties":[{"key":"ProteinId","value":"KAJ4165300.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056060215.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056191947.1"}]},{"database":"GeneID","id":"80894096","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_006937","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 1"}]},{"database":"GO","id":"GO:0005835","properties":[{"key":"GoTerm","value":"C:fatty acid synthase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019171","properties":[{"key":"GoTerm","value":"F:(3R)-hydroxyacyl-[acyl-carrier-protein] dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004313","properties":[{"key":"GoTerm","value":"F:[acyl-carrier-protein] S-acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004314","properties":[{"key":"GoTerm","value":"F:[acyl-carrier-protein] S-malonyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004318","properties":[{"key":"GoTerm","value":"F:enoyl-[acyl-carrier-protein] reductase (NADH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004312","properties":[{"key":"GoTerm","value":"F:fatty acid synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0016297","properties":[{"key":"GoTerm","value":"F:fatty acyl-[ACP] hydrolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004321","properties":[{"key":"GoTerm","value":"F:fatty-acyl-CoA synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0042759","properties":[{"key":"GoTerm","value":"P:long-chain fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd03447","properties":[{"key":"EntryName","value":"FAS_MaoC"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1050.120:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.930.70:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000017","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000078","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.1120.100:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.366.10:FF:000007","properties":[{"key":"EntryName","value":"Fatty acid synthase beta subunit dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.129.10:FF:000015","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit beta"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.3330:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit beta dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.366.10:FF:000003","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit beta dehydratase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.1050.120","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.930.70","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.1120.100","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.3330","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.140.1400","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.60.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.20.240.10","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":"2"}]},{"database":"Gene3D","id":"3.10.129.10","properties":[{"key":"EntryName","value":"Hotdog Thioesterase"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.366.10","properties":[{"key":"EntryName","value":"Malonyl-Coenzyme A Acyl Carrier Protein, domain 2"},{"key":"MatchStatus","value":"3"}]},{"database":"InterPro","id":"IPR001227","properties":[{"key":"EntryName","value":"Ac_transferase_dom_sf"}]},{"database":"InterPro","id":"IPR014043","properties":[{"key":"EntryName","value":"Acyl_transferase_dom"}]},{"database":"InterPro","id":"IPR016035","properties":[{"key":"EntryName","value":"Acyl_Trfase/lysoPLipase"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR039569","properties":[{"key":"EntryName","value":"FAS1-like_DH_region"}]},{"database":"InterPro","id":"IPR016452","properties":[{"key":"EntryName","value":"Fas1/AflB-like"}]},{"database":"InterPro","id":"IPR013565","properties":[{"key":"EntryName","value":"Fas1/AflB-like_central"}]},{"database":"InterPro","id":"IPR041099","properties":[{"key":"EntryName","value":"FAS1_N"}]},{"database":"InterPro","id":"IPR040883","properties":[{"key":"EntryName","value":"FAS_meander"}]},{"database":"InterPro","id":"IPR003965","properties":[{"key":"EntryName","value":"Fatty_acid_synthase"}]},{"database":"InterPro","id":"IPR050830","properties":[{"key":"EntryName","value":"Fungal_FAS"}]},{"database":"InterPro","id":"IPR029069","properties":[{"key":"EntryName","value":"HotDog_dom_sf"}]},{"database":"InterPro","id":"IPR002539","properties":[{"key":"EntryName","value":"MaoC-like_dom"}]},{"database":"InterPro","id":"IPR032088","properties":[{"key":"EntryName","value":"SAT"}]},{"database":"PANTHER","id":"PTHR10982:SF21","properties":[{"key":"EntryName","value":"FATTY ACID SYNTHASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10982","properties":[{"key":"EntryName","value":"MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00698","properties":[{"key":"EntryName","value":"Acyl_transf_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08354","properties":[{"key":"EntryName","value":"Fas1-AflB-like_hel"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13452","properties":[{"key":"EntryName","value":"FAS1_DH_region"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22235","properties":[{"key":"EntryName","value":"FAS1_thioest_ins"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17951","properties":[{"key":"EntryName","value":"FAS_meander"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17828","properties":[{"key":"EntryName","value":"FAS_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01575","properties":[{"key":"EntryName","value":"MaoC_dehydratas"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16073","properties":[{"key":"EntryName","value":"SAT"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF005562","properties":[{"key":"EntryName","value":"FAS_yeast_beta"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01483","properties":[{"key":"EntryName","value":"FASYNTHASE"}]},{"database":"SMART","id":"SM00827","properties":[{"key":"EntryName","value":"PKS_AT"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52151","properties":[{"key":"EntryName","value":"FabD/lysophospholipase-like"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF51412","properties":[{"key":"EntryName","value":"Inosine monophosphate dehydrogenase (IMPDH)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54637","properties":[{"key":"EntryName","value":"Thioesterase/thiol ester dehydrase-isomerase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MYGAGTGPQTGINTPRSSSSLRPLTLSHGTLETSFLVPTSLHFHASQLKERFTASLPPPTDELAQDDEPSSVAELVARYLGSVADQVENGEDDAQGSYEEVLRLVLNEFERAFLHGNEVHALAATLPGIESKKLEVIKSYYAARSVSNRTIKPHESALLRAADDGAADIYTIFGGQGNIEEYFEELRQIFTTYSGFVSELVTNAAELLQTLSNDPSAEKSFAKGLDIMNWLQHPEATPDVDYLISAPVSFPLIGLVQLAHYEVTCKVLGISPGHLRERLRGSTGHSQGIVMAAATAAADSWESWREITTSTLTILFWIGTRSQQAFPVTSMTPTMLRESMDHGEGTPTPMLSIRDLSQQEVQKHIDATNQYLPANRHISISLINSPRNLVVTGPPTSLYGLNSQLRKVKAPTGLDQTRVPYTERKVRFVNRFLPITAPFHSQYLAEATTMIDEDLKDISIDSSSLGMAVFDTNTGKDLRTEVSGNIVPTLVRLITRDPVNWETATVFPNASHVLDFGPGGASGLGNLTSRNKEGNGVRVIIAGAIEGALEAVGYKPELFDRDEENAIRYAIDWVKEFGPKLVKNSKGEKYVDTKMSRLLGLPPVMVAGMTPCTVPWDFVAATMNSGYHIELAGGGYFNTRTMTQALEKIEKAIPAGRGITVNLIYVNPRAMAWQIPLLGRLRAEGVPIEGLTIGAGVPSIEVAQEYIETLGLKHIAFKPGSVEAVQAVINIAKANPTFPVLLQWTGGRGGGHHSFEDFHQPILQMYGRIRRQENIILVAGSGFGGADDTYPYVTGDWSKKYGYPPMPFDGCLFGSRMMVAKEAHTSKNAKQAIIDAPGLEDAQWENTYKGPAGGVITVRSEMGEPIHKLATRGVRFWSEMDQKIFALPKEKRVAELKKNREYIIKKLNDDFQKVWFGCNKAGKAVDLEDMTYAEIVRRLVDLLYVRHQERWIDPSFARLTGDFIHRVEERFTTTPGKPSLLQSYAELDEPYTAVKRILSFYPEADKQIVNAQDVQHFLLLCMRPGQKPVTFIPALDNNFEFFFKKDSLWQSEDLDAVIDQDVGRTCILQGPTAVKFSTILDEPVKSILDGIHDSHIEYLTRDYYGGKESSIPTIEYFGGELVEAEIPLDIEGLTVNYDEHKNTYRLASGAGAALPPLDAWLSLLAGPNRNWRHALLMSDVVVQGQKFQTNPMRRIFAPARGLYVEINYPNDPSKTEIVVKEQPRYNQYVTVIEVKLAGKNEILVNMIKDTTALGRPLGLPLRFTYHPETGYAPIREVMDDRNDRIKEFYWKAWFGEDHMDLDARVTGRFDGGKTIITAEAINDFVHAVGNTGEAFVDRPGKVVYAPMDFAIVVGWKAITKPIFPRTIDGDLLKLVHLSNGFRMLPGAEPLKKGDEISTTAQINAVINQESGKMVEVCGTITRDGQPVMEVTSQFLYRGAYTDFENTFQRKVETPVEVHLATSKDVAVLRSKEWFSTDEMPNDFDLLGKTLTFRLQSLMRYKNKNVFRTVETRGEVLLELPTKEIIQVASVDYEAGESHGNPVIDYLERTGSPLDQPINFENPIPLSGRTPLQLRAPASNETYARVSGDYNPIHVSRVFSSYASLPGTITHGMYSSAAVRSLVETWAAENNVGRVRSFHASLVGMVLPNDDIQVQLQHVGMVAGRKIIKVEVSNKETEEKVLLGEAEVEQPVTAYVFTGQGSQEQGMGMELYDSSPVAKEVWDRADKYLLDNYGFSITNIVRNNPKELTIHFGGPRGKAIRQNYMAMTFETVAADGSIKSERIFKDVNEKTTSYTYRSPTGLLSATQFTQPALTLMEKASFEDMKSKGLVPRDSTFAGHSLGEYSALAALADVMPIESLVSVVFYRGLTMQVAVERDAAGRSNYSMCAVNPSRISKTFNEEALQFVVNNIAEETGWLLEIVNYNIANMQYVCAGDLRALDTLAGVTNFLKMQKIDIEEMRSNIEEAKDALREIIRGCAEATLKKPVPIELERGFATIPLRGIDVPFHSTFLRSGVKPFRSFLLKKINKTTIDPSKLVGKYIPNVTAKPFALTKEYFEDVYKLTNSPKIGAVLANWDKITQDGTEGKPGSDSEASGEYEGPGAAA","length":2103,"molWeight":233087,"crc64":"0B30312BF295A8B1","md5":"3F56426541FC987EAC75A9214543D287"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":6,"SUBUNIT":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Coiled coil":1,"Compositional bias":1,"Active site":2},"uniParcId":"UPI00230976A1"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8ULC7","uniProtkbId":"A0A9W8ULC7_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":5.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4153298.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Pentafunctional AROM polypeptide"}},"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"DHQS"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.3.4"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-phosphoshikimate 1-carboxyvinyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.5.1.19"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"5-enolpyruvylshikimate-3-phosphate synthase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSP synthase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"EPSPS"}]}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate kinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"SK"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"2.7.1.71"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinate dehydratase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"3-dehydroquinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"4.2.1.10"}]}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Shikimate dehydrogenase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"1.1.1.25"}]}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4153298.1"}],"value":"LMH87_009792"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00054455"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"The AROM polypeptide catalyzes 5 consecutive enzymatic reactions in prechorismate polyaromatic amino acid biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-dehydroquinate = 3-dehydroshikimate + H2O","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21096"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:32364"}],"ecNumber":"4.2.1.10","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-phosphoshikimate + phosphoenolpyruvate = 5-O-(1-carboxyvinyl)-3-phosphoshikimate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21256"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57701"},{"database":"ChEBI","id":"CHEBI:58702"},{"database":"ChEBI","id":"CHEBI:145989"}],"ecNumber":"2.5.1.19","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00044633"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate = 3-dehydroquinate + phosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21968"},{"database":"ChEBI","id":"CHEBI:32364"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:58394"}],"ecNumber":"4.2.3.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + ATP = 3-phosphoshikimate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13121"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:145989"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.71","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048567"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"shikimate + NADP(+) = 3-dehydroshikimate + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17737"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16630"},{"database":"ChEBI","id":"CHEBI:36208"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"}],"ecNumber":"1.1.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Binds 2 Zn(2+) ions per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 2/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 3/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 4/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004811"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 6/7"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009948"}],"value":"Belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 2nd section; belongs to the EPSP synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006477"}],"value":"In the 2nd section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 3rd section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the 4th section; belongs to the type-I 3-dehydroquinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the C-terminal section; belongs to the shikimate dehydrogenase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000514"}],"value":"In the N-terminal section; belongs to the dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009349"}],"value":"In the N-terminal section; belongs to the shikimate kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"In the N-terminal section; belongs to the sugar phosphate cyclases superfamily. Dehydroquinate synthase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4153298.1"}],"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":78,"modifier":"EXACT"},"end":{"value":190,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01761"}]},{"type":"Domain","location":{"start":{"value":192,"modifier":"EXACT"},"end":{"value":355,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF24621"}]},{"type":"Domain","location":{"start":{"value":400,"modifier":"EXACT"},"end":{"value":830,"modifier":"EXACT"}},"description":"Enolpyruvate transferase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00275"}]},{"type":"Domain","location":{"start":{"value":1284,"modifier":"EXACT"},"end":{"value":1364,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase substrate binding N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF08501"}]},{"type":"Domain","location":{"start":{"value":1402,"modifier":"EXACT"},"end":{"value":1513,"modifier":"EXACT"}},"description":"Quinate/shikimate 5-dehydrogenase/glutamyl-tRNA reductase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01488"}]},{"type":"Domain","location":{"start":{"value":1529,"modifier":"EXACT"},"end":{"value":1558,"modifier":"EXACT"}},"description":"SDH C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF18317"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":382,"modifier":"EXACT"}},"description":"3-dehydroquinate synthase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Region","location":{"start":{"value":1279,"modifier":"EXACT"},"end":{"value":1562,"modifier":"EXACT"}},"description":"Shikimate dehydrogenase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":258,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":818,"modifier":"EXACT"},"end":{"value":818,"modifier":"EXACT"}},"description":"For EPSP synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1169,"modifier":"EXACT"},"end":{"value":1169,"modifier":"EXACT"}},"description":"Proton acceptor; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Active site","location":{"start":{"value":1197,"modifier":"EXACT"},"end":{"value":1197,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; for 3-dehydroquinate dehydratase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}]},{"type":"Binding site","location":{"start":{"value":49,"modifier":"EXACT"},"end":{"value":51,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":87,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":115,"modifier":"EXACT"},"end":{"value":117,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":140,"modifier":"EXACT"},"end":{"value":141,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":147,"modifier":"EXACT"},"end":{"value":147,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":153,"modifier":"EXACT"},"end":{"value":153,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":162,"modifier":"EXACT"},"end":{"value":162,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":180,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57540"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"NAD(+)","id":"ChEBI:CHEBI:57540"}},{"type":"Binding site","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"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_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":248,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":266,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":269,"modifier":"EXACT"},"end":{"value":269,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":285,"modifier":"EXACT"},"end":{"value":285,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":354,"modifier":"EXACT"},"end":{"value":354,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58394"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"7-phospho-2-dehydro-3-deoxy-D-arabino-heptonate","id":"ChEBI:CHEBI:58394"}},{"type":"Binding site","location":{"start":{"value":866,"modifier":"EXACT"},"end":{"value":873,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022605"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023141"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0057","category":"Biological process","name":"Aromatic amino acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"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_03143"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03143"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4153298.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4153298.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000008","properties":[{"key":"ProteinId","value":"KAJ4153298.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056053956.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056196849.1"}]},{"database":"GeneID","id":"80896951","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_009792","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 5"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003855","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate dehydratase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003856","properties":[{"key":"GoTerm","value":"F:3-dehydroquinate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003866","properties":[{"key":"GoTerm","value":"F:3-phosphoshikimate 1-carboxyvinyltransferase 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:0004764","properties":[{"key":"GoTerm","value":"F:shikimate 3-dehydrogenase (NADP+) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004765","properties":[{"key":"GoTerm","value":"F:shikimate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009073","properties":[{"key":"GoTerm","value":"P:aromatic amino acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009423","properties":[{"key":"GoTerm","value":"P:chorismate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd00502","properties":[{"key":"EntryName","value":"DHQase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08195","properties":[{"key":"EntryName","value":"DHQS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01556","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd01065","properties":[{"key":"EntryName","value":"NAD_bind_Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00464","properties":[{"key":"EntryName","value":"SK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.1090.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.70:FF:000135","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1970:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001256","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000007","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.65.10.10:FF:000008","properties":[{"key":"EntryName","value":"Pentafunctional AROM polypeptide"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1970","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":"Gene3D","id":"1.20.1090.10","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like - alpha domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.65.10.10","properties":[{"key":"EntryName","value":"Enolpyruvate transferase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.10860","properties":[{"key":"EntryName","value":"Leucine Dehydrogenase, chain A, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00210","properties":[{"key":"EntryName","value":"EPSP_synth"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03143","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00109","properties":[{"key":"EntryName","value":"Shikimate_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR018508","properties":[{"key":"EntryName","value":"3-dehydroquinate_DH_AS"}]},{"database":"InterPro","id":"IPR013785","properties":[{"key":"EntryName","value":"Aldolase_TIM"}]},{"database":"InterPro","id":"IPR046346","properties":[{"key":"EntryName","value":"Aminoacid_DH-like_N_sf"}]},{"database":"InterPro","id":"IPR016037","properties":[{"key":"EntryName","value":"DHQ_synth_AroB"}]},{"database":"InterPro","id":"IPR030960","properties":[{"key":"EntryName","value":"DHQS/DOIS_N"}]},{"database":"InterPro","id":"IPR056179","properties":[{"key":"EntryName","value":"DHQS_C"}]},{"database":"InterPro","id":"IPR001381","properties":[{"key":"EntryName","value":"DHquinase_I"}]},{"database":"InterPro","id":"IPR001986","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_dom"}]},{"database":"InterPro","id":"IPR036968","properties":[{"key":"EntryName","value":"Enolpyruvate_Tfrase_sf"}]},{"database":"InterPro","id":"IPR006264","properties":[{"key":"EntryName","value":"EPSP_synthase"}]},{"database":"InterPro","id":"IPR023193","properties":[{"key":"EntryName","value":"EPSP_synthase_CS"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008289","properties":[{"key":"EntryName","value":"Pentafunct_AroM"}]},{"database":"InterPro","id":"IPR013792","properties":[{"key":"EntryName","value":"RNA3'P_cycl/enolpyr_Trfase_a/b"}]},{"database":"InterPro","id":"IPR041121","properties":[{"key":"EntryName","value":"SDH_C"}]},{"database":"InterPro","id":"IPR031322","properties":[{"key":"EntryName","value":"Shikimate/glucono_kinase"}]},{"database":"InterPro","id":"IPR013708","properties":[{"key":"EntryName","value":"Shikimate_DH-bd_N"}]},{"database":"InterPro","id":"IPR010110","properties":[{"key":"EntryName","value":"Shikimate_DH_AroM-type"}]},{"database":"InterPro","id":"IPR000623","properties":[{"key":"EntryName","value":"Shikimate_kinase/TSH1"}]},{"database":"InterPro","id":"IPR023000","properties":[{"key":"EntryName","value":"Shikimate_kinase_CS"}]},{"database":"InterPro","id":"IPR006151","properties":[{"key":"EntryName","value":"Shikm_DH/Glu-tRNA_Rdtase"}]},{"database":"NCBIfam","id":"TIGR01356","properties":[{"key":"EntryName","value":"aroA"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01357","properties":[{"key":"EntryName","value":"aroB"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01093","properties":[{"key":"EntryName","value":"aroD"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01809","properties":[{"key":"EntryName","value":"Shik-DH-AROM"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090","properties":[{"key":"EntryName","value":"AROM/DEHYDROQUINATE SYNTHASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR21090:SF5","properties":[{"key":"EntryName","value":"PENTAFUNCTIONAL AROM POLYPEPTIDE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01761","properties":[{"key":"EntryName","value":"DHQ_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF24621","properties":[{"key":"EntryName","value":"DHQS_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01487","properties":[{"key":"EntryName","value":"DHquinase_I"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00275","properties":[{"key":"EntryName","value":"EPSP_synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18317","properties":[{"key":"EntryName","value":"SDH_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01488","properties":[{"key":"EntryName","value":"Shikimate_DH"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08501","properties":[{"key":"EntryName","value":"Shikimate_dh_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01202","properties":[{"key":"EntryName","value":"SKI"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000514","properties":[{"key":"EntryName","value":"Pentafunct_AroM"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR01100","properties":[{"key":"EntryName","value":"SHIKIMTKNASE"}]},{"database":"SUPFAM","id":"SSF51569","properties":[{"key":"EntryName","value":"Aldolase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53223","properties":[{"key":"EntryName","value":"Aminoacid dehydrogenase-like, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56796","properties":[{"key":"EntryName","value":"Dehydroquinate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55205","properties":[{"key":"EntryName","value":"EPT/RTPC-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"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":"PS01028","properties":[{"key":"EntryName","value":"DEHYDROQUINASE_I"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00104","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00885","properties":[{"key":"EntryName","value":"EPSP_SYNTHASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01128","properties":[{"key":"EntryName","value":"SHIKIMATE_KINASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAESASESPVIIPILGQPSIVVDNGLWADYIVQDLLNNVASSTYVLITDTNLHNTYVPRFRASFENITKGQSARLLTYTIPPGEASKNRETKGEVEDWMLSQQCTRDTVIVALGGGVIGDMIGYVAATFMRGVRFVQIPTTLLAMVDSSIGGKTAIDTPMGKNLVGAFWQPRRIYIDLQFLETLPVREFINGMAEVVKTAAIWNETEFEFLEASASKILACVRSRATDRLMPIKNTLKRIVVGSAGVKAEVVSSDEREGGLRNLLNFGHSIGHGIEAILTPQLLHGEAVAIGMVKEAELARHLGVLRPEAVARLVKCIAAYGLPISLQDKRVQRLTAGRLCPVDVVLQKMAVDKKNDGLKKKIVLLSAVGKTYEPKASVVDDQSIRTILSPAVVVSPMVPTDLNVTVSPPGSKSISNRALVLAALGSGSCKIKNLLHSDDTGYMLSAIAKLRGASYSWEAGGELLVVNGNAGKLSSSSEELYIGNAGTASRFLTTVAALCSPSDAAKSVVLTGNSHMKARPIGPLVDALRLNGVSIEYMEQEKSLPLRIGSSSGFEGGVIELAATISSQYVSSILMAAPYAKNPVTLKLVGGKPISQLYIDLTVAMMKSFGVSVTASTTEPHTYHIPQGTYKNPPEYVIEGDASSATYPLAMAAITGTTCTIPNIGSASLQGDARFAVDVLRPMGCTVEQTETSTTVTGPKLGALKPLPHVDMEPMTDAFLTASVLAAVAGGKTQITGIANQRVKECNRIAAMRIQLAKFGVKCAELDDGIEVFGIAPGNLKTPAKGIFCYDDHRVAMSLSVLSVVAPAGAVITQQDCVGKTWPGWWDTMSQSFKVRLDGTDKCKAEEEDIPAAAGADGRSVFLIGMRGAGKTTAGNWIAKSLGWKSVDLDHELERRCGQSIPEIIAKHGWEGFRKQELQLLQDVAEKQPLGYVFSCGGGIVETPEARDLLQGYAGSGGKVILIQRNIDEVMQYLERDKSRPAYSSEIRGVYNRRKTWYKQCSNYSYYSIHTNEPTGKSLIPNDFVRFVSTVFGKATQLPQLRKKTQSFFVSLTLPDLSTATNILPKAVVGSDAVELRVDLLKSQDIDFVTEQVSILRQHTGLPIIFTVRTVSQGGSFPDDSIEALLALYHLGLQLGSEYLDVEITAPDEILESVSSARGHTKLIASHHDPRGALSWRNASWIAHYNRALQYGDIIKLVGIAQKVEDNFDLLRFKSRMASDQGPPLIAVNMGSAGQLSRVLNGFLTPVSHPALPFKAAPGQLSASEIRQALALVGESKSLNFHLFGKPISQSRSPALHNGLFGQCGLPHQYHLLETDNVADVKATLRDPSFGGASVTIPLKLDIIDELDDLTEAARTIGAVNTVIPVFGTAEDGTPRLLGDNTDWKGIAYALREGGLREVSSESAAMVVGSGGTTRAAVFALHSLGFSRIYVVGRTAKNVTAMIADFPNSYNLQAVTDAATITTLPNVIVSTIPGDKPIDPVTEKVISGVVNASATASQQRVLLDMAYKPRETPAVKLAESAGWPTIPGLEVLASQGWYQFQLWTGISPLYNDARQLVQGGQ","length":1562,"molWeight":167741,"crc64":"B802BF2380E8BE57","md5":"A26880B03A8261EF75F50A25F68629A8"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"COFACTOR":1,"PATHWAY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":9,"CAUTION":2},"countByFeatureType":{"Domain":6,"Region":2,"Active site":5,"Binding site":22},"uniParcId":"UPI00231322BF"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q451","uniProtkbId":"A0A9W8Q451_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-01-28","lastSequenceUpdateDate":"2023-11-08","entryVersion":8,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145623.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase proenzyme 1, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phosphatidylserine decarboxylase 1 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"PSD1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145623.1"}],"value":"LMH87_004469"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 alpha chain","note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain"}]},"subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"commentType":"SUBCELLULAR LOCATION","molecule":"Phosphatidylserine decarboxylase 1 beta chain","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Single-pass membrane protein","id":"SL-9904"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Intermembrane side","id":"SL-9912"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"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 autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, 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 prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type I sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145623.1"}],"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":512,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5041026106"},{"type":"Chain","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":552,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 1 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"featureId":"PRO_5041026105"},{"type":"Topological domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Mitochondrial matrix","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Topological domain","location":{"start":{"value":120,"modifier":"EXACT"},"end":{"value":552,"modifier":"EXACT"}},"description":"Mitochondrial intermembrane","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Region","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":85,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":262,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":311,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":19,"modifier":"EXACT"},"end":{"value":38,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":56,"modifier":"EXACT"},"end":{"value":80,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":265,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":281,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":333,"modifier":"EXACT"},"end":{"value":342,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":231,"modifier":"EXACT"},"end":{"value":231,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":385,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Active site","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Site","location":{"start":{"value":512,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]},{"type":"Modified residue","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":513,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03208"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145623.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145623.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4145623.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q451","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0005743","properties":[{"key":"GoTerm","value":"C:mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016540","properties":[{"key":"GoTerm","value":"P:protein autoprocessing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"HAMAP","id":"MF_03208","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type1_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033661","properties":[{"key":"EntryName","value":"PSD_type1_euk"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF6","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MQPRVSCFCCLKLGRHEPSLTSDDQTANRSRPSRSTQRGHALSPLRRQCARAGSRRPSTASLRPRTPSTTREFSSGSSGQRPRFSQRLGEALRKTKITWYHIPVGLGVGFLGFVQFYKVQARERERQEGGEKPKPRPRIQPEGPWQVRVMSTLPLKAISRIWGKFNELTIPYYLRVPGFKLYSWVFGVNLSEVSEPDLHIYPNLAAFFYRTLKPGARPLDPDPQVLLSPSDGKILQYGQIDGGNIEQVKGMTYTVDALLGKHTPSPSMSSASSIRSGDSTPKPREHEGDEDVVGKEEEFARVNGISYTLPDFLTGQKEPTHDDAANRAGAVEDQSTQSSQRAVSEVRADLALGERAWYDILPRDKATSLYYAVIYLAPGDYHRFHSPTNWVVERRRHFAGELYSVSPYLQRTLPGLFTLNERVVLLGRWRWGFFGYVPVGATNVGSIKVNFDRELRTNSLTTDTAADLAADEAASRGEPYSGFAEATYESASPVLHGHALRRGEEMGGFQLGSTIVLVFEAPTTDDGKGWEWKVDKGQTVKMGQALGRVNEE","length":552,"molWeight":61567,"crc64":"898F71B7F1DBFFD9","md5":"B78D271AB761930E2C5B86125EF47E92"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":2,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Topological domain":2,"Region":3,"Compositional bias":5,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI0023247F16"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q5E0","uniProtkbId":"A0A9W8Q5E0_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147452.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"2.7.7.4"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"ATP-sulfurylase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfate adenylate transferase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"SAT"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"MET3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147452.1"}],"value":"LMH87_001969"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Catalyzes the first intracellular reaction of sulfate assimilation, forming adenosine-5'-phosphosulfate (APS) from inorganic sulfate and ATP. Plays an important role in sulfate activation as a component of the biosynthesis pathway of sulfur-containing amino acids"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"adenosine 5'-phosphosulfate + ATP = 3'-phosphoadenylyl sulfate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24152"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:58243"},{"database":"ChEBI","id":"CHEBI:58339"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001823"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"sulfate + ATP + H(+) = adenosine 5'-phosphosulfate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:18133"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16189"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:58243"}],"ecNumber":"2.7.7.4","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Allosterically inhibited by 3'-phosphoadenosine 5'-phosphosulfate (PAPS)"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 1/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00062002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Homohexamer. Dimer of trimers"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"The adenylyl-sulfate kinase (APS kinase) is non-functional. It is involved in allosteric regulation by PAPS. PAPS binding induces a large rotational rearrangement of domains lowering the substrate affinity of the enzyme"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the C-terminal section; belongs to the APS kinase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"In the N-terminal section; belongs to the sulfate adenylyltransferase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147452.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":4,"modifier":"EXACT"},"end":{"value":166,"modifier":"EXACT"}},"description":"ATP-sulfurylase PUA-like","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF14306"}]},{"type":"Domain","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":388,"modifier":"EXACT"}},"description":"Sulphate adenylyltransferase catalytic","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01747"}]},{"type":"Domain","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"APS kinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF01583"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":170,"modifier":"EXACT"}},"description":"N-terminal","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Region","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":574,"modifier":"EXACT"}},"description":"Allosteric regulation domain; adenylyl-sulfate kinase-like","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":199,"modifier":"EXACT"},"end":{"value":199,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Active site","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":201,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":198,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":200,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:16189"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"sulfate","id":"ChEBI:CHEBI:16189"}},{"type":"Binding site","location":{"start":{"value":334,"modifier":"EXACT"},"end":{"value":334,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":435,"modifier":"EXACT"},"end":{"value":438,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Binding site","location":{"start":{"value":516,"modifier":"EXACT"},"end":{"value":516,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58339"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"ligand":{"name":"3'-phosphoadenylyl sulfate","id":"ChEBI:CHEBI:58339","note":"allosteric inhibitor"}},{"type":"Site","location":{"start":{"value":204,"modifier":"EXACT"},"end":{"value":204,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":207,"modifier":"EXACT"},"end":{"value":207,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]},{"type":"Site","location":{"start":{"value":331,"modifier":"EXACT"},"end":{"value":331,"modifier":"EXACT"}},"description":"Induces change in substrate recognition on ATP binding","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0028","category":"Biological process","name":"Amino-acid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0198","category":"Biological process","name":"Cysteine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0486","category":"Biological process","name":"Methionine biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03106"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"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_03106"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147452.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147452.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000010","properties":[{"key":"ProteinId","value":"KAJ4147452.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q5E0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 3"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004020","properties":[{"key":"GoTerm","value":"F:adenylylsulfate kinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004781","properties":[{"key":"GoTerm","value":"F:sulfate adenylyltransferase (ATP) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0070814","properties":[{"key":"GoTerm","value":"P:hydrogen sulfide biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000103","properties":[{"key":"GoTerm","value":"P:sulfate assimilation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02027","properties":[{"key":"EntryName","value":"APSK"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00517","properties":[{"key":"EntryName","value":"ATPS"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.10.400.10:FF:000003","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000802","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.620:FF:000052","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.620","properties":[{"key":"EntryName","value":"HUPs"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.300","properties":[{"key":"EntryName","value":"P-loop containing nucleotide triphosphate hydrolases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.10.400.10","properties":[{"key":"EntryName","value":"Sulfate adenylyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03106","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR002891","properties":[{"key":"EntryName","value":"APS"}]},{"database":"InterPro","id":"IPR059117","properties":[{"key":"EntryName","value":"APS_kinase_dom"}]},{"database":"InterPro","id":"IPR025980","properties":[{"key":"EntryName","value":"ATP-Sase_PUA-like_dom"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR014729","properties":[{"key":"EntryName","value":"Rossmann-like_a/b/a_fold"}]},{"database":"InterPro","id":"IPR027535","properties":[{"key":"EntryName","value":"Sulf_adenylyltr_euk"}]},{"database":"InterPro","id":"IPR050512","properties":[{"key":"EntryName","value":"Sulf_AdTrans/APS_kinase"}]},{"database":"InterPro","id":"IPR024951","properties":[{"key":"EntryName","value":"Sulfurylase_cat_dom"}]},{"database":"InterPro","id":"IPR002650","properties":[{"key":"EntryName","value":"Sulphate_adenylyltransferase"}]},{"database":"NCBIfam","id":"TIGR00455","properties":[{"key":"EntryName","value":"apsK"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF004040","properties":[{"key":"EntryName","value":"PRK05537.1"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR00339","properties":[{"key":"EntryName","value":"sopT"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR42700:SF1","properties":[{"key":"EntryName","value":"SULFATE ADENYLYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01583","properties":[{"key":"EntryName","value":"APS_kinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01747","properties":[{"key":"EntryName","value":"ATP-sulfurylase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF14306","properties":[{"key":"EntryName","value":"PUA_2"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52374","properties":[{"key":"EntryName","value":"Nucleotidylyl transferase"},{"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":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MANSPHGGVLKDLFARDLPRQSELLAESENLPALVLTERHLCDLELILNGGFSPLEGFMTEKDYNGVVKDNRLASGLLFSMPITLDVDQKQIDDLGLKAGARITLRDSRDDRNLAILTVEDVYRPDKVNEAKNVFGSDDDTHPGVKHLFSTAKEFYVGGKLEAINRLEHYDFLDLRFTPSELRSHFSKLGWQKVVAFQTRNPMHRAHRELTVRAARSQQANVLIHPVVGMTKPGDIDHFTRVRVYKALIARYPNGMAALALLPLAMRMGGPREALWHAIIRKNHGSTHFIVGRDHAGPGKNKDGKDHYGPYDAQTLVQQHQEELGIKMVEFQEMIYIPDRDEYMPANEIPEGTRTMNISGTELRNRLRTGKEIPEWFSYPEVVKVLREQNPLPREKGFTVFMTGFQNSGKDQIARALQTTLNQGGGRPVSMLLGETVRSELSSELGFSRADRDLNISRIAYVASELTRAGAAVIAAPIAPFEQARQQARELVEKSGPFFLVHVATPLEYAEKTDRRGIYKAARAGEIKGFTGVDDPYEAPSKADLVVDVEKQNVRSIVHEIILMLESRGLLDRF","length":574,"molWeight":64408,"crc64":"2A23B67E2917D36A","md5":"85CC07BE644A078FF7BB01AB65B71BBA"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"SIMILARITY":2,"CAUTION":2},"countByFeatureType":{"Domain":3,"Region":2,"Active site":3,"Binding site":8,"Site":3},"uniParcId":"UPI0007C01575"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q6L4","uniProtkbId":"A0A9W8Q6L4_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147824.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Phospholipid-transporting ATPase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"7.6.2.1"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147824.1"}],"value":"LMH87_002326"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O + phospholipidSide 1 = ADP + phosphate + phospholipidSide 2.","ecNumber":"7.6.2.1","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00034036"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phospho-L-serine(in) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:38567"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051303"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:38568"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051303"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphocholine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphocholine(in) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:38583"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:57643"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052223"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:38584"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00052223"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(out) + ATP + H2O = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66132"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:64612"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049128"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66133"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049128"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(out) + ATP + H2O = a beta-D-glucosyl-(1<->1')-N-acylsphing-4-enine(in) + ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:66036"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:22801"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050913"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:66037"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00050913"}]}]},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"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":"RuleBase","id":"RU362033"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00008109"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"value":"Belongs to the cation transport ATPase (P-type) (TC 3.A.3) family. Type IV subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147824.1"}],"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":146,"modifier":"EXACT"},"end":{"value":163,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":169,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":513,"modifier":"EXACT"},"end":{"value":538,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":558,"modifier":"EXACT"},"end":{"value":581,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1143,"modifier":"EXACT"},"end":{"value":1159,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1171,"modifier":"EXACT"},"end":{"value":1192,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1222,"modifier":"EXACT"},"end":{"value":1243,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1263,"modifier":"EXACT"},"end":{"value":1281,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1288,"modifier":"EXACT"},"end":{"value":1308,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Transmembrane","location":{"start":{"value":1328,"modifier":"EXACT"},"end":{"value":1348,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}]},{"type":"Domain","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":169,"modifier":"EXACT"}},"description":"P-type ATPase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16209"}]},{"type":"Domain","location":{"start":{"value":1109,"modifier":"EXACT"},"end":{"value":1357,"modifier":"EXACT"}},"description":"P-type ATPase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF16212"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":93,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":253,"modifier":"EXACT"},"end":{"value":279,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1379,"modifier":"EXACT"},"end":{"value":1444,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1493,"modifier":"EXACT"},"end":{"value":1527,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":26,"modifier":"EXACT"},"end":{"value":52,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":75,"modifier":"EXACT"},"end":{"value":92,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1379,"modifier":"EXACT"},"end":{"value":1388,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1396,"modifier":"EXACT"},"end":{"value":1406,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1423,"modifier":"EXACT"},"end":{"value":1444,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1507,"modifier":"EXACT"},"end":{"value":1527,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":629,"modifier":"EXACT"},"end":{"value":629,"modifier":"EXACT"}},"description":"4-aspartylphosphate intermediate","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-1"}]},{"type":"Binding site","location":{"start":{"value":629,"modifier":"EXACT"},"end":{"value":629,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":629,"modifier":"EXACT"},"end":{"value":629,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":630,"modifier":"EXACT"},"end":{"value":630,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":631,"modifier":"EXACT"},"end":{"value":631,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":631,"modifier":"EXACT"},"end":{"value":631,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"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":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":804,"modifier":"EXACT"},"end":{"value":804,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":827,"modifier":"EXACT"},"end":{"value":827,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":862,"modifier":"EXACT"},"end":{"value":862,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":942,"modifier":"EXACT"},"end":{"value":942,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":943,"modifier":"EXACT"},"end":{"value":943,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":944,"modifier":"EXACT"},"end":{"value":944,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1056,"modifier":"EXACT"},"end":{"value":1056,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1062,"modifier":"EXACT"},"end":{"value":1062,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1082,"modifier":"EXACT"},"end":{"value":1082,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1085,"modifier":"EXACT"},"end":{"value":1085,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1086,"modifier":"EXACT"},"end":{"value":1086,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":1086,"modifier":"EXACT"},"end":{"value":1086,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"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":"ARBA","id":"ARBA00023055"}],"id":"KW-0445","category":"Biological process","name":"Lipid transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-3"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR606539-2"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022967"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-1278","category":"Molecular function","name":"Translocase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU362033"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"}],"id":"KW-0813","category":"Biological process","name":"Transport"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147824.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4147824.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000010","properties":[{"key":"ProteinId","value":"KAJ4147824.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056050765.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056193761.1"}]},{"database":"GeneID","id":"80889485","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_002326","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 3"}]},{"database":"GO","id":"GO:0070867","properties":[{"key":"GoTerm","value":"C:mating projection tip membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0140351","properties":[{"key":"GoTerm","value":"F:glycosylceramide flippase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0140346","properties":[{"key":"GoTerm","value":"F:phosphatidylserine flippase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0099040","properties":[{"key":"GoTerm","value":"P:ceramide translocation"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006897","properties":[{"key":"GoTerm","value":"P:endocytosis"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0007163","properties":[{"key":"GoTerm","value":"P:establishment or maintenance of cell polarity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd02073","properties":[{"key":"EntryName","value":"P-type_ATPase_APLT_Dnf-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.1110.10:FF:000048","properties":[{"key":"EntryName","value":"Phospholipid-transporting ATPase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1000:FF:000108","properties":[{"key":"EntryName","value":"Phospholipid-transporting ATPase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.1000:FF:000001","properties":[{"key":"EntryName","value":"Phospholipid-transporting ATPase IC"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.1110.10","properties":[{"key":"EntryName","value":"Calcium-transporting ATPase, cytoplasmic domain N"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.70.150.10","properties":[{"key":"EntryName","value":"Calcium-transporting ATPase, cytoplasmic transduction domain A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.1000","properties":[{"key":"EntryName","value":"HAD superfamily/HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR023299","properties":[{"key":"EntryName","value":"ATPase_P-typ_cyto_dom_N"}]},{"database":"InterPro","id":"IPR018303","properties":[{"key":"EntryName","value":"ATPase_P-typ_P_site"}]},{"database":"InterPro","id":"IPR023298","properties":[{"key":"EntryName","value":"ATPase_P-typ_TM_dom_sf"}]},{"database":"InterPro","id":"IPR008250","properties":[{"key":"EntryName","value":"ATPase_P-typ_transduc_dom_A_sf"}]},{"database":"InterPro","id":"IPR036412","properties":[{"key":"EntryName","value":"HAD-like_sf"}]},{"database":"InterPro","id":"IPR023214","properties":[{"key":"EntryName","value":"HAD_sf"}]},{"database":"InterPro","id":"IPR006539","properties":[{"key":"EntryName","value":"P-type_ATPase_IV"}]},{"database":"InterPro","id":"IPR032631","properties":[{"key":"EntryName","value":"P-type_ATPase_N"}]},{"database":"InterPro","id":"IPR001757","properties":[{"key":"EntryName","value":"P_typ_ATPase"}]},{"database":"InterPro","id":"IPR032630","properties":[{"key":"EntryName","value":"P_typ_ATPase_c"}]},{"database":"InterPro","id":"IPR044492","properties":[{"key":"EntryName","value":"P_typ_ATPase_HD_dom"}]},{"database":"NCBIfam","id":"TIGR01652","properties":[{"key":"EntryName","value":"ATPase-Plipid"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01494","properties":[{"key":"EntryName","value":"ATPase_P-type"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24092:SF180","properties":[{"key":"EntryName","value":"PHOSPHOLIPID-TRANSPORTING ATPASE DNF1-RELATED"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR24092","properties":[{"key":"EntryName","value":"PROBABLE PHOSPHOLIPID-TRANSPORTING ATPASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13246","properties":[{"key":"EntryName","value":"Cation_ATPase"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16212","properties":[{"key":"EntryName","value":"PhoLip_ATPase_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF16209","properties":[{"key":"EntryName","value":"PhoLip_ATPase_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00119","properties":[{"key":"EntryName","value":"CATATPASE"}]},{"database":"SFLD","id":"SFLDG00002","properties":[{"key":"EntryName","value":"C1.7:_P-type_atpase_like"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDS00003","properties":[{"key":"EntryName","value":"Haloacid_Dehalogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"SFLD","id":"SFLDF00027","properties":[{"key":"EntryName","value":"p-type_atpase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81653","properties":[{"key":"EntryName","value":"Calcium ATPase, transduction domain A"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81665","properties":[{"key":"EntryName","value":"Calcium ATPase, transmembrane domain M"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56784","properties":[{"key":"EntryName","value":"HAD-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF81660","properties":[{"key":"EntryName","value":"Metal cation-transporting ATPase, ATP-binding domain N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00154","properties":[{"key":"EntryName","value":"ATPASE_E1_E2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPDSLTPEAAANGADLDKVQTQRARWATRRMTIKSGSTKRRSLLNRHNRKKSSASEKSVGAPGGDGGHGPFSIGDDNDENDAEASEDEVEEDPDKRTLFFNLPLPDDMLDDEGNPSTSYARNKIRTAKYTPLSFIPKNIWFQFHNVANIFFLFVIILVIFPIFGSVNPGLSAVPLIVIICLTAIKDAIEDYRRTVTDIELNNAPVHRLMNWDNVNVEVGDVSTWRRIKKATSRFFGGIWYAIQSMWSKQARQKRIERKAKANGIEEEEPRPSVETQRTRMSIRQSINSHFGHRESTHEDIQMTPVPSPSPTGHIKIQEPAKPDNARLAAMQDMKTDIINYRRAPTNARFKKDAWKNIVVGDFVRIYNDDELPADVIILATSDPDGACYVETKNLDGETNLKVRQALRCGRTLKHARDCERSEFIVESEAPQSNLYKFNGAIRWKQNIPGYEDDEREDMTEAITIDNLLLRGCNLRNTDWILGVVVYTGHDTKIMMNTGMTPSKRARIAREMNFNVVCNFGILFIMCLVSAIINGAAWARTDTSKNFFDFGSIGGSPPVTGFITFWAAIINFQNLVPISLYITLEIVRTLQAVFIFSDAEMYYEPIDQPCVPKTWNISDDVGQIEYIFSDKTGTLTQNVMEFKKATINGHPYGEAYTEAQAGMQKRAGIDVSTESDRIRAEIAEAKVQSIAGLRKIYDNPYFYDDSLTFVAPDFVADLSGESGSAQKEANETFMLALALCHSVIAEKAPGDPPRMLFKAQSPDEEALVATARDMGFTVLGSSGDGIDVNIMGEDRHYPILNTIEFNSTRKRMSSIVKMPDGRIVIFCKGADSVIYSRLRKGEQRELRQETAEHLEMFAREGLRTLCIAMKEITEEEYRSWKKEHDLAASALEHREEKLEAAAELIEQDFLLLGGTAIEDRLQIGVPDTIELLGQAGIKLWVLTGDKVETAINIGFSCNLLNNDMELIHLKVDEEADDDVSDDMLLDELEKELDQHLNHFGMTGSDEELKAAKKNHEPPGPTHGLVIDGFALRWALHDRLKQKFLLLCKQCRSVLCCRVSPAQKASVVAMVKNGLDVMTLSIGDGANDVAMIQEADVGVGIAGLEGRQASMSSDYAIGQFRFLQRLVLVHGRWSYRRLAESISNFFYKNMVWVFGLLWFQIYCDFDITYLFEYSYIIMFNLFFTSVPVGVLGVLDQDVSDKVSLAVPELYRTGIERLEWTQRKFWLYMFDGVYQSVMAFYVPYLIFSNSRPVTFNGLAVDDRYRLGAYVAHPAVLTINGYIMINSYRWDWLMLLIIAISDLFVFFWTGVYTSFTSSSTFYKAGAEIYGEASFWACFFIVPVLCLFPRFSIKALQKVFYPYDVDIVREQVFMGKFDYLKEPKEKDDGKTDSRSQGSHGSSKRSSRKSKHMQYASVDEDLRPIYPPSTVTRETYNGAHSQQGSADTTNMQRYSVENPMHRISTDRPRPSFDRMRASYDRTRASFEASNDFTSAARLSRIESSHSRGHSHSHSGMIRSRLRALSSLSKKSDA","length":1527,"molWeight":172588,"crc64":"52D7B98443448D4D","md5":"C1E8886F25935F8916943AFD0B28B0DC"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":5,"COFACTOR":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Transmembrane":10,"Domain":2,"Region":4,"Compositional bias":6,"Active site":1,"Binding site":18},"uniParcId":"UPI0023123528"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QD00","uniProtkbId":"A0A9W8QD00_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4151562.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039850"}],"value":"Short/branched chain specific acyl-CoA dehydrogenase, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012046"}],"value":"1.3.8.1"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00039036"}],"value":"1.3.8.5"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00042821"}],"value":"2-methyl branched chain acyl-CoA dehydrogenase"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00041537"}],"value":"2-methylbutyryl-coenzyme A dehydrogenase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4151562.1"}],"value":"LMH87_012253"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00094237"}],"value":"Short and branched chain specific acyl-CoA dehydrogenase that catalyzes the proR-proR stereospecific alpha,beta-dehydrogenation of fatty acyl-CoA thioesters using the electron transfer flavoprotein (ETF) as their physiologic electron acceptor, resulting in the formation of trans-2-enoyl-CoA ((2E)-enoyl-CoA). Among the different mitochondrial acyl-CoA dehydrogenases, acts specifically on short and branched chain acyl-CoA derivatives such as (S)-2-methylbutyryl-CoA as well as short straight chain acyl-CoAs such as butyryl-CoA (butanoyl-CoA). Plays an important role in the metabolism of L-isoleucine by catalyzing the dehydrogenation of 2-methylbutyryl-CoA, one of the steps of the L-isoleucine catabolic pathway. Can also act on valproyl-CoA, a metabolite of valproic acid, an antiepileptic drug"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2R)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = ethylacryloyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65296"},{"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:156439"},{"database":"ChEBI","id":"CHEBI:156440"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65297"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048592"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2S)-2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48256"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:88166"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:48257"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049552"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylbutanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-methylbut-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43780"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57336"},{"database":"ChEBI","id":"CHEBI:57337"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"}],"ecNumber":"1.3.8.5","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43781"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048235"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-methylpropanoyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = 2-methylpropenoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44180"},{"database":"Rhea","id":"RHEA-COMP:10685"},{"database":"Rhea","id":"RHEA-COMP:10686"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57338"},{"database":"ChEBI","id":"CHEBI:57692"},{"database":"ChEBI","id":"CHEBI:58307"},{"database":"ChEBI","id":"CHEBI:62500"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:44181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051903"}]}]},{"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":"ARBA00051002"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:47197"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00051002"}]}]},{"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":"ARBA00049096"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24005"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049096"}]}]},{"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":"ARBA00049192"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:43465"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049192"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"valproyl-CoA + oxidized [electron-transfer flavoprotein] + H(+) = (2E)-2-propylpent-2-enoyl-CoA + reduced [electron-transfer flavoprotein]","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:65344"},{"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:156457"},{"database":"ChEBI","id":"CHEBI:156458"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:65345"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048307"}]}]},{"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":"ARBA00037895"}],"value":"Amino-acid degradation; L-isoleucine degradation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005198"}],"value":"Lipid metabolism; mitochondrial fatty acid beta-oxidation"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011881"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"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":"KAJ4151562.1"}],"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":67,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF02771"}]},{"type":"Domain","location":{"start":{"value":181,"modifier":"EXACT"},"end":{"value":276,"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":435,"modifier":"EXACT"}},"description":"Acyl-CoA dehydrogenase/oxidase C-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00441"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"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":"ARBA00023128"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"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:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4151562.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4151562.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000009","properties":[{"key":"ProteinId","value":"KAJ4151562.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056053276.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056201533.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8QD00","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80899412","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_012253","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 4"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0050660","properties":[{"key":"GoTerm","value":"F:flavin adenine dinucleotide binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003853","properties":[{"key":"GoTerm","value":"F:short-chain 2-methyl fatty acyl-CoA dehydrogenase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046395","properties":[{"key":"GoTerm","value":"P:carboxylic acid catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006631","properties":[{"key":"GoTerm","value":"P:fatty acid metabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd01158","properties":[{"key":"EntryName","value":"SCAD_SBCAD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.540.10:FF:000012","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.140.10:FF:000002","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase short/branched chain"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.40.110.10:FF:000001","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.540.10","properties":[{"key":"EntryName","value":"Acyl-CoA dehydrogenase/oxidase, N-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.110.10","properties":[{"key":"EntryName","value":"Butyryl-CoA Dehydrogenase, subunit A, domain 2"},{"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":"IPR006089","properties":[{"key":"EntryName","value":"Acyl-CoA_DH_CS"}]},{"database":"InterPro","id":"IPR046373","properties":[{"key":"EntryName","value":"Acyl-CoA_Oxase/DH_mid-dom_sf"}]},{"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":"IPR013786","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N"}]},{"database":"InterPro","id":"IPR037069","properties":[{"key":"EntryName","value":"AcylCoA_DH/ox_N_sf"}]},{"database":"InterPro","id":"IPR009100","properties":[{"key":"EntryName","value":"AcylCoA_DH/oxidase_NM_dom_sf"}]},{"database":"PANTHER","id":"PTHR43884","properties":[{"key":"EntryName","value":"ACYL-COA DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43884:SF1","properties":[{"key":"EntryName","value":"SHORT_BRANCHED CHAIN SPECIFIC ACYL-COA DEHYDROGENASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00441","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02770","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_M"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02771","properties":[{"key":"EntryName","value":"Acyl-CoA_dh_N"},{"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"}]},{"database":"PROSITE","id":"PS00072","properties":[{"key":"EntryName","value":"ACYL_COA_DH_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00073","properties":[{"key":"EntryName","value":"ACYL_COA_DH_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MSSFTRAIRPALQGGRRVLLAQRLPATQALARPVAAAALRSLSTTAPRLSSVDISEIPPTPITHLSEVETAMADTVSKFATEVVLPKARDMDEAEAMDPTVVEQLFEQGLMGIEIPEEYGGAGMNFTAAIIAIEELARADPSVSVMVDVHNTLCNTALMKWGSEALKKKYLPKLATNTVASFCLSEPVSGSDAFAMATRATATADGYKINGSKMWITNSMEAGFFIVFANLDPSKGYKGITAFIVDKDTPGFSIAKKEKKLGIRASSTCVLNFDDVVVPKENLLGKEGDGYKYAIGILNEGRIGIAAQMTGLALGAFENAVKYVWNDRKQFGALVGEFQGMQHQIAQSYTEIAAARALVYNAARKKEAGEDFVRDAAMAKLYASQVAGRVSGLAVEWMGGMGFVREGLAEKFWRDSKIGAIYEGTSNIQLNTIAKLLQKEYTA","length":443,"molWeight":47698,"crc64":"2F1A88FE93E69B4A","md5":"3CE6172ED0871FFCA7D960846B18D04B"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":8,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":3},"uniParcId":"UPI00230A5368"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QEH6","uniProtkbId":"A0A9W8QEH6_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4154125.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Adenylyltransferase and sulfurtransferase uba4"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Common component for nitrate reductase and xanthine dehydrogenase protein F"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Ubiquitin-like protein activator 4"}}],"includes":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Molybdopterin-synthase adenylyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"2.7.7.80"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Adenylyltransferase uba4"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Sulfur carrier protein MOCS2A adenylyltransferase"}}]},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Molybdopterin-synthase sulfurtransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"2.8.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Sulfurtransferase uba4"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Sulfur carrier protein MOCS2A sulfurtransferase"}}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"uba4"},"synonyms":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"cnxF"}],"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4154125.1"}],"value":"LMH87_010588"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and MOCS2A. Its N-terminus first activates urm1 and MOCS2A as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and MOCS2A to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as nucleophile towards urm1 and MOCS2A. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00043893"}],"value":"Plays a central role in 2-thiolation of mcm(5)S(2)U at tRNA wobble positions of cytosolic tRNA(Lys), tRNA(Glu) and tRNA(Gln). Also essential during biosynthesis of the molybdenum cofactor. Acts by mediating the C-terminal thiocarboxylation of sulfur carriers urm1 and mocs2a. Its N-terminus first activates urm1 and mocs2a as acyl-adenylates (-COAMP), then the persulfide sulfur on the catalytic cysteine is transferred to urm1 and mocs2a to form thiocarboxylation (-COSH) of their C-terminus. The reaction probably involves hydrogen sulfide that is generated from the persulfide intermediate and that acts as a nucleophile towards urm1 and mocs2a. Subsequently, a transient disulfide bond is formed. Does not use thiosulfate as sulfur donor; nfs1 probably acting as a sulfur donor for thiocarboxylation reactions"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly + ATP + H(+) = [molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:43616"},{"database":"Rhea","id":"RHEA-COMP:12159"},{"database":"Rhea","id":"RHEA-COMP:12202"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:90618"},{"database":"ChEBI","id":"CHEBI:90778"}],"ecNumber":"2.7.7.80","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"[molybdopterin-synthase sulfur-carrier protein]-C-terminal Gly-Gly-AMP + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] + AH2 = [molybdopterin-synthase sulfur-carrier protein]-C-terminal-Gly-aminoethanethioate + L-cysteinyl-[cysteine desulfurase] + A + AMP + 2 H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:48612"},{"database":"Rhea","id":"RHEA-COMP:12157"},{"database":"Rhea","id":"RHEA-COMP:12158"},{"database":"Rhea","id":"RHEA-COMP:12159"},{"database":"Rhea","id":"RHEA-COMP:19907"},{"database":"ChEBI","id":"CHEBI:13193"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17499"},{"database":"ChEBI","id":"CHEBI:29950"},{"database":"ChEBI","id":"CHEBI:61963"},{"database":"ChEBI","id":"CHEBI:90618"},{"database":"ChEBI","id":"CHEBI:232372"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.8.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Zn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29105"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Binds 1 zinc ion per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Cofactor biosynthesis; molybdopterin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"tRNA modification; 5-methoxycarbonylmethyl-2-thiouridine-tRNA biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004514"}],"value":"Cytoplasm, cytosol","id":"SL-0091"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"In the N-terminal section; belongs to the HesA/MoeB/ThiF family. UBA4 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4154125.1"}],"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":334,"modifier":"EXACT"},"end":{"value":439,"modifier":"EXACT"}},"description":"Rhodanese","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50206"}]},{"type":"Active site","location":{"start":{"value":235,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"Glycyl thioester intermediate; for adenylyltransferase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}]},{"type":"Active site","location":{"start":{"value":394,"modifier":"EXACT"},"end":{"value":394,"modifier":"EXACT"}},"description":"Cysteine persulfide intermediate; for sulfurtransferase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}]},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":107,"modifier":"EXACT"},"end":{"value":107,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":118,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":131,"modifier":"EXACT"},"end":{"value":131,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":218,"modifier":"EXACT"},"end":{"value":218,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}},{"type":"Binding site","location":{"start":{"value":221,"modifier":"EXACT"},"end":{"value":221,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29105"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"ligand":{"name":"Zn(2+)","id":"ChEBI:CHEBI:29105"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023150"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"id":"KW-0501","category":"Biological process","name":"Molybdenum cofactor biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"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_03049"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022695"}],"id":"KW-0548","category":"Molecular function","name":"Nucleotidyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"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_03049"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022694"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"id":"KW-0819","category":"Biological process","name":"tRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022786"}],"id":"KW-0833","category":"Biological process","name":"Ubl conjugation pathway"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03049"}],"id":"KW-0862","category":"Ligand","name":"Zinc"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4154125.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4154125.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000008","properties":[{"key":"ProteinId","value":"KAJ4154125.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8QEH6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 5"}]},{"database":"GO","id":"GO:0005829","properties":[{"key":"GoTerm","value":"C:cytosol"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0061605","properties":[{"key":"GoTerm","value":"F:molybdopterin-synthase adenylyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0061604","properties":[{"key":"GoTerm","value":"F:molybdopterin-synthase sulfurtransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004792","properties":[{"key":"GoTerm","value":"F:thiosulfate-cyanide sulfurtransferase activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042292","properties":[{"key":"GoTerm","value":"F:URM1 activating enzyme activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006777","properties":[{"key":"GoTerm","value":"P:Mo-molybdopterin cofactor biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0032447","properties":[{"key":"GoTerm","value":"P:protein urmylation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0002143","properties":[{"key":"GoTerm","value":"P:tRNA wobble position uridine thiolation"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00757","properties":[{"key":"EntryName","value":"ThiF_MoeB_HesA_family"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000033","properties":[{"key":"EntryName","value":"Adenylyltransferase and sulfurtransferase MOCS3"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.250.10","properties":[{"key":"EntryName","value":"Rhodanese-like domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03049","properties":[{"key":"EntryName","value":"MOCS3_Uba4"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR028885","properties":[{"key":"EntryName","value":"MOCS3/Uba4"}]},{"database":"InterPro","id":"IPR001763","properties":[{"key":"EntryName","value":"Rhodanese-like_dom"}]},{"database":"InterPro","id":"IPR036873","properties":[{"key":"EntryName","value":"Rhodanese-like_dom_sf"}]},{"database":"InterPro","id":"IPR045886","properties":[{"key":"EntryName","value":"ThiF/MoeB/HesA"}]},{"database":"InterPro","id":"IPR000594","properties":[{"key":"EntryName","value":"ThiF_NAD_FAD-bd"}]},{"database":"InterPro","id":"IPR035985","properties":[{"key":"EntryName","value":"Ubiquitin-activating_enz"}]},{"database":"PANTHER","id":"PTHR10953:SF102","properties":[{"key":"EntryName","value":"ADENYLYLTRANSFERASE AND SULFURTRANSFERASE MOCS3"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10953","properties":[{"key":"EntryName","value":"UBIQUITIN-ACTIVATING ENZYME E1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00581","properties":[{"key":"EntryName","value":"Rhodanese"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00899","properties":[{"key":"EntryName","value":"ThiF"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00450","properties":[{"key":"EntryName","value":"RHOD"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69572","properties":[{"key":"EntryName","value":"Activating enzymes of the ubiquitin-like proteins"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50206","properties":[{"key":"EntryName","value":"RHODANESE_3"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MCLTPEEIAQRESELADLKSQLAVAESAKREADDGADTSAAQQDWKWPLKEDEYERYSRQMIVPNFGLQGQLRLRNAKVLLVGAGGLGCPAAAYLAGAGVGVLGLVDGDTVEVSNLHRQVAHSTSRVGMTKVESAITYLKELNPSITYKAHQTHLTPQNAASILSRYDLVLDCTDHPTSRYLISDVCVLLRKPLVSASAFQTSGQLLTLNSPPSRGPCYRCVFPKPPPAESVVGCGEGGIVGPVVGAMGVLQALEAIKLITQGGLEPIDGAAADAAMPKQMTMLLFSSMADTMFRTMQSSLDYVQFCGVAQPVKLLHPAERIPASDYARIAADRGSPHLLIDVREKEHFGLSSIEGSINVPISQFMRSRASTVTGALDWMPADLPHSAPIYVVCRVGNDSQVAAKKLKELGLDRNGERFVGDIDGGLRAWRKDVDPTLPFV","length":441,"molWeight":47465,"crc64":"3AA71D2D17D94C47","md5":"975260580472E663E4E7936236879B5A"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Active site":2,"Binding site":7},"uniParcId":"UPI0023154BCC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QFI2","uniProtkbId":"A0A9W8QFI2_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":10,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155699.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase proenzyme 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"4.1.1.65"}]},"contains":[{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 beta chain"}}},{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phosphatidylserine decarboxylase 2 alpha chain"}}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"PSD2"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155699.1"}],"value":"LMH87_000933"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:20828"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:57262"},{"database":"ChEBI","id":"CHEBI:64612"}],"ecNumber":"4.1.1.65","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyruvate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:15361"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Binds 1 pyruvoyl group covalently per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005189"}],"value":"Lipid metabolism"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit. Interacts with pstB2. This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Golgi apparatus membrane","id":"SL-0134"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Endosome membrane","id":"SL-0100"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function"}],"commentType":"DOMAIN"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"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 autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, 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 prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"value":"Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155699.1"}],"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":968,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 beta chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5041026805"},{"type":"Chain","location":{"start":{"value":969,"modifier":"EXACT"},"end":{"value":1069,"modifier":"EXACT"}},"description":"Phosphatidylserine decarboxylase 2 alpha chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"featureId":"PRO_5041026806"},{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":120,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":248,"modifier":"EXACT"},"end":{"value":367,"modifier":"EXACT"}},"description":"C2","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50004"}]},{"type":"Domain","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":531,"modifier":"EXACT"}},"description":"EF-hand","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50222"}]},{"type":"Region","location":{"start":{"value":170,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":240,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":374,"modifier":"EXACT"},"end":{"value":461,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":594,"modifier":"EXACT"},"end":{"value":626,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1005,"modifier":"EXACT"},"end":{"value":1069,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":195,"modifier":"EXACT"},"end":{"value":223,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":396,"modifier":"EXACT"},"end":{"value":407,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":413,"modifier":"EXACT"},"end":{"value":451,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":602,"modifier":"EXACT"},"end":{"value":618,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":824,"modifier":"EXACT"},"end":{"value":824,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":882,"modifier":"EXACT"},"end":{"value":882,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":969,"modifier":"EXACT"},"end":{"value":969,"modifier":"EXACT"}},"description":"Charge relay system; for autoendoproteolytic cleavage activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Active site","location":{"start":{"value":969,"modifier":"EXACT"},"end":{"value":969,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Site","location":{"start":{"value":968,"modifier":"EXACT"},"end":{"value":969,"modifier":"EXACT"}},"description":"Cleavage (non-hydrolytic); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]},{"type":"Modified residue","location":{"start":{"value":969,"modifier":"EXACT"},"end":{"value":969,"modifier":"EXACT"}},"description":"Pyruvic acid (Ser); by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022837"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10142"}],"id":"KW-0106","category":"Ligand","name":"Calcium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022793"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0210","category":"Molecular function","name":"Decarboxylase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0967","category":"Cellular component","name":"Endosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0333","category":"Cellular component","name":"Golgi apparatus"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022516"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023239"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0456","category":"Molecular function","name":"Lyase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10142"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023209"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0594","category":"Biological process","name":"Phospholipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023264"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-1208","category":"Biological process","name":"Phospholipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023317"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0670","category":"Ligand","name":"Pyruvate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023145"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03209"}],"id":"KW-0865","category":"PTM","name":"Zymogen"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155699.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155699.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000007","properties":[{"key":"ProteinId","value":"KAJ4155699.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8QFI2","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 6"}]},{"database":"GO","id":"GO:0010008","properties":[{"key":"GoTerm","value":"C:endosome membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0000139","properties":[{"key":"GoTerm","value":"C:Golgi membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005795","properties":[{"key":"GoTerm","value":"C:Golgi stack"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005509","properties":[{"key":"GoTerm","value":"F:calcium ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004609","properties":[{"key":"GoTerm","value":"F:phosphatidylserine decarboxylase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006646","properties":[{"key":"GoTerm","value":"P:phosphatidylethanolamine biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0016540","properties":[{"key":"GoTerm","value":"P:protein autoprocessing"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd04039","properties":[{"key":"EntryName","value":"C2_PSD"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd04024","properties":[{"key":"EntryName","value":"C2A_Synaptotagmin-like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.238.10:FF:000445","properties":[{"key":"EntryName","value":"Phosphatidylserine decarboxylase proenzyme 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.150:FF:000198","properties":[{"key":"EntryName","value":"Phosphatidylserine decarboxylase proenzyme 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.60.40.150:FF:000295","properties":[{"key":"EntryName","value":"Phosphatidylserine decarboxylase proenzyme 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.60.40.150","properties":[{"key":"EntryName","value":"C2 domain"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.238.10","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00663","properties":[{"key":"EntryName","value":"PS_decarb_PSD_B_type2"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000008","properties":[{"key":"EntryName","value":"C2_dom"}]},{"database":"InterPro","id":"IPR035892","properties":[{"key":"EntryName","value":"C2_domain_sf"}]},{"database":"InterPro","id":"IPR011992","properties":[{"key":"EntryName","value":"EF-hand-dom_pair"}]},{"database":"InterPro","id":"IPR018247","properties":[{"key":"EntryName","value":"EF_Hand_1_Ca_BS"}]},{"database":"InterPro","id":"IPR002048","properties":[{"key":"EntryName","value":"EF_hand_dom"}]},{"database":"InterPro","id":"IPR003817","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"}]},{"database":"InterPro","id":"IPR033177","properties":[{"key":"EntryName","value":"PSD-B"}]},{"database":"InterPro","id":"IPR033179","properties":[{"key":"EntryName","value":"PSD_type2_pro"}]},{"database":"NCBIfam","id":"TIGR00163","properties":[{"key":"EntryName","value":"PS_decarb"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10067:SF17","properties":[{"key":"EntryName","value":"PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00168","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF02666","properties":[{"key":"EntryName","value":"PS_Dcarbxylase"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00239","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF49562","properties":[{"key":"EntryName","value":"C2 domain (Calcium/lipid-binding domain, CaLB)"},{"key":"MatchStatus","value":"2"}]},{"database":"SUPFAM","id":"SSF47473","properties":[{"key":"EntryName","value":"EF-hand"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50004","properties":[{"key":"EntryName","value":"C2"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00018","properties":[{"key":"EntryName","value":"EF_HAND_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50222","properties":[{"key":"EntryName","value":"EF_HAND_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MGRFKSDNGSSASEATTGLALNIVIMKARNLAAKDRNGTSDPYLVLRLGDARAVTHAVPKTLNPEWNIIEQLPINGINSLVLDVICWDKDRFGKDYLGEFDLALEEIFQNEKNAQEPKWYPLRSKRPGKKTSIVSGEVMLQFNLLDIANPASPHQQTMDRLQALLRSVPDASGSAGVTPAASTTPQADPLAEFVEDDDEEVSDFEEDSNDEGEGEGEGGGEGEDASKPETAEKRRRRLRIRGLKRKNRRGAYAFTNGDSDVVGIIYLEICKITDLPPEHNLTRTSFDMDPFVVASLGRKTYRTRRVRHNLNPVFNEKMLFQLLGHEKSYSFSFTVIDHDKYSGNDFIASCTLPVQELFKKAPQADPATGLYEVREPHEHRGAAPLPHKSRLQRMGLSRTSSSQSLNKKSNKTASVTSATSQAPSLEASQATSNPSLLATPDLQSTSLTESEGNVDDDDPEFHEFSVPLNLKNIEKWESKHNPVIYLRAKYVPYPALRQQFWRAMLRQYDTDESGRISRIELTTMLDTLGSTLKDSTIDSFFQRFPHKAADDEDSWDLTFDEAVICLEDQLEAKSKHSGVADKIKSVTSDVKNLAVGSNAEQSSPASGSSTPSEEGGPEFIEREDSGDEHVVEIRECPICHQPRLNKRKDTDIITHIATCASQDWRQVKTVLMGGFVTASQAQRKWYSKVITKLSYGGYKLGANSANILVQDRMTGQINEEKMSVYVRLGIRMLYKGLKSREMEHKQIRKMLKNLSNKQGKKFDDPASKDEIEKFIHFHRLNIDEVLLPLDQFQNFNEFFYRALKPGARPCSAPNNPAIIVSPADCRSVVFNQITQATKVWVKGREFSMKRLLGDAYPDDVARFENGALGIFRLAPQDYHRFHIPVDGIMGEPKTIAGEYYTVNPMAIRSALDVYGENVRVVVPIDSEVHGRVMVICVGAMMVGSTIITRKAGEKVHRAEELGYFKFGGSTILLLFEPGKMRFDSDLTENSSGALETLIRVGMSVGHSPEEPQWAPDMPLSDENITEEQKKDAKRRIQGSLAQDSPSDSNDDDRMHSLPPSMGTIAASSL","length":1069,"molWeight":119236,"crc64":"65B964E39C011CA0","md5":"3AB8E2B19BAC5711E16A403EBE364E3C"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"DOMAIN":1,"PTM":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Chain":2,"Domain":3,"Region":5,"Compositional bias":4,"Active site":4,"Site":1,"Modified residue":1},"uniParcId":"UPI00230A0C39"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QHC1","uniProtkbId":"A0A9W8QHC1_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4157963.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"Catalase-peroxidase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"value":"CP"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"value":"1.11.1.21"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"value":"Peroxidase/catalase"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"value":"katG"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4157963.1"}],"value":"LMH87_008512"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"value":"Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Confers resistance to H(2)O(2) in hyphae. May play an antioxidative role in fungal defense against the host-produced H(2)O(2) (oxidative burst) at the early stage of plant infection"}],"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_03108"},{"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":"HAMAP-Rule","id":"MF_03108"},{"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_03108"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:60344"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"value":"Binds 1 heme b (iron(II)-protoporphyrin IX) group per monomer."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"value":"Homodimer; disulfide-linked"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"value":"Secreted","id":"SL-0243"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"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":"HAMAP-Rule","id":"MF_03108"},{"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_03108"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00297"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4157963.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":19,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}]},{"type":"Chain","location":{"start":{"value":20,"modifier":"EXACT"},"end":{"value":797,"modifier":"EXACT"}},"description":"Catalase-peroxidase","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"featureId":"PRO_5041020160"},{"type":"Domain","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":462,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Domain","location":{"start":{"value":514,"modifier":"EXACT"},"end":{"value":797,"modifier":"EXACT"}},"description":"Plant heme peroxidase family profile","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50873"}]},{"type":"Region","location":{"start":{"value":45,"modifier":"EXACT"},"end":{"value":68,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":143,"modifier":"EXACT"},"end":{"value":143,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10012"}]},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30413"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"ligand":{"name":"heme","id":"ChEBI:CHEBI:30413"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Binding site","location":{"start":{"value":318,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"axial binding residue","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:60344"},{"database":"ChEBI","id":"CHEBI:18248"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00297"}],"ligand":{"name":"heme b","id":"ChEBI:CHEBI:60344"},"ligandPart":{"name":"Fe","id":"ChEBI:CHEBI:18248"}},{"type":"Site","location":{"start":{"value":139,"modifier":"EXACT"},"end":{"value":139,"modifier":"EXACT"}},"description":"Transition state stabilizer","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}]},{"type":"Cross-link","location":{"start":{"value":277,"modifier":"EXACT"},"end":{"value":303,"modifier":"EXACT"}},"description":"Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with Trp-142)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022617"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"id":"KW-0349","category":"Ligand","name":"Heme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023324"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"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_03108"}],"id":"KW-0408","category":"Ligand","name":"Iron"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022559"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"id":"KW-0575","category":"Molecular function","name":"Peroxidase"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"}],"id":"KW-0964","category":"Cellular component","name":"Secreted"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03108"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003451"}],"id":"KW-0732","category":"Domain","name":"Signal"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4157963.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4157963.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000006","properties":[{"key":"ProteinId","value":"KAJ4157963.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8QHC1","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","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:0005576","properties":[{"key":"GoTerm","value":"C:extracellular region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"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:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0005506","properties":[{"key":"GoTerm","value":"F:iron ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"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:TreeGrafter"}]},{"database":"CDD","id":"cd08200","properties":[{"key":"EntryName","value":"catalase_peroxidase_2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.420.10:FF:000004","properties":[{"key":"EntryName","value":"Catalase-peroxidase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.520.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"1.10.420.10","properties":[{"key":"EntryName","value":"Peroxidase, domain 2"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_01961","properties":[{"key":"EntryName","value":"Catal_peroxid"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000763","properties":[{"key":"EntryName","value":"Catalase_peroxidase"}]},{"database":"InterPro","id":"IPR002016","properties":[{"key":"EntryName","value":"Haem_peroxidase"}]},{"database":"InterPro","id":"IPR010255","properties":[{"key":"EntryName","value":"Haem_peroxidase_sf"}]},{"database":"InterPro","id":"IPR019794","properties":[{"key":"EntryName","value":"Peroxidases_AS"}]},{"database":"InterPro","id":"IPR019793","properties":[{"key":"EntryName","value":"Peroxidases_heam-ligand_BS"}]},{"database":"NCBIfam","id":"TIGR00198","properties":[{"key":"EntryName","value":"cat_per_HPI"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"NF011635","properties":[{"key":"EntryName","value":"PRK15061.1"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555:SF0","properties":[{"key":"EntryName","value":"CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR30555","properties":[{"key":"EntryName","value":"HYDROPEROXIDASE I, BIFUNCTIONAL CATALASE-PEROXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00141","properties":[{"key":"EntryName","value":"peroxidase"},{"key":"MatchStatus","value":"2"}]},{"database":"PRINTS","id":"PR00460","properties":[{"key":"EntryName","value":"BPEROXIDASE"}]},{"database":"PRINTS","id":"PR00458","properties":[{"key":"EntryName","value":"PEROXIDASE"}]},{"database":"SUPFAM","id":"SSF48113","properties":[{"key":"EntryName","value":"Heme-dependent peroxidases"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS00435","properties":[{"key":"EntryName","value":"PEROXIDASE_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00436","properties":[{"key":"EntryName","value":"PEROXIDASE_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50873","properties":[{"key":"EntryName","value":"PEROXIDASE_4"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MPSPSLLALAVSVLPLTTAVSCPYIQGNQAHDAVPVYHPEAIVEGRASPDGPDFGRCPQKSKVAGGGTRSTDFWPCELNLGVLRQNADKTSPLDADFDYASAFTKVDVAQLKKDLTKLQTDSQKFWPADFGNYGPFWIRLSWHNAGTYRMIDGRGGAGMGQQRFAPLNSWPDNASLDKARRLLWPIKQKYGSGLSWADLFVYAGNVGMENMGFPTYGFAFGRVDTWQSDEGIYWGSEQEFFPSKKSSADRYNASTDINERADKLESPLAASNLGLIYVNPEGPDGTPDPKASAKDIRMTFGRMGMDDEETVALIAGGHAFGKTHGAVSGDNIGSEPNAAPLEQQGLGWKNSFKSGVGNYSYTSGLEVIWSRTPTKWANDFIFSLLSHNWTIVTSPGGAKQWEATGANASYPDPFDPHKFHKPTMLTSDLALRYDPTYKNISETFLHDFEYFTEKFALAWYKLLHRDMGPLARYLGPEIPQKAPLIWQDPLPVASEHTIDDADVTQLKKEILSASGLNISNLVTTAWGSASTFRISDKRGGANGARIALKPQSSFAVNNPDRLKTVVSALQGVMEKFNSNNKNKQVSLADLIVLGGTAAVEKAATDAGFNVTVPFTPGRVDATQNQTDEKSFSFLEPQADGFRNYGKGTSRALTEELLVDKAALLTLSPPELTVLVGGLRALDANFDGSKHGILTDCPGKLTNDYFVQLLDISNTWTPVANSNEELYESKDSESGKLKYTATRADLIFSSHPELRAVAEVYASSDAKQKFANDFIKAWNKVMELDRYDIKGRKQNNVQ","length":797,"molWeight":87331,"crc64":"F66F176E98A4ED52","md5":"965129533F6947EE404372F6C71CA6D6"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":4,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"PTM":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Signal":1,"Chain":1,"Domain":2,"Region":1,"Active site":1,"Binding site":2,"Site":1,"Cross-link":1},"uniParcId":"UPI00230B5299"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QHU3","uniProtkbId":"A0A9W8QHU3_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155438.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022255"}],"value":"Histone acetyltransferase ESA1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013184"}],"value":"2.3.1.48"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00074445"}],"value":"Histone acetyltransferase esa1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031065"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00075313"}],"value":"protein 2-hydroxyisobutyryltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031553"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00076782"}],"value":"protein acetyltransferase ESA1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00031133"},{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00077673"}],"value":"protein crotonyltransferase ESA1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155438.1"}],"value":"LMH87_000680"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045805"}],"value":"Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, and histone H2A to form H2AK4ac and H2AK7ac. The NuA4 complex is involved in the DNA damage response and is required for chromosome segregation. The NuA4 complex plays a direct role in repair of DNA double-strand breaks (DSBs) through homologous recombination. Recruitment to promoters depends on H3K4me. Also acetylates non-histone proteins. In addition to protein acetyltransferase, can use different acyl-CoA substrates, such as 2-hydroxyisobutanoyl-CoA (2-hydroxyisobutyryl-CoA) or (2E)-butenoyl-CoA (crotonyl-CoA), and is able to mediate protein 2-hydroxyisobutyrylation and crotonylation, respectively"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(2E)-butenoyl-CoA + L-lysyl-[protein] = N(6)-(2E)-butenoyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:53908"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:13707"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57332"},{"database":"ChEBI","id":"CHEBI:137954"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:53909"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047752"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"2-hydroxyisobutanoyl-CoA + L-lysyl-[protein] = N(6)-(2-hydroxyisobutanoyl)-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:24180"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:15921"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:131780"},{"database":"ChEBI","id":"CHEBI:144968"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:24181"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047557"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[histone] + acetyl-CoA = N(6)-acetyl-L-lysyl-[histone] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:21992"},{"database":"Rhea","id":"RHEA-COMP:9845"},{"database":"Rhea","id":"RHEA-COMP:11338"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:21993"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048940"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"ecNumber":"2.3.1.48","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-lysyl-[protein] + acetyl-CoA = N(6)-acetyl-L-lysyl-[protein] + CoA + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:45948"},{"database":"Rhea","id":"RHEA-COMP:9752"},{"database":"Rhea","id":"RHEA-COMP:10731"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:29969"},{"database":"ChEBI","id":"CHEBI:57287"},{"database":"ChEBI","id":"CHEBI:57288"},{"database":"ChEBI","id":"CHEBI:61930"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:45949"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047787"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00011353"}],"value":"Component of the NuA4 histone acetyltransferase complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00010107"}],"value":"Belongs to the MYST (SAS/MOZ) family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155438.1"}],"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":213,"modifier":"EXACT"},"end":{"value":487,"modifier":"EXACT"}},"description":"MYST-type HAT","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51726"}]},{"type":"Region","location":{"start":{"value":84,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":89,"modifier":"EXACT"},"end":{"value":100,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":112,"modifier":"EXACT"},"end":{"value":122,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":163,"modifier":"EXACT"},"end":{"value":175,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":189,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":201,"modifier":"EXACT"},"end":{"value":211,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":389,"modifier":"EXACT"},"end":{"value":389,"modifier":"EXACT"}},"description":"Proton donor/acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR602717-51"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]},{"type":"Binding site","location":{"start":{"value":393,"modifier":"EXACT"},"end":{"value":393,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:57288"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"ligand":{"name":"acetyl-CoA","id":"ChEBI:CHEBI:57288"}},{"type":"Modified residue","location":{"start":{"value":313,"modifier":"EXACT"},"end":{"value":313,"modifier":"EXACT"}},"description":"N6-acetyllysine; by autocatalysis","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022990"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0007","category":"PTM","name":"Acetylation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023159"}],"id":"KW-0010","category":"Molecular function","name":"Activator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022853"}],"id":"KW-0156","category":"Molecular function","name":"Chromatin regulator"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023163"}],"id":"KW-0804","category":"Biological process","name":"Transcription"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023015"}],"id":"KW-0805","category":"Biological process","name":"Transcription regulation"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01063"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155438.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4155438.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000007","properties":[{"key":"ProteinId","value":"KAJ4155438.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056055562.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056198630.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8QHU3","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80887839","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_000680","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 6"}]},{"database":"GO","id":"GO:0000785","properties":[{"key":"GoTerm","value":"C:chromatin"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005634","properties":[{"key":"GoTerm","value":"C:nucleus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0003682","properties":[{"key":"GoTerm","value":"F:chromatin binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0004402","properties":[{"key":"GoTerm","value":"F:histone acetyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003712","properties":[{"key":"GoTerm","value":"F:transcription coregulator activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006357","properties":[{"key":"GoTerm","value":"P:regulation of transcription by RNA polymerase II"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd04301","properties":[{"key":"EntryName","value":"NAT_SF"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.10.10:FF:000022","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.60.60:FF:000001","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.630.30:FF:000002","properties":[{"key":"EntryName","value":"Histone acetyltransferase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.30.140","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.630.30","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.60.60","properties":[{"key":"EntryName","value":"N-acetyl transferase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.10.10","properties":[{"key":"EntryName","value":"Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016181","properties":[{"key":"EntryName","value":"Acyl_CoA_acyltransferase"}]},{"database":"InterPro","id":"IPR016197","properties":[{"key":"EntryName","value":"Chromo-like_dom_sf"}]},{"database":"InterPro","id":"IPR002717","properties":[{"key":"EntryName","value":"HAT_MYST-type"}]},{"database":"InterPro","id":"IPR050603","properties":[{"key":"EntryName","value":"MYST_HAT"}]},{"database":"InterPro","id":"IPR025995","properties":[{"key":"EntryName","value":"Tudor-knot"}]},{"database":"InterPro","id":"IPR036388","properties":[{"key":"EntryName","value":"WH-like_DNA-bd_sf"}]},{"database":"InterPro","id":"IPR040706","properties":[{"key":"EntryName","value":"Zf-MYST"}]},{"database":"PANTHER","id":"PTHR10615","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10615:SF218","properties":[{"key":"EntryName","value":"HISTONE ACETYLTRANSFERASE ESA1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01853","properties":[{"key":"EntryName","value":"MOZ_SAS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF11717","properties":[{"key":"EntryName","value":"Tudor-knot"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17772","properties":[{"key":"EntryName","value":"zf-MYST"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55729","properties":[{"key":"EntryName","value":"Acyl-CoA N-acyltransferases (Nat)"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54160","properties":[{"key":"EntryName","value":"Chromo domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51726","properties":[{"key":"EntryName","value":"MYST_HAT"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MTAGPSNGEPAVGADVPRLKSFATADTLATGVIAWVKKDGQPRRAEILSIKETKSGKQFYCNFDNFNKRLDEWVPLARIDLSQEVEWPNPEKDKPKEANKKKVPSGAIKKSAVAKKNQKRPGKREDSIKSEATTPHPWSDFVESQRKSTSVGPDGDSQAPDSAGPGTTPATPAGGDEMDVDEKEDDKEEFSREEEIEKLRTSGSMTQNPTEVSRIRNISKVQFGKFDLFPWYFSPYPESFSGEDIIFICEFCLSYYGDEFSFNRHRHKCTLQHPPGNEIYRDDYVSFFEIDGRRQRTWCRNLCLVSKMFLDHKTLYYDVDPFLFYVMAARTDKGFPFVGYFSKEKESADGYNVACILTLPQYQRKGYGRLLIQFSYELSKIEGKLGSPEKPLSDLGLLSYRQYWAENILDLLVGACERGEKVTIEAISSALAMTTVDVEHTLQAMKMQVYHKSDHKIVIPEKLIQQREKRLLKPRRTLDAAKVQWKPPIFTASSRTWGW","length":499,"molWeight":56876,"crc64":"E911E56DF543D630","md5":"79CA3BF810DE519F81CE543F884E6ED9"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":5,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":6,"Active site":1,"Binding site":1,"Modified residue":1},"uniParcId":"UPI002318D486"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QP95","uniProtkbId":"A0A9W8QP95_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165299.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00014008"}],"value":"Fatty acid synthase subunit alpha"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012948"}],"value":"1.1.1.100"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013191"}],"value":"2.3.1.41"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012878"}],"value":"2.3.1.86"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165299.1"}],"value":"LMH87_006936"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a (3R)-hydroxyacyl-[ACP] + NADP(+) = a 3-oxoacyl-[ACP] + NADPH + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:17397"},{"database":"Rhea","id":"RHEA-COMP:9916"},{"database":"Rhea","id":"RHEA-COMP:9945"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57783"},{"database":"ChEBI","id":"CHEBI:58349"},{"database":"ChEBI","id":"CHEBI:78776"},{"database":"ChEBI","id":"CHEBI:78827"}],"ecNumber":"1.1.1.100","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048508"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a fatty acyl-[ACP] + malonyl-[ACP] + H(+) = a 3-oxoacyl-[ACP] + holo-[ACP] + CO2","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:22836"},{"database":"Rhea","id":"RHEA-COMP:9623"},{"database":"Rhea","id":"RHEA-COMP:9685"},{"database":"Rhea","id":"RHEA-COMP:9916"},{"database":"Rhea","id":"RHEA-COMP:14125"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16526"},{"database":"ChEBI","id":"CHEBI:64479"},{"database":"ChEBI","id":"CHEBI:78449"},{"database":"ChEBI","id":"CHEBI:78776"},{"database":"ChEBI","id":"CHEBI:138651"}],"ecNumber":"2.3.1.41","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00049541"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"acetyl-CoA + n malonyl-CoA + 2n NADPH + 4n H(+) = a long-chain-acyl-CoA + n CoA + n CO2 + 2n NADP(+).","ecNumber":"2.3.1.86","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048237"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pantetheine 4'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:47942"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007485"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000454"}],"value":"Belongs to the thiolase-like superfamily. Fungal fatty acid synthetase subunit alpha family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165299.1"}],"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":141,"modifier":"EXACT"},"end":{"value":216,"modifier":"EXACT"}},"description":"Carrier","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50075"}]},{"type":"Domain","location":{"start":{"value":1091,"modifier":"EXACT"},"end":{"value":1628,"modifier":"EXACT"}},"description":"Ketosynthase family 3 (KS3)","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS52004"}]},{"type":"Region","location":{"start":{"value":118,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":1326,"modifier":"EXACT"},"end":{"value":1345,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1326,"modifier":"EXACT"},"end":{"value":1335,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":1274,"modifier":"EXACT"},"end":{"value":1274,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10022"}]},{"type":"Active site","location":{"start":{"value":1274,"modifier":"EXACT"},"end":{"value":1274,"modifier":"EXACT"}},"description":"For beta-ketoacyl synthase activity","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-1"}]},{"type":"Binding site","location":{"start":{"value":1745,"modifier":"EXACT"},"end":{"value":1745,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1746,"modifier":"EXACT"},"end":{"value":1746,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1747,"modifier":"EXACT"},"end":{"value":1747,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1845,"modifier":"EXACT"},"end":{"value":1845,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":1846,"modifier":"EXACT"},"end":{"value":1846,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-3"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Modified residue","location":{"start":{"value":176,"modifier":"EXACT"},"end":{"value":176,"modifier":"EXACT"}},"description":"O-(pantetheine 4'-phosphoryl)serine","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-4"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00258"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023160"}],"id":"KW-0275","category":"Biological process","name":"Fatty acid biosynthesis"},{"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":"ARBA00022516"}],"id":"KW-0444","category":"Biological process","name":"Lipid biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023098"}],"id":"KW-0443","category":"Biological process","name":"Lipid metabolism"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-3"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000454-3"}],"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"}],"id":"KW-0520","category":"Ligand","name":"NAD"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022857"}],"id":"KW-0521","category":"Ligand","name":"NADP"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023002"}],"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022450"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000454"}],"id":"KW-0596","category":"PTM","name":"Phosphopantetheine"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022553"}],"id":"KW-0597","category":"PTM","name":"Phosphoprotein"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000454"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165299.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165299.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000001","properties":[{"key":"ProteinId","value":"KAJ4165299.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056060214.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056191946.1"}]},{"database":"GeneID","id":"80894095","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_006936","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 1"}]},{"database":"GO","id":"GO:0005835","properties":[{"key":"GoTerm","value":"C:fatty acid synthase complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004316","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] reductase (NADPH) activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004315","properties":[{"key":"GoTerm","value":"F:3-oxoacyl-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004312","properties":[{"key":"GoTerm","value":"F:fatty acid synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0004321","properties":[{"key":"GoTerm","value":"F:fatty-acyl-CoA synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0008897","properties":[{"key":"GoTerm","value":"F:holo-[acyl-carrier-protein] synthase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000287","properties":[{"key":"GoTerm","value":"F:magnesium ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0042759","properties":[{"key":"GoTerm","value":"P:long-chain fatty acid biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0044550","properties":[{"key":"GoTerm","value":"P:secondary metabolite biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"CDD","id":"cd00828","properties":[{"key":"EntryName","value":"elong_cond_enzymes"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd08950","properties":[{"key":"EntryName","value":"KR_fFAS_SDR_c_like"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.470.20:FF:000005","properties":[{"key":"EntryName","value":"Fatty acid synthase alpha subunit FasA"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.70.2490:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.720:FF:000168","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.90.25.70:FF:000001","properties":[{"key":"EntryName","value":"Fatty acid synthase subunit alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.2490","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.47.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.25.70","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.140.1390","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.140.1410","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.1930","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"6.10.250.1940","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.470.20","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.720","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-like Domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00101","properties":[{"key":"EntryName","value":"AcpS"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR008278","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom"}]},{"database":"InterPro","id":"IPR037143","properties":[{"key":"EntryName","value":"4-PPantetheinyl_Trfase_dom_sf"}]},{"database":"InterPro","id":"IPR002582","properties":[{"key":"EntryName","value":"ACPS"}]},{"database":"InterPro","id":"IPR016035","properties":[{"key":"EntryName","value":"Acyl_Trfase/lysoPLipase"}]},{"database":"InterPro","id":"IPR040899","properties":[{"key":"EntryName","value":"Fas_alpha_ACP"}]},{"database":"InterPro","id":"IPR047224","properties":[{"key":"EntryName","value":"FAS_alpha_su_C"}]},{"database":"InterPro","id":"IPR026025","properties":[{"key":"EntryName","value":"FAS_alpha_yeast"}]},{"database":"InterPro","id":"IPR041550","properties":[{"key":"EntryName","value":"FASI_helical"}]},{"database":"InterPro","id":"IPR050830","properties":[{"key":"EntryName","value":"Fungal_FAS"}]},{"database":"InterPro","id":"IPR014031","properties":[{"key":"EntryName","value":"KAS_C"}]},{"database":"InterPro","id":"IPR014030","properties":[{"key":"EntryName","value":"KAS_N"}]},{"database":"InterPro","id":"IPR018201","properties":[{"key":"EntryName","value":"Ketoacyl_synth_AS"}]},{"database":"InterPro","id":"IPR036291","properties":[{"key":"EntryName","value":"NAD(P)-bd_dom_sf"}]},{"database":"InterPro","id":"IPR020841","properties":[{"key":"EntryName","value":"PKS_Beta-ketoAc_synthase_dom"}]},{"database":"InterPro","id":"IPR009081","properties":[{"key":"EntryName","value":"PP-bd_ACP"}]},{"database":"InterPro","id":"IPR004568","properties":[{"key":"EntryName","value":"Ppantetheine-prot_Trfase_dom"}]},{"database":"InterPro","id":"IPR016039","properties":[{"key":"EntryName","value":"Thiolase-like"}]},{"database":"NCBIfam","id":"TIGR00556","properties":[{"key":"EntryName","value":"pantethn_trn"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10982:SF21","properties":[{"key":"EntryName","value":"FATTY ACID SYNTHASE SUBUNIT BETA"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10982","properties":[{"key":"EntryName","value":"MALONYL COA-ACYL CARRIER PROTEIN TRANSACYLASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01648","properties":[{"key":"EntryName","value":"ACPS"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18325","properties":[{"key":"EntryName","value":"Fas_alpha_ACP"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF18314","properties":[{"key":"EntryName","value":"FAS_I_H"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00109","properties":[{"key":"EntryName","value":"ketoacyl-synt"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02801","properties":[{"key":"EntryName","value":"Ketoacyl-synt_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000454","properties":[{"key":"EntryName","value":"FAS_yeast_alpha"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56214","properties":[{"key":"EntryName","value":"4'-phosphopantetheinyl transferase"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52151","properties":[{"key":"EntryName","value":"FabD/lysophospholipase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51735","properties":[{"key":"EntryName","value":"NAD(P)-binding Rossmann-fold domains"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53901","properties":[{"key":"EntryName","value":"Thiolase-like"},{"key":"MatchStatus","value":"2"}]},{"database":"PROSITE","id":"PS50075","properties":[{"key":"EntryName","value":"CARRIER"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00606","properties":[{"key":"EntryName","value":"KS3_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS52004","properties":[{"key":"EntryName","value":"KS3_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MRPEVEQELSHTLLIELLAYQFASPVRWIETQDVFLAERTAERVVEVGPADTLGVMAKRTLASKYEAYDAAKSVQRQILCYNKDAKEIYYDVDPVEDEPEPAAPAAAASGGAAPAAAAPAAAAAPPPPSAGPAAQVPDQPVQAVDIVRALIAQKLKKPLLDVPLSKAIKDLVGGKSTLQNEILGDLGKEFGSTPEKPEDTPLDELGASIQPTFDGNLGKVSQSLIARLISSKMPGGFNITAARKYLETRWGLGSGRQDGALLLALTMEPAARLGAEGDAKAFLDDVTQKYAANAGVSLTTTAAADAGGGGGGGMMMDPAAIDALTKDQRALFKQQLELFARYLKMDLRSGDKAFINSQKSEKVLQAQLDLWTAEHGDFYASGIEPVFSPLKARTYDSSWNWARQDGLSMYFEIIFGRLQTVDREIVSQCIRIMNKSNPKLLDFMQYHIDNCPTERGETYKLAQELGYQLIENCKDVLNVAPHYKDVAVPTGPRTTVDARGNLNYEEVPRASCRKLEHYVQQMVEGGKISEYGNRTKVQSDLQRIYKLIKQQHKMSKTSQLEIKSLYGDVLRSLGMNENQIIPKENGKSRRATTLKGSSNNKGRVETIPFLHLKKKSLHGWDYSKKLTSVYLDCLEEAARSGVTYTGKHVLMTGAGAGSIGAEVLQGLISGGARVVVTTSRFSKEVTEYYQSMYTRYGSRGSQVVVVPFNQGSKQDVEALIDYIYDPKNGLGWDLDYIVPFAAISENGRQIDSIDSRSELAHRIMLTNLVRLLGCVKAQKAERGFETRPAQVVLPLSPNHGTFGNDGLYSESKLALETLFNRWYSESWANYLTICGAVIGWTRGTGLMSGNNIVAEGVEAFGVRTFSQQEMAFNLLGLMSPTIVDLCQSEPVFADLNGGLQFIPNLNEAMTKLRKDIMETSEIRRAVTKESAIENTIVNGAESEVLYKKKTIDPRANIKFDFPTLPDWKKEVAPLNEKLKGMVDLEKVVVVTGFAEVGPWGNSRTRWEMEASGEFSLEGCVEMAWIMGLIKNHNGPIKGKPYAGWVDAKTGDPVDDKDIKAKYEKYILDHSGIRLIEPELFAGYDPNRKQLLHEVVIEEDLEPFESSKETAEEFKREHGDKVEVFEIPESGEYIIRLKKGASLWIPKALRFDRLVAGQIPTGWDAKRYGIPEDIIDQVDPVTLFLLVSTAEALLSSGITDPYEFYKYVHVSEVGNCVGSGMGGATALRGMHKDRYLDQPLQNDILQESFINTMAAWVNMLLISSSGPIKTPVGACATSVESVDIGYETIMEGKARVCFVGGFDDFGEEGSYEFANMKATSNTVDEMAHGRTPKEMSRPTTTTRNGFMESQGCGVQVIMTAKLALDMGVPIHGILALTTTASDKIGRSVPAPGQGVLTTARENAGKFPSPLLDIDYRRRQIERRKKQIKQWQESELEFVHDEISAMKSQQGEFDENEYAHERVQHIEKEAARQEKELLRSMGNNFWKSDPSIAPLRGALATWGLTIDDLGVASFHGTSTKANDKNESSVICQQLRHLGRSEGNAVLGIFQKYLTGHPKGAAGAWMMNGCLQVLNTGLVPGNRNADNVDPIMEDFDMILYPSRSIQTDGIKAFSVTSFGFGQKGAQAIGVHPKYLFATLDERTYADYCTKVEARQKKAYRFFHNGLINNSLFVAKSKAPYTDEQLSSVLLNPDARVSTEKKTSDLTYAANFMKQSEKVVSSTQAKETQQVMETLARKVASQNSKVGVDVEDISAINIENDTFIQRNFTASEIAYCKEAPSPQSSFAGRWSAKEAVFKSLGVTSKGAGAAMKEIEISRDDTGAPKVSLHGDAASAAKQAGVKDISLSISHSDNQAIAVAVASF","length":1859,"molWeight":204108,"crc64":"9E6CF291B3DEEC55","md5":"61EFD0CBC4039910994FA6829E4F28F4"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":3,"COFACTOR":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":2,"Compositional bias":1,"Active site":2,"Binding site":5,"Modified residue":1},"uniParcId":"UPI00231A89D6"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8QS69","uniProtkbId":"A0A9W8QS69_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165499.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"Kynureninase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"3.7.1.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"value":"Biosynthesis of nicotinic acid protein 5"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"value":"L-kynurenine hydrolase"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"value":"BNA5"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165499.1"}],"value":"LMH87_007129"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"Catalyzes the cleavage of L-kynurenine (L-Kyn) and L-3-hydroxykynurenine (L-3OHKyn) into anthranilic acid (AA) and 3-hydroxyanthranilic acid (3-OHAA), respectively"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"3-hydroxy-L-kynurenine + H2O = 3-hydroxyanthranilate + L-alanine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:25143"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:36559"},{"database":"ChEBI","id":"CHEBI:57972"},{"database":"ChEBI","id":"CHEBI:58125"}],"ecNumber":"3.7.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"L-kynurenine + H2O = anthranilate + L-alanine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16813"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:16567"},{"database":"ChEBI","id":"CHEBI:57959"},{"database":"ChEBI","id":"CHEBI:57972"}],"ecNumber":"3.7.1.3","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"pyridoxal 5'-phosphate","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:597326"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"Amino-acid degradation; L-kynurenine degradation; L-alanine and anthranilate from L-kynurenine: step 1/1"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate from L-kynurenine: step 2/3"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"Homodimer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR038800"}],"value":"Belongs to the kynureninase family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"value":"Lacks conserved residue(s) required for the propagation of feature annotation"}],"commentType":"CAUTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165499.1"}],"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":128,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"Aminotransferase class V","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00266"}]},{"type":"Region","location":{"start":{"value":57,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":63,"modifier":"EXACT"},"end":{"value":76,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":158,"modifier":"EXACT"},"end":{"value":158,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":159,"modifier":"EXACT"},"end":{"value":159,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":186,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":270,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":273,"modifier":"EXACT"},"end":{"value":273,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":295,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":336,"modifier":"EXACT"},"end":{"value":336,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Binding site","location":{"start":{"value":364,"modifier":"EXACT"},"end":{"value":364,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:597326"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"ligand":{"name":"pyridoxal 5'-phosphate","id":"ChEBI:CHEBI:597326"}},{"type":"Modified residue","location":{"start":{"value":296,"modifier":"EXACT"},"end":{"value":296,"modifier":"EXACT"}},"description":"N6-(pyridoxal phosphate)lysine","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022642"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"id":"KW-0662","category":"Biological process","name":"Pyridine nucleotide biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022898"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03017"}],"id":"KW-0663","category":"Ligand","name":"Pyridoxal phosphate"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165499.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4165499.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000001","properties":[{"key":"ProteinId","value":"KAJ4165499.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8QS69","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 1"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0030429","properties":[{"key":"GoTerm","value":"F:kynureninase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030170","properties":[{"key":"GoTerm","value":"F:pyridoxal phosphate binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0034354","properties":[{"key":"GoTerm","value":"P:'de novo' NAD+ biosynthetic process from L-tryptophan"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006569","properties":[{"key":"GoTerm","value":"P:L-tryptophan catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0019805","properties":[{"key":"GoTerm","value":"P:quinolinate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"FunFam","id":"3.40.640.10:FF:000031","properties":[{"key":"EntryName","value":"Kynureninase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.90.1150.10","properties":[{"key":"EntryName","value":"Aspartate Aminotransferase, domain 1"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.640.10","properties":[{"key":"EntryName","value":"Type I PLP-dependent aspartate aminotransferase-like (Major domain)"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_01970","properties":[{"key":"EntryName","value":"Kynureninase"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000192","properties":[{"key":"EntryName","value":"Aminotrans_V_dom"}]},{"database":"InterPro","id":"IPR010111","properties":[{"key":"EntryName","value":"Kynureninase"}]},{"database":"InterPro","id":"IPR015424","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase"}]},{"database":"InterPro","id":"IPR015421","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_major"}]},{"database":"InterPro","id":"IPR015422","properties":[{"key":"EntryName","value":"PyrdxlP-dep_Trfase_small"}]},{"database":"NCBIfam","id":"TIGR01814","properties":[{"key":"EntryName","value":"kynureninase"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14084","properties":[{"key":"EntryName","value":"KYNURENINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14084:SF2","properties":[{"key":"EntryName","value":"KYNURENINASE 2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00266","properties":[{"key":"EntryName","value":"Aminotran_5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22580","properties":[{"key":"EntryName","value":"KYNU_C"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF038800","properties":[{"key":"EntryName","value":"KYNU"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53383","properties":[{"key":"EntryName","value":"PLP-dependent transferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MDLSAYSERLRGGAPAKFPADANSLEFAQKLDSQDALSHLRHEFILPTKTSIKKTALDGTLPSTAKTNGTAATNGTSSEDPDVGIYFVGNSLGAQPKAVRKFIDAQLETWASIGVNGHFKTLGNSPLTQWQDMAEDCAKRSADLVGASPSEIVIMNTLTINLHMMMASFYKPDAKRHKIILEWRPFPSDYYAIESQITWHGLDPEKSMVKIEPDESSYMPTEKILATIDAHAEETALLLLPGIQYYSGQLLDMPRITAYARERGIVVGWDLAHAAGNVELKLHDWDVDFACWCTYKYINAGPGAIGGAFVHERHGAVEWNDGADGRPAYRPRLTGWYGGDKSVRFNMDNKFVPTPGAGGYQASNPSALELANLAGALSVFNKTTMRDLRSKALVLTAYAETLLDGILADAGDDTLFRILTPRDPLQRGTQLSVMLREGLLDGVNDALELNGVLCDKRKPGVIRVAPVPLYSRFEDVWRFMQILRGALKV","length":489,"molWeight":53720,"crc64":"A6A46F8AA28D1C84","md5":"0CE0D83665E6D17925348BE2CD1640F7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"PATHWAY":2,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":2},"countByFeatureType":{"Domain":1,"Region":1,"Compositional bias":1,"Binding site":8,"Modified residue":1},"uniParcId":"UPI002322D41C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8UHR9","uniProtkbId":"A0A9W8UHR9_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":14,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145455.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-dependent 6-phosphofructokinase"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"ATP-PFK"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphofructokinase"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"2.7.1.11"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Phosphohexokinase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145455.1"}],"value":"LMH87_004305"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00002659"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Catalyzes the phosphorylation of D-fructose 6-phosphate to fructose 1,6-bisphosphate by ATP, the first committing step of glycolysis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"beta-D-fructose 6-phosphate + ATP = beta-D-fructose 1,6-bisphosphate + ADP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:16109"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:32966"},{"database":"ChEBI","id":"CHEBI:57634"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"2.7.1.11","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048070"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Allosterically activated by ADP, AMP, or fructose 2,6-bisphosphate, and allosterically inhibited by ATP or citrate"}],"commentType":"ACTIVITY REGULATION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004679"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"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_03184"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Cytoplasm","id":"SL-0086"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004287"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004287"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004287"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004325"}],"value":"Mitochondrion membrane","id":"SL-0171"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000533"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade \"E\" sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"value":"Belongs to the phosphofructokinase type A (PFKA) family. ATP-dependent PFK group I subfamily. Eukaryotic two domain clade 'E' sub-subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145455.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":318,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Domain","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":696,"modifier":"EXACT"}},"description":"Phosphofructokinase","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00365"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":384,"modifier":"EXACT"}},"description":"N-terminal catalytic PFK domain 1","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Region","location":{"start":{"value":385,"modifier":"EXACT"},"end":{"value":398,"modifier":"EXACT"}},"description":"Interdomain linker","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Region","location":{"start":{"value":399,"modifier":"EXACT"},"end":{"value":784,"modifier":"EXACT"}},"description":"C-terminal regulatory PFK domain 2","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Active site","location":{"start":{"value":156,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}]},{"type":"Binding site","location":{"start":{"value":15,"modifier":"EXACT"},"end":{"value":15,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":79,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":108,"modifier":"EXACT"},"end":{"value":111,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}},{"type":"Binding site","location":{"start":{"value":109,"modifier":"EXACT"},"end":{"value":109,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420","note":"catalytic"}},{"type":"Binding site","location":{"start":{"value":154,"modifier":"EXACT"},"end":{"value":156,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":191,"modifier":"EXACT"},"end":{"value":191,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":200,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":254,"modifier":"EXACT"},"end":{"value":254,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":286,"modifier":"EXACT"},"end":{"value":286,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":292,"modifier":"EXACT"},"end":{"value":295,"modifier":"EXACT"}},"description":"in other chain","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"substrate","note":"ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":475,"modifier":"EXACT"},"end":{"value":475,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":533,"modifier":"EXACT"},"end":{"value":537,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":571,"modifier":"EXACT"},"end":{"value":571,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":578,"modifier":"EXACT"},"end":{"value":580,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":638,"modifier":"EXACT"},"end":{"value":638,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":664,"modifier":"EXACT"},"end":{"value":664,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":670,"modifier":"EXACT"},"end":{"value":673,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}},{"type":"Binding site","location":{"start":{"value":741,"modifier":"EXACT"},"end":{"value":741,"modifier":"EXACT"}},"description":"in other chain","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:58579"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"ligand":{"name":"beta-D-fructose 2,6-bisphosphate","id":"ChEBI:CHEBI:58579","note":"allosteric activator; ligand shared between dimeric partners"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022533"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0021","category":"Molecular function","name":"Allosteric enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023152"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0324","category":"Biological process","name":"Glycolysis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03184"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"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_03184"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145455.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4145455.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4145455.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056049125.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056195502.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8UHR9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80891464","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_004305","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0005945","properties":[{"key":"GoTerm","value":"C:6-phosphofructokinase complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005741","properties":[{"key":"GoTerm","value":"C:mitochondrial outer membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"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: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":"GO","id":"GO:1902600","properties":[{"key":"GoTerm","value":"P:proton transmembrane transport"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0051453","properties":[{"key":"GoTerm","value":"P:regulation of intracellular pH"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"FunFam","id":"3.40.50.450:FF:000010","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.460:FF:000008","properties":[{"key":"EntryName","value":"ATP-dependent 6-phosphofructokinase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.450","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"3.40.50.460","properties":[{"key":"EntryName","value":"Phosphofructokinase domain"},{"key":"MatchStatus","value":"2"}]},{"database":"HAMAP","id":"MF_03184","properties":[{"key":"EntryName","value":"Phosphofructokinase_I_E"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR009161","properties":[{"key":"EntryName","value":"6-Pfructokinase_euk"}]},{"database":"InterPro","id":"IPR022953","properties":[{"key":"EntryName","value":"ATP_PFK"}]},{"database":"InterPro","id":"IPR015912","properties":[{"key":"EntryName","value":"Phosphofructokinase_CS"}]},{"database":"InterPro","id":"IPR000023","properties":[{"key":"EntryName","value":"Phosphofructokinase_dom"}]},{"database":"InterPro","id":"IPR035966","properties":[{"key":"EntryName","value":"PKF_sf"}]},{"database":"NCBIfam","id":"TIGR02478","properties":[{"key":"EntryName","value":"6PF1K_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697:SF4","properties":[{"key":"EntryName","value":"ATP-DEPENDENT 6-PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR13697","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00365","properties":[{"key":"EntryName","value":"PFK"},{"key":"MatchStatus","value":"2"}]},{"database":"PIRSF","id":"PIRSF000533","properties":[{"key":"EntryName","value":"ATP_PFK_euk"},{"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":"2"}]},{"database":"PROSITE","id":"PS00433","properties":[{"key":"EntryName","value":"PHOSPHOFRUCTOKINASE"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MEAPKKKIAVMTSGGDSPGMNAVVRAVVRTAIHLGCDAFCVYEGYEGLVKGGDLIRQMGWAEVRGYLSEGGTLIGTARCMAFYERPGRLTAAKNMVLNGIDALIICGGDGSLTGADKFRGEWPSLLEELVSTGQLTADQVKPYQHLNIVGLVGSIDNDLSGTDATIGCYSALSRICEMVDYIEATASSHSRAFVIEVMGRHCGWLALLAGVATGADFVFIPERPVSECWHEEMCAVVKRHRSFGKRKTIVIVAEGANDKDGNKISPEQIKDLLADKSEGGLALDTRITTLGHVQRGGTAVAYDRMLGTLQGVEAVKAVLEATPETETCFIAINENKIVRKPLMKAVAETKSVVQAVEAKQFDKAMSLRDTEFSDQYKSYLTTTNVKTDEHKLPEKERMKIGFINVGAPAGGMNAAVRAAVAYCFSRGHTPMAIHNGFAGFARHHDDKPVGAVREFDWLEVDGWASKGGSEIGTNRELPSESGMEHVASLIAKYEFDALFMVGGFEAFHALSQLRIARGQFPALRIPMVLLPATISNNVPGTEYSLGSDTCLNELVQYCDKIKQSASATRRRVFVIETQGGRSGYIATLAGLAVGASAVYIPEEGISLGMLNTDVTHLKKVFAEDTGQSRAGRLILINEKASSVYDAKLIANIIRDEAHGRFESRESIPGHVQQGGVPSPMDRCRAVRHAIKCMEHLQGYGKKSAAGSTDALSTSVIGIKGSELVFTAVQELEEHGTDWPNRRPKQSEWLRMRDIVDVLGGRPQHARPESNVKGLLAKDIKRGLA","length":784,"molWeight":84830,"crc64":"45494DE053F4B121","md5":"5D9B8A7C2B692B420181D2781505E97E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"COFACTOR":1,"ACTIVITY REGULATION":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":2,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Active site":1,"Binding site":18},"uniParcId":"UPI0023178578"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8UID9","uniProtkbId":"A0A9W8UID9_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150618.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Ubiquinone biosynthesis O-methyltransferase, mitochondrial"}},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"3-demethylubiquinol 3-O-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.64"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"3-demethylubiquinone 3-O-methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.-"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Polyprenyldihydroxybenzoate methyltransferase"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"2.1.1.114"}]}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"COQ3"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150618.1"}],"value":"LMH87_011360"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"O-methyltransferase required for two non-consecutive steps during ubiquinone biosynthesis. Catalyzes the 2 O-methylation of 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoic acid into 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoic acid. Also catalyzes the last step of ubiquinone biosynthesis by mediating methylation of 3-demethylubiquinone into ubiquinone. Also able to mediate the methylation of 3-demethylubiquinol into ubiquinol"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3,4-dihydroxy-5-(all-trans-polyprenyl)benzoate + S-adenosyl-L-methionine = a 4-hydroxy-3-methoxy-5-(all-trans-polyprenyl)benzoate + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44452"},{"database":"Rhea","id":"RHEA-COMP:10930"},{"database":"Rhea","id":"RHEA-COMP:10931"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:64694"},{"database":"ChEBI","id":"CHEBI:84443"}],"ecNumber":"2.1.1.114","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-demethylubiquinol + S-adenosyl-L-methionine = a ubiquinol + S-adenosyl-L-homocysteine + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:44380"},{"database":"Rhea","id":"RHEA-COMP:9566"},{"database":"Rhea","id":"RHEA-COMP:10914"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:17976"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:84422"}],"ecNumber":"2.1.1.64","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a 3-demethylubiquinone + S-adenosyl-L-methionine = a ubiquinone + S-adenosyl-L-homocysteine","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:81215"},{"database":"Rhea","id":"RHEA-COMP:9565"},{"database":"Rhea","id":"RHEA-COMP:19654"},{"database":"ChEBI","id":"CHEBI:16389"},{"database":"ChEBI","id":"CHEBI:57856"},{"database":"ChEBI","id":"CHEBI:59789"},{"database":"ChEBI","id":"CHEBI:231825"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Cofactor biosynthesis; ubiquinone biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Component of a multi-subunit COQ enzyme complex, composed of at least COQ3, COQ4, COQ5, COQ6, COQ7 and COQ9"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Mitochondrion inner membrane","id":"SL-0168"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Matrix side","id":"SL-9913"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"value":"Belongs to the class I-like SAM-binding methyltransferase superfamily. UbiG/COQ3 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150618.1"}],"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":21,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":42,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":86,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":114,"modifier":"EXACT"},"end":{"value":114,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":137,"modifier":"EXACT"},"end":{"value":137,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":183,"modifier":"EXACT"},"end":{"value":183,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:59789"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"S-adenosyl-L-methionine","id":"ChEBI:CHEBI:59789"}},{"type":"Binding site","location":{"start":{"value":184,"modifier":"EXACT"},"end":{"value":184,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":187,"modifier":"EXACT"},"end":{"value":187,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}},{"type":"Binding site","location":{"start":{"value":188,"modifier":"EXACT"},"end":{"value":188,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:18420"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"ligand":{"name":"Mg(2+)","id":"ChEBI:CHEBI:18420"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022603"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0999","category":"Cellular component","name":"Mitochondrion inner membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022691"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"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_03190"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022688"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03190"}],"id":"KW-0831","category":"Biological process","name":"Ubiquinone biosynthesis"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150618.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150618.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000009","properties":[{"key":"ProteinId","value":"KAJ4150618.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8UID9","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 4"}]},{"database":"GO","id":"GO:0031314","properties":[{"key":"GoTerm","value":"C:extrinsic component of mitochondrial inner membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0061542","properties":[{"key":"GoTerm","value":"F:3-demethylubiquinol 3-O-methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0010420","properties":[{"key":"GoTerm","value":"F:polyprenyldihydroxybenzoate methyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd02440","properties":[{"key":"EntryName","value":"AdoMet_MTases"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.150","properties":[{"key":"EntryName","value":"Vaccinia Virus protein VP39"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_00472","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR029063","properties":[{"key":"EntryName","value":"SAM-dependent_MTases_sf"}]},{"database":"InterPro","id":"IPR010233","properties":[{"key":"EntryName","value":"UbiG_MeTrfase"}]},{"database":"NCBIfam","id":"TIGR01983","properties":[{"key":"EntryName","value":"UbiG"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464","properties":[{"key":"EntryName","value":"METHYLTRANSFERASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43464:SF19","properties":[{"key":"EntryName","value":"UBIQUINONE BIOSYNTHESIS O-METHYLTRANSFERASE, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13489","properties":[{"key":"EntryName","value":"Methyltransf_23"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53335","properties":[{"key":"EntryName","value":"S-adenosyl-L-methionine-dependent methyltransferases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPRTPLRQPAARLGRCLCTTTRSQPRSVSTQLPASSQGRLPTQQRRWHSEFSSVNPNEVEHFNALAADWWSPHGSSRLLHLMNPLRHDFIRACLARDDIASNAQPTKLRYLDIGCGGGIFAESAARLPTTAHVTAIDPTPSVLAVAQAHAKRDPALRGKLDYQLTSIEKLAVPEKPYDIVSLFEVIEHIDDPGAFLDRVRPFVRPGGWLVMSTIARTWMSWFTTNLVAEDLLRIVPPGTHDWNKYINEEELRGFFAGKGWNSPKVMGVVYVPGLGWKEVQGSEKVGNYFFAVRRDE","length":296,"molWeight":33192,"crc64":"727541D293E03020","md5":"54BB503BE45E243A1FBDFED0D1089EDF"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Region":1,"Compositional bias":1,"Binding site":7},"uniParcId":"UPI00230ED70E"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8UIP0","uniProtkbId":"A0A9W8UIP0_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150963.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"ATP-dependent DNA helicase PIF1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"5.6.2.3"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA 5'-3' helicase PIF1"}},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA repair and recombination helicase PIF1"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"PIF1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150963.1"}],"value":"LMH87_011688"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"DNA-dependent ATPase and 5'-3' DNA helicase required for the maintenance of both mitochondrial and nuclear genome stability"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"ATP + H2O = ADP + phosphate + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:13065"},{"database":"ChEBI","id":"CHEBI:15377"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:43474"},{"database":"ChEBI","id":"CHEBI:456216"}],"ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00048954"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Couples ATP hydrolysis with the unwinding of duplex DNA at the replication fork by translocating in the 5'-3' direction.","ecNumber":"5.6.2.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00093875"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Monomer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004604"}],"value":"Nucleus, nucleolus","id":"SL-0188"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Nucleus","id":"SL-0191"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Mitochondrion","id":"SL-0173"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"value":"Belongs to the helicase family. PIF1 subfamily"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150963.1"}],"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":333,"modifier":"EXACT"},"end":{"value":628,"modifier":"EXACT"}},"description":"AAA+ ATPase","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM00382"}]},{"type":"DNA binding","location":{"start":{"value":741,"modifier":"EXACT"},"end":{"value":760,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}]},{"type":"Region","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":164,"modifier":"EXACT"},"end":{"value":316,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":58,"modifier":"EXACT"},"end":{"value":72,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":175,"modifier":"EXACT"},"end":{"value":189,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":198,"modifier":"EXACT"},"end":{"value":210,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Binding site","location":{"start":{"value":341,"modifier":"EXACT"},"end":{"value":348,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"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_03176"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023235"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03176"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150963.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4150963.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000009","properties":[{"key":"ProteinId","value":"KAJ4150963.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8UIP0","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 4"}]},{"database":"GO","id":"GO:0005739","properties":[{"key":"GoTerm","value":"C:mitochondrion"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0005730","properties":[{"key":"GoTerm","value":"C:nucleolus"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043139","properties":[{"key":"GoTerm","value":"F:5'-3' 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:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006281","properties":[{"key":"GoTerm","value":"P:DNA repair"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000723","properties":[{"key":"GoTerm","value":"P:telomere maintenance"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd18037","properties":[{"key":"EntryName","value":"DEXSc_Pif1_like"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd18809","properties":[{"key":"EntryName","value":"SF1_C_RecD"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:001226","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase PIF1"},{"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_03176","properties":[{"key":"EntryName","value":"PIF1"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR010285","properties":[{"key":"EntryName","value":"DNA_helicase_pif1-like_DEAD"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR049163","properties":[{"key":"EntryName","value":"Pif1-like_2B_dom"}]},{"database":"InterPro","id":"IPR051055","properties":[{"key":"EntryName","value":"PIF1_helicase"}]},{"database":"InterPro","id":"IPR048293","properties":[{"key":"EntryName","value":"PIF1_RRM3_pfh1"}]},{"database":"PANTHER","id":"PTHR47642","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR47642:SF5","properties":[{"key":"EntryName","value":"ATP-DEPENDENT DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05970","properties":[{"key":"EntryName","value":"PIF1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF21530","properties":[{"key":"EntryName","value":"Pif1_2B_dom"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF52540","properties":[{"key":"EntryName","value":"P-loop containing nucleoside triphosphate hydrolases"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MLAKANKSYEANQPPPSQRSSKGGELAKQLFPSSSPSQPPSDIRDQLKWRGPPRFLDSSPSTARASRPQCEQSGDKPTKDNGAASGGRAGKGSLASLYRNSSSSFQASVIDLTADDTTKTRQPEVFFVEDDFSDDDDLDLDFKVPLAVSPSKVTSISQFTAPKEKITPISRFAAPQSSEQAIPWSSSPASHFLPPQQPRNESTLSGSSNSLKRESPEADDDCFETPAPKKTKKRALPAAWRRDKALEEESLNAKPETPAEKAQARGLWDPSASAIKEQKKQLKNQRSTKQEVSEAEASADLPPPDPSTLPVQRSAAISLSSEQRHVLDLVVEQGQSVFFTGPAGTGKSVLMRAIISELKAKYARESERVAVTASTGLAACNIGGVTLHSFSGIGLGKEDASVLVKKVRRNPKAKNRWLKCKVLIIDEISMVDGDLFDKLSQIGRTIRNNGRPWGGIQLVITGDFFQLPPVPDDSKVAAKFAFDAATWTTSIEHTIGLTQVFRQRDPDFARMLNEMRLGKITDETVEAFKALERPLNFDDGVDSAELFPLRAQVEGSNEKRLRDLPGEIHRFGAADSGDPAIKERLLANMMAPKSIDLKLNAQVMLIKNLDASLVNGSLGRVIGFSDERTFEMGGGIPDDPTMDAAFNKARKKLSSFSRDSELISNSKKQFPVVQFVSASGMPRVILCQPEEWKVELPNGEVQAKRTQLPLILAWALSIHKAQGQTLERVTVNLSRVFEKGQAYVALSRATCQDGLRVIGFDRHKVMAHPKVVEFYGKLYSAAEAGTRRGPSSILDFVAARRGV","length":803,"molWeight":87693,"crc64":"8D51AEABF79CA137","md5":"ECF4360BB605BBFB0DDB64F27E4DA8F5"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"DNA binding":1,"Region":2,"Compositional bias":3,"Binding site":1},"uniParcId":"UPI00231540FE"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8UNP6","uniProtkbId":"A0A9W8UNP6_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4158184.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Lon protease homolog, mitochondrial"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"3.4.21.53"}]}},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"PIM1"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4158184.1"}],"value":"LMH87_008722"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"ATP-dependent serine protease that mediates the selective degradation of misfolded, unassembled or oxidatively damaged polypeptides as well as certain short-lived regulatory proteins in the mitochondrial matrix. May also have a chaperone function in the assembly of inner membrane protein complexes. Participates in the regulation of mitochondrial gene expression and in the maintenance of the integrity of the mitochondrial genome. Binds to mitochondrial DNA in a site-specific manner"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"Hydrolysis of proteins in presence of ATP.","ecNumber":"3.4.21.53","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Homohexamer or homoheptamer. Organized in a ring with a central cavity"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004305"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"value":"Mitochondrion matrix","id":"SL-0170"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU000591"}],"value":"Belongs to the peptidase S16 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4158184.1"}],"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":190,"modifier":"EXACT"},"end":{"value":467,"modifier":"EXACT"}},"description":"Lon N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51787"}]},{"type":"Domain","location":{"start":{"value":915,"modifier":"EXACT"},"end":{"value":1101,"modifier":"EXACT"}},"description":"Lon proteolytic","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51786"}]},{"type":"Region","location":{"start":{"value":78,"modifier":"EXACT"},"end":{"value":179,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":287,"modifier":"EXACT"},"end":{"value":330,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":837,"modifier":"EXACT"},"end":{"value":885,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":86,"modifier":"EXACT"},"end":{"value":95,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":99,"modifier":"EXACT"},"end":{"value":126,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":132,"modifier":"EXACT"},"end":{"value":146,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":150,"modifier":"EXACT"},"end":{"value":165,"modifier":"EXACT"}},"description":"Gly residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":166,"modifier":"EXACT"},"end":{"value":178,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":299,"modifier":"EXACT"},"end":{"value":310,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":841,"modifier":"EXACT"},"end":{"value":880,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":1007,"modifier":"EXACT"},"end":{"value":1007,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU10087"}]},{"type":"Active site","location":{"start":{"value":1050,"modifier":"EXACT"},"end":{"value":1050,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01122"}]},{"type":"Binding site","location":{"start":{"value":620,"modifier":"EXACT"},"end":{"value":627,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:30616"}],"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"ligand":{"name":"ATP","id":"ChEBI:CHEBI:30616"}}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023128"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0496","category":"Cellular component","name":"Mitochondrion"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022670"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0645","category":"Molecular function","name":"Protease"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022825"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03120"}],"id":"KW-0720","category":"Molecular function","name":"Serine protease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022946"}],"id":"KW-0809","category":"Domain","name":"Transit peptide"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4158184.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4158184.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000006","properties":[{"key":"ProteinId","value":"KAJ4158184.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8UNP6","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005759","properties":[{"key":"GoTerm","value":"C:mitochondrial matrix"},{"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:0016887","properties":[{"key":"GoTerm","value":"F:ATP hydrolysis activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004176","properties":[{"key":"GoTerm","value":"F:ATP-dependent peptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0043565","properties":[{"key":"GoTerm","value":"F:sequence-specific DNA binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0004252","properties":[{"key":"GoTerm","value":"F:serine-type endopeptidase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003697","properties":[{"key":"GoTerm","value":"F:single-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0034599","properties":[{"key":"GoTerm","value":"P:cellular response to oxidative stress"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0051131","properties":[{"key":"GoTerm","value":"P:chaperone-mediated protein complex assembly"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0141164","properties":[{"key":"GoTerm","value":"P:mitochondrial protein quality control"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-ARBA"}]},{"database":"GO","id":"GO:0007005","properties":[{"key":"GoTerm","value":"P:mitochondrion organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0070407","properties":[{"key":"GoTerm","value":"P:oxidation-dependent protein catabolic process"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0006508","properties":[{"key":"GoTerm","value":"P:proteolysis"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd19500","properties":[{"key":"EntryName","value":"RecA-like_Lon"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.300:FF:000021","properties":[{"key":"EntryName","value":"Lon protease homolog"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.8.60:FF:000113","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.5.5270:FF:000001","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.20.58.1480:FF:000003","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"2.30.130.40:FF:000006","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.230.10:FF:000015","properties":[{"key":"EntryName","value":"Lon protease homolog, mitochondrial"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.8.60","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.5.5270","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.20.58.1480","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.230.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.30.130.40","properties":[{"key":"EntryName","value":"LON domain-like"},{"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_03120","properties":[{"key":"EntryName","value":"lonm_euk"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR003593","properties":[{"key":"EntryName","value":"AAA+_ATPase"}]},{"database":"InterPro","id":"IPR003959","properties":[{"key":"EntryName","value":"ATPase_AAA_core"}]},{"database":"InterPro","id":"IPR004815","properties":[{"key":"EntryName","value":"Lon_bac/euk-typ"}]},{"database":"InterPro","id":"IPR054594","properties":[{"key":"EntryName","value":"Lon_lid"}]},{"database":"InterPro","id":"IPR008269","properties":[{"key":"EntryName","value":"Lon_proteolytic"}]},{"database":"InterPro","id":"IPR027065","properties":[{"key":"EntryName","value":"Lon_Prtase"}]},{"database":"InterPro","id":"IPR003111","properties":[{"key":"EntryName","value":"Lon_prtase_N"}]},{"database":"InterPro","id":"IPR046336","properties":[{"key":"EntryName","value":"Lon_prtase_N_sf"}]},{"database":"InterPro","id":"IPR027503","properties":[{"key":"EntryName","value":"Lonm_euk"}]},{"database":"InterPro","id":"IPR027417","properties":[{"key":"EntryName","value":"P-loop_NTPase"}]},{"database":"InterPro","id":"IPR008268","properties":[{"key":"EntryName","value":"Peptidase_S16_AS"}]},{"database":"InterPro","id":"IPR015947","properties":[{"key":"EntryName","value":"PUA-like_sf"}]},{"database":"InterPro","id":"IPR020568","properties":[{"key":"EntryName","value":"Ribosomal_Su5_D2-typ_SF"}]},{"database":"InterPro","id":"IPR014721","properties":[{"key":"EntryName","value":"Ribsml_uS5_D2-typ_fold_subgr"}]},{"database":"NCBIfam","id":"TIGR00763","properties":[{"key":"EntryName","value":"lon"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718","properties":[{"key":"EntryName","value":"LON PROTEASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43718:SF2","properties":[{"key":"EntryName","value":"LON PROTEASE HOMOLOG, MITOCHONDRIAL"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00004","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF05362","properties":[{"key":"EntryName","value":"Lon_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22667","properties":[{"key":"EntryName","value":"Lon_lid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02190","properties":[{"key":"EntryName","value":"LON_substr_bdg"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00830","properties":[{"key":"EntryName","value":"ENDOLAPTASE"}]},{"database":"SMART","id":"SM00382","properties":[{"key":"EntryName","value":"AAA"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00464","properties":[{"key":"EntryName","value":"LON"},{"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":"SSF88697","properties":[{"key":"EntryName","value":"PUA domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54211","properties":[{"key":"EntryName","value":"Ribosomal protein S5 domain 2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51787","properties":[{"key":"EntryName","value":"LON_N"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51786","properties":[{"key":"EntryName","value":"LON_PROTEOLYTIC"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS01046","properties":[{"key":"EntryName","value":"LON_SER"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MIPRSRVSGRLLIGRSAARTVPSSTSTRAVAGFPAVAHYTQQHACARRLQPAPACTAAQHRIPALYFSTSAFLGKEKDKPSKFFDPSAEPESTEPLSEEEVKANLENKKKEAISAEKAANESKDSDADATVSAKSDNSASQAQENKAGSSAGGAAGAGSGDGSGDGGKRGRKSSEKALQKPVVPDVYPQVLAIPIARRPLFPGFYKAITIKDPDVATAITESIKRGQPYVGAFLFKDENQDEDVIRNVEDVYDVGVFAQITSAFPIHGQEGALTAILYPHRRIKLSSLVPPTPQQQQQEAKKAETKKEPEVPEPIPAKPATEEAPATDKKGDVVASFEETAVDKKPDQVAEKYEPTSFLKKYPVSLVNVENLADEPYDPKSPVIRAVTNEIVNVFKEVATMNNLFRDQISTFSMSQSTGNVTSEPAKLADFAAAVSSGEQTELQEVLGCMNVEERMQKALIVLKKELMNAQLQSKITKDVESKISKRQREYWLMEQMKGIRRELGLESDGKDKLVEKFKEKAGKLAMPDAVRKVFDEEVNKLAHLETAASEFNVTRNYLDWLTQIPWGQRSAENFGIPNAIKVLDEDHYGLQDVKDRILEFIAVGKLRGSVEGKILCFVGPPGVGKTSIGKSIARALNREYYRFSVGGLTDVAEIKGHRRTYVGALPGRIIQALKKCQTENPLILIDEIDKIGRGYQGDPSSALLELLDPEQNNSFLDHYMDVPVDLSKVLFVCTANMTDTIPRPLLDRMELITLSGYVADEKKAIANKYLAPAAKEAAGLRDAKVDLTDEAIEELIKAYCRESGVRNLKKQIEKVYRKSALKIVQDLGEDAIPEEEALTEEGKEAAEESAKKAEEASESEGKEQPSTEATEKETTEKPRKALRVPDTVEVSINKSNLTDYIGPPVFTSDRLYEVSPAGVAMGLAWTQMGGAAMYIESILQSPLRQSTRPGMEITGNLKSVMKESTAIAYSFAKSFMATKFADNDFFDKAKMHLHVPDGAVPKDGPSAGITMATSLLSLALDAPVNPTVAMTGELTLTGKVLRIGGLREKTVAARRAGCTTIIFPKDCMSDWLELPAAIKEGIEGHPVEWYTQVFDLVFPDLDLAAANKSRVVKDGKKEGQDDE","length":1124,"molWeight":122776,"crc64":"0D7B7FD621A47D97","md5":"AC77CF81F8BD88EE40C77B2B982585E3"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":3,"Compositional bias":7,"Active site":2,"Binding site":1},"uniParcId":"UPI002311DC45"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8UTC2","uniProtkbId":"A0A9W8UTC2_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4164979.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00067568"}],"value":"Folic acid synthesis protein FOL1"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012458"}],"value":"2.5.1.15"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013253"}],"value":"2.7.6.3"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00013043"}],"value":"4.1.2.25"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00068111"}],"value":"Folic acid synthesis protein fol1"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4164979.1"}],"value":"LMH87_006631"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00058009"}],"value":"Catalyzes three sequential steps of tetrahydrofolate biosynthesis"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"(7,8-dihydropterin-6-yl)methyl diphosphate + 4-aminobenzoate = 7,8-dihydropteroate + diphosphate","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:19949"},{"database":"ChEBI","id":"CHEBI:17836"},{"database":"ChEBI","id":"CHEBI:17839"},{"database":"ChEBI","id":"CHEBI:33019"},{"database":"ChEBI","id":"CHEBI:72950"}],"ecNumber":"2.5.1.15","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000012"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"6-hydroxymethyl-7,8-dihydropterin + ATP = (7,8-dihydropterin-6-yl)methyl diphosphate + AMP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:11412"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:30616"},{"database":"ChEBI","id":"CHEBI:44841"},{"database":"ChEBI","id":"CHEBI:72950"},{"database":"ChEBI","id":"CHEBI:456215"}],"ecNumber":"2.7.6.3","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00000198"}]}},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"7,8-dihydroneopterin = 6-hydroxymethyl-7,8-dihydropterin + glycolaldehyde","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:10540"},{"database":"ChEBI","id":"CHEBI:17001"},{"database":"ChEBI","id":"CHEBI:17071"},{"database":"ChEBI","id":"CHEBI:44841"}],"ecNumber":"4.1.2.25","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001353"}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Mg(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001946"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:18420"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005013"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 3/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00005051"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate from 7,8-dihydroneopterin triphosphate: step 4/4"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004763"}],"value":"Cofactor biosynthesis; tetrahydrofolate biosynthesis; 7,8-dihydrofolate from 2-amino-4-hydroxy-6-hydroxymethyl-7,8-dihydropteridine diphosphate and 4-aminobenzoate: step 1/2"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009951"}],"value":"In the C-terminal section; belongs to the DHPS family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009640"}],"value":"In the N-terminal section; belongs to the DHNA family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00061548"}],"value":"In the central section; belongs to the HPPK family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4164979.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":258,"modifier":"EXACT"},"end":{"value":521,"modifier":"EXACT"}},"description":"Pterin-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50972"}]},{"type":"Region","location":{"start":{"value":42,"modifier":"EXACT"},"end":{"value":61,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022909"}],"id":"KW-0289","category":"Biological process","name":"Folate biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022777"}],"id":"KW-0418","category":"Molecular function","name":"Kinase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022842"}],"id":"KW-0460","category":"Ligand","name":"Magnesium"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023268"}],"id":"KW-0511","category":"Molecular function","name":"Multifunctional enzyme"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"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"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4164979.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4164979.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000001","properties":[{"key":"ProteinId","value":"KAJ4164979.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056059894.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056204547.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8UTC2","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80893790","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_006631","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 1"}]},{"database":"GO","id":"GO:0005740","properties":[{"key":"GoTerm","value":"C:mitochondrial envelope"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003848","properties":[{"key":"GoTerm","value":"F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004150","properties":[{"key":"GoTerm","value":"F:dihydroneopterin aldolase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0004156","properties":[{"key":"GoTerm","value":"F:dihydropteroate synthase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0046654","properties":[{"key":"GoTerm","value":"P:tetrahydrofolate biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00739","properties":[{"key":"EntryName","value":"DHPS"},{"key":"MatchStatus","value":"1"}]},{"database":"CDD","id":"cd00483","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.20.20.20:FF:000006","properties":[{"key":"EntryName","value":"Dihydropteroate synthase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.70.560","properties":[{"key":"EntryName","value":"7,8-Dihydro-6-hydroxymethylpterin-pyrophosphokinase HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.20.20.20","properties":[{"key":"EntryName","value":"Dihydropteroate synthase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR045031","properties":[{"key":"EntryName","value":"DHP_synth-like"}]},{"database":"InterPro","id":"IPR006390","properties":[{"key":"EntryName","value":"DHP_synth_dom"}]},{"database":"InterPro","id":"IPR011005","properties":[{"key":"EntryName","value":"Dihydropteroate_synth-like_sf"}]},{"database":"InterPro","id":"IPR000550","properties":[{"key":"EntryName","value":"Hppk"}]},{"database":"InterPro","id":"IPR035907","properties":[{"key":"EntryName","value":"Hppk_sf"}]},{"database":"InterPro","id":"IPR000489","properties":[{"key":"EntryName","value":"Pterin-binding_dom"}]},{"database":"NCBIfam","id":"TIGR01496","properties":[{"key":"EntryName","value":"DHPS"},{"key":"MatchStatus","value":"1"}]},{"database":"NCBIfam","id":"TIGR01498","properties":[{"key":"EntryName","value":"folK"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20941","properties":[{"key":"EntryName","value":"FOLATE SYNTHESIS PROTEINS"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR20941:SF1","properties":[{"key":"EntryName","value":"FOLIC ACID SYNTHESIS PROTEIN FOL1"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01288","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00809","properties":[{"key":"EntryName","value":"Pterin_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF55083","properties":[{"key":"EntryName","value":"6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase, HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF51717","properties":[{"key":"EntryName","value":"Dihydropteroate synthetase-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00792","properties":[{"key":"EntryName","value":"DHPS_1"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00793","properties":[{"key":"EntryName","value":"DHPS_2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS00794","properties":[{"key":"EntryName","value":"HPPK"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50972","properties":[{"key":"EntryName","value":"PTERIN_BINDING"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MNPRLSSTSLPRLAWPSACRAVHAGASRSLTSRANAGAALLPSTAARPRHASSKLHSLAPSRNNRRSYAGCGCRGAKSTTTAYIALGGNLGDRVAEIERACSEMDRRGIKVTRTSSLWETEPMYVTDQDRFLNGVCEVETELEPMALLDVLQSIEKDLGRRKLIDKGPRNIDLDILLYGDERISNDRLNVPHISIPEREFVLRPLSELIPSKSIDPSKPWKLVQDYLNDLPVGEPLSSVTRISATAAPLTPLTSTRKSRLMAILNLTPDSFSDGGKHAATDLSSTILDMVRDGATIIDVGGQSTAPGRPEVGADEEAARVLPAVELIRSMPGCGHVAVSVDTYRASVAAQAVARGADIINDVSAGQLDADMLPTVGRLGATICLMHMRGTPRTMNQLADYPDGVVPAVAAELRARVAAAEAAGIRRWRIMLDPGLGFAKTAAHNLELLRRLDELRAWPGLEGLPWLVGSSRKTFVGQATGIADPAARTWGTAATVAAAVHGGADVLRVHDVGQMAAAAAMSDAIWRV","length":527,"molWeight":56233,"crc64":"84A2DF55968E1329","md5":"2397B947D830FBC80416123E6EB3C254"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":3,"COFACTOR":1,"PATHWAY":3,"SIMILARITY":3,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1},"uniParcId":"UPI002326F6C2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q0Z6","uniProtkbId":"A0A9W8Q0Z6_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144308.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"value":"Double-strand break repair protein"}}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144308.1"}],"value":"LMH87_003198"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"value":"Core component of the MRN complex, which plays a central role in double-strand break (DSB) repair, DNA recombination, maintenance of telomere integrity and meiosis. The MRN complex is involved in the repair of DNA double-strand breaks (DSBs) via homologous recombination (HR), an error-free mechanism which primarily occurs during S and G2 phases. The complex (1) mediates the end resection of damaged DNA, which generates proper single-stranded DNA, a key initial steps in HR, and is (2) required for the recruitment of other repair factors and efficient activation of ATM and ATR upon DNA damage. Within the MRN complex, MRE11 possesses both single-strand endonuclease activity and double-strand-specific 3'-5' exonuclease activity. MRE11 first endonucleolytically cleaves the 5' strand at DNA DSB ends to prevent non-homologous end joining (NHEJ) and licence HR. It then generates a single-stranded DNA gap via 3' to 5' exonucleolytic degradation, which is required for single-strand invasion and recombination"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Mn(2+)","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00001936"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29035"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00064981"}],"value":"Component of the MRN complex composed of two heterodimers RAD50 and MRE11 associated with a single NBS1"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004286"}],"value":"Chromosome","id":"SL-0468"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00009028"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU003447"}],"value":"Belongs to the MRE11/RAD32 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144308.1"}],"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":290,"modifier":"EXACT"},"end":{"value":464,"modifier":"EXACT"}},"description":"Mre11 DNA-binding","evidences":[{"evidenceCode":"ECO:0000259","source":"SMART","id":"SM01347"}]},{"type":"Region","location":{"start":{"value":568,"modifier":"EXACT"},"end":{"value":708,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Coiled coil","location":{"start":{"value":319,"modifier":"EXACT"},"end":{"value":361,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}]},{"type":"Compositional bias","location":{"start":{"value":583,"modifier":"EXACT"},"end":{"value":595,"modifier":"EXACT"}},"description":"Basic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":611,"modifier":"EXACT"},"end":{"value":629,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":639,"modifier":"EXACT"},"end":{"value":666,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":667,"modifier":"EXACT"},"end":{"value":678,"modifier":"EXACT"}},"description":"Polar residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":684,"modifier":"EXACT"},"end":{"value":695,"modifier":"EXACT"}},"description":"Acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Active site","location":{"start":{"value":125,"modifier":"EXACT"},"end":{"value":125,"modifier":"EXACT"}},"description":"Proton donor","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRSR","id":"PIRSR000882-1"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022454"}],"id":"KW-0158","category":"Cellular component","name":"Chromosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"Coils"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022759"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0255","category":"Molecular function","name":"Endonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022839"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0269","category":"Molecular function","name":"Exonuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023211"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0464","category":"Ligand","name":"Manganese"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023254"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0469","category":"Biological process","name":"Meiosis"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022722"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0540","category":"Molecular function","name":"Nuclease"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR000882"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144308.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144308.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4144308.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056047978.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056203219.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q0Z6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80890357","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_003198","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0030870","properties":[{"key":"GoTerm","value":"C:Mre11 complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0035861","properties":[{"key":"GoTerm","value":"C:site of double-strand break"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0008296","properties":[{"key":"GoTerm","value":"F:3'-5'-DNA exonuclease activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0030145","properties":[{"key":"GoTerm","value":"F:manganese ion binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000014","properties":[{"key":"GoTerm","value":"F:single-stranded DNA endonuclease activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000724","properties":[{"key":"GoTerm","value":"P:double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006303","properties":[{"key":"GoTerm","value":"P:double-strand break repair via nonhomologous end joining"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042138","properties":[{"key":"GoTerm","value":"P:meiotic DNA double-strand break formation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0097552","properties":[{"key":"GoTerm","value":"P:mitochondrial double-strand break repair via homologous recombination"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007095","properties":[{"key":"GoTerm","value":"P:mitotic G2 DNA damage checkpoint signaling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0031573","properties":[{"key":"GoTerm","value":"P:mitotic intra-S DNA damage checkpoint signaling"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000723","properties":[{"key":"GoTerm","value":"P:telomere maintenance"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"CDD","id":"cd00840","properties":[{"key":"EntryName","value":"MPP_Mre11_N"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.60.21.10:FF:000011","properties":[{"key":"EntryName","value":"Double-strand break repair protein"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.60.21.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.110.110","properties":[{"key":"EntryName","value":"Mre11, capping domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR004843","properties":[{"key":"EntryName","value":"Calcineurin-like_PHP"}]},{"database":"InterPro","id":"IPR029052","properties":[{"key":"EntryName","value":"Metallo-depent_PP-like"}]},{"database":"InterPro","id":"IPR003701","properties":[{"key":"EntryName","value":"Mre11"}]},{"database":"InterPro","id":"IPR038487","properties":[{"key":"EntryName","value":"Mre11_capping_dom"}]},{"database":"InterPro","id":"IPR007281","properties":[{"key":"EntryName","value":"Mre11_DNA-bd"}]},{"database":"InterPro","id":"IPR041796","properties":[{"key":"EntryName","value":"Mre11_N"}]},{"database":"NCBIfam","id":"TIGR00583","properties":[{"key":"EntryName","value":"mre11"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10139","properties":[{"key":"EntryName","value":"DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10139:SF1","properties":[{"key":"EntryName","value":"DOUBLE-STRAND BREAK REPAIR PROTEIN MRE11"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00149","properties":[{"key":"EntryName","value":"Metallophos"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF04152","properties":[{"key":"EntryName","value":"Mre11_DNA_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF000882","properties":[{"key":"EntryName","value":"DSB_repair_MRE11"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM01347","properties":[{"key":"EntryName","value":"Mre11_DNA_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF56300","properties":[{"key":"EntryName","value":"Metallo-dependent phosphatases"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPGSTDAHTIRILVATDNHVGFEERDAIRKDDSWRTFDEILTVARTEDVDMVLLAGDLFHDNKPSRKSLYQVMRTLRQNCLGMKPCPLEFLSDAATVFEGAFPHVNYEDPDINISIPVFSIHGNHDDPSGDGNLCSLDLLQACGLLNYYGRVAEADNIEARPILLQKGETKLALFGLSNVRDERMFRTFRDHKVKWFKPSAETGDWFNLLAVHQNHHAHTATSYLPENVLPDWMNLIVWGHEHECLIDPTQNPETGFHVMQPGSSVATSLVPGEAVQKHVAIVSVTGKEFKMEKIPLKTVRPFVTREIILNQDKRFKGLDKKKDNRQEVTRRLMEVVEEMIEEASTEWEAIQTDQEALEERPLPLIRLKVEYTAPEGGLFECENPQRFSNRFVGKVANTNDVVYFYRKKTVQRKATADAPAEVMDTLGDDGDMVKVDSLVQDFLSAQSLKVLPQGPFSEAVNQFVAKDDKHAMELFVSEHLTGQVKQMLGLESDDEDLNSAMEIYRTRVEQQLDRGVKPVYGERRRVLRPKPATWDSDFDGNWEEEPDAWTYEPVSEVSFLAGSAPSRIADSLPNEDAAPAKTTRRAAATKKAPAKKTTTARGRGRKAPLVEEEEEEEDVLMESDEEPEPAPPPKRATRAAPAKKTAAAPKKAAATRTSTRAKPATQTTLNFSQSGTQAKGIEISDDEISDDDAFEPAPPVATRSRRR","length":708,"molWeight":79386,"crc64":"16A9E31DD20A821E","md5":"3691BAB22E603268D59FDD8B9E05A1BE"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":1,"Coiled coil":1,"Compositional bias":5,"Active site":1},"uniParcId":"UPI002321EFD9"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q1G6","uniProtkbId":"A0A9W8Q1G6_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144243.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Pre-mRNA-processing factor 19"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"2.3.2.27"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144243.1"}],"value":"LMH87_003133"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Ubiquitin-protein ligase which is mainly involved pre-mRNA splicing and DNA repair. Required for pre-mRNA splicing as component of the spliceosome"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.","ecNumber":"2.3.2.27","evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004906"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Protein modification; protein ubiquitination"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Homotetramer"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00006388"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"value":"Belongs to the WD repeat PRP19 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144243.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":70,"modifier":"EXACT"}},"description":"U-box","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS51698"}]},{"type":"Repeat","location":{"start":{"value":271,"modifier":"EXACT"},"end":{"value":312,"modifier":"EXACT"}},"description":"WD","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023110"}],"id":"KW-0413","category":"Molecular function","name":"Isomerase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022664"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0507","category":"Biological process","name":"mRNA processing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023187"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0508","category":"Biological process","name":"mRNA splicing"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022737"}],"id":"KW-0677","category":"Domain","name":"Repeat"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023110"}],"id":"KW-0697","category":"Molecular function","name":"Rotamase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022728"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0747","category":"Cellular component","name":"Spliceosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367101"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022786"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01034"}],"id":"KW-0833","category":"Biological process","name":"Ubl conjugation pathway"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022574"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00221"}],"id":"KW-0853","category":"Domain","name":"WD repeat"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144243.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144243.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4144243.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056047913.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056202461.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q1G6","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80890292","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_003133","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0005737","properties":[{"key":"GoTerm","value":"C:cytoplasm"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000974","properties":[{"key":"GoTerm","value":"C:Prp19 complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071006","properties":[{"key":"GoTerm","value":"C:U2-type catalytic step 1 spliceosome"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0000151","properties":[{"key":"GoTerm","value":"C:ubiquitin ligase complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0061630","properties":[{"key":"GoTerm","value":"F:ubiquitin protein ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000398","properties":[{"key":"GoTerm","value":"P:mRNA splicing, via spliceosome"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0070534","properties":[{"key":"GoTerm","value":"P:protein K63-linked ubiquitination"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"CDD","id":"cd16656","properties":[{"key":"EntryName","value":"RING-Ubox_PRP19"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.30.40.10:FF:000027","properties":[{"key":"EntryName","value":"Pre-mRNA-processing factor 19, putative"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.130.10.10","properties":[{"key":"EntryName","value":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.40.10","properties":[{"key":"EntryName","value":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR024977","properties":[{"key":"EntryName","value":"Apc4-like_WD40_dom"}]},{"database":"InterPro","id":"IPR060769","properties":[{"key":"EntryName","value":"EIF3B-like_beta-prop_sf"}]},{"database":"InterPro","id":"IPR038959","properties":[{"key":"EntryName","value":"Prp19"}]},{"database":"InterPro","id":"IPR013915","properties":[{"key":"EntryName","value":"Prp19_cc"}]},{"database":"InterPro","id":"IPR055340","properties":[{"key":"EntryName","value":"RING-Ubox_PRP19"}]},{"database":"InterPro","id":"IPR003613","properties":[{"key":"EntryName","value":"Ubox_domain"}]},{"database":"InterPro","id":"IPR015943","properties":[{"key":"EntryName","value":"WD40/YVTN_repeat-like_dom_sf"}]},{"database":"InterPro","id":"IPR001680","properties":[{"key":"EntryName","value":"WD40_rpt"}]},{"database":"InterPro","id":"IPR013083","properties":[{"key":"EntryName","value":"Znf_RING/FYVE/PHD"}]},{"database":"PANTHER","id":"PTHR43995","properties":[{"key":"EntryName","value":"PRE-MRNA-PROCESSING FACTOR 19"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR43995:SF1","properties":[{"key":"EntryName","value":"PRE-MRNA-PROCESSING FACTOR 19"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF12894","properties":[{"key":"EntryName","value":"ANAPC4_WD40"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08606","properties":[{"key":"EntryName","value":"Prp19"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00504","properties":[{"key":"EntryName","value":"Ubox"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00320","properties":[{"key":"EntryName","value":"WD40"},{"key":"MatchStatus","value":"4"}]},{"database":"SUPFAM","id":"SSF57850","properties":[{"key":"EntryName","value":"RING/U-box"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF69322","properties":[{"key":"EntryName","value":"Tricorn protease domain 2"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS51698","properties":[{"key":"EntryName","value":"U_BOX"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50082","properties":[{"key":"EntryName","value":"WD_REPEATS_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MLCGISGEAPQEPVASRKSGVIYEKRLIEQYINEHGTEPSTGEALTADDLLSINSSRIARPRPPTLTSIPALLATFQNEWDSLALETYNLREQLARTREELATSLYQHDAAVRVIARLTKERNEARDTLSRITVSGAGANSDEMVVDTEGLPDALAARVDEVHQELSKGRKKRPVPKDWVTPHEIAAFEVTATNALPVAQTTCLDTEGAYAAVGGLQGQGAIYAVAADSLEREIAVGEPATSTLWTGSKLIYGTGNGGLKVFEGGNQVAAASEHSGPTTGLSIHPSGDIVASVGTDKSLVLYDLTSNLKRVSRTFVDASLTTVSFHPDGHLVAAGTVTGDVKLYMTKTLEQAAVFKLGAPIQALTFSENGFWLAATAKGQNSVTIFDLRKEGDAATAKVLETGGAVQSLAWDYTGQYLATAGPSGLTIQQYAKGGKKWAEPFRNATGAVAVRWGESGKTLVAVNGDGVISVVGIKA","length":476,"molWeight":50281,"crc64":"24DF50C3E1AAD26E","md5":"3EAFBD790EC062B283FA774F5CE11D47"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":1,"PATHWAY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Repeat":1},"uniParcId":"UPI00230A8EAC"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q1H9","uniProtkbId":"A0A9W8Q1H9_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144410.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"E3 ubiquitin-protein ligase PEP5"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"2.3.2.27"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144410.1"}],"value":"LMH87_003294"}]}],"comments":[{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.","ecNumber":"2.3.2.27","evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Component of the homotypic vacuole fusion and vacuole protein sorting (HOPS) complex. Component of the class C core vacuole/endosome tethering (CORVET) complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029433"}],"value":"Endomembrane system","id":"SL-0147"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029433"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00029433"}],"value":"Cytoplasmic side","id":"SL-9910"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Vacuole membrane","id":"SL-0271"},"topology":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Peripheral membrane protein","id":"SL-9903"},"orientation":{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Cytoplasmic side","id":"SL-9910"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007070"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"value":"Belongs to the VPS11 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144410.1"}],"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":"Repeat","location":{"start":{"value":402,"modifier":"EXACT"},"end":{"value":550,"modifier":"EXACT"}},"description":"CHCR","evidences":[{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU01006"}]},{"type":"Domain","location":{"start":{"value":879,"modifier":"EXACT"},"end":{"value":917,"modifier":"EXACT"}},"description":"RING-type","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50089"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022723"}],"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022927"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0653","category":"Biological process","name":"Protein transport"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022448"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0813","category":"Biological process","name":"Transport"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0833","category":"Biological process","name":"Ubl conjugation pathway"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR007860"}],"id":"KW-0926","category":"Cellular component","name":"Vacuole"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022833"}],"id":"KW-0862","category":"Ligand","name":"Zinc"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022771"},{"evidenceCode":"ECO:0000256","source":"PROSITE-ProRule","id":"PRU00175"}],"id":"KW-0863","category":"Domain","name":"Zinc-finger"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144410.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144410.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4144410.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056048080.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056204340.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q1H9","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80890453","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_003294","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0033263","properties":[{"key":"GoTerm","value":"C:CORVET complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0000329","properties":[{"key":"GoTerm","value":"C:fungal-type vacuole membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030897","properties":[{"key":"GoTerm","value":"C:HOPS complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0030674","properties":[{"key":"GoTerm","value":"F:protein-macromolecule adaptor activity"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0061630","properties":[{"key":"GoTerm","value":"F:ubiquitin protein ligase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0007032","properties":[{"key":"GoTerm","value":"P:endosome organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0006886","properties":[{"key":"GoTerm","value":"P:intracellular protein transport"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0048284","properties":[{"key":"GoTerm","value":"P:organelle fusion"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0007033","properties":[{"key":"GoTerm","value":"P:vacuole organization"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0016192","properties":[{"key":"GoTerm","value":"P:vesicle-mediated transport"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd16688","properties":[{"key":"EntryName","value":"RING-H2_Vps11"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.25.40.10:FF:000440","properties":[{"key":"EntryName","value":"E3 ubiquitin-protein ligase PEP5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.25.40.10","properties":[{"key":"EntryName","value":"Tetratricopeptide repeat domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.130.10.10","properties":[{"key":"EntryName","value":"YVTN repeat-like/Quinoprotein amine dehydrogenase"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.30.40.10","properties":[{"key":"EntryName","value":"Zinc/RING finger domain, C3HC4 (zinc finger)"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR016024","properties":[{"key":"EntryName","value":"ARM-type_fold"}]},{"database":"InterPro","id":"IPR057308","properties":[{"key":"EntryName","value":"CHCR_PEP5_VPS11"}]},{"database":"InterPro","id":"IPR000547","properties":[{"key":"EntryName","value":"Clathrin_H-chain/VPS_repeat"}]},{"database":"InterPro","id":"IPR057307","properties":[{"key":"EntryName","value":"PEP5_VPS11_N"}]},{"database":"InterPro","id":"IPR011990","properties":[{"key":"EntryName","value":"TPR-like_helical_dom_sf"}]},{"database":"InterPro","id":"IPR016528","properties":[{"key":"EntryName","value":"VPS11"}]},{"database":"InterPro","id":"IPR024763","properties":[{"key":"EntryName","value":"VPS11_C"}]},{"database":"InterPro","id":"IPR015943","properties":[{"key":"EntryName","value":"WD40/YVTN_repeat-like_dom_sf"}]},{"database":"InterPro","id":"IPR036322","properties":[{"key":"EntryName","value":"WD40_repeat_dom_sf"}]},{"database":"InterPro","id":"IPR001841","properties":[{"key":"EntryName","value":"Znf_RING"}]},{"database":"InterPro","id":"IPR013083","properties":[{"key":"EntryName","value":"Znf_RING/FYVE/PHD"}]},{"database":"PANTHER","id":"PTHR23323","properties":[{"key":"EntryName","value":"VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR23323:SF24","properties":[{"key":"EntryName","value":"VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 11 HOMOLOG"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23341","properties":[{"key":"EntryName","value":"PEP5_VPS11_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF23356","properties":[{"key":"EntryName","value":"TPR_PEP5_VPS11"},{"key":"MatchStatus","value":"2"}]},{"database":"Pfam","id":"PF12451","properties":[{"key":"EntryName","value":"VPS11_C"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF17122","properties":[{"key":"EntryName","value":"zf-C3H2C3"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF007860","properties":[{"key":"EntryName","value":"VPS11"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF48371","properties":[{"key":"EntryName","value":"ARM repeat"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF57850","properties":[{"key":"EntryName","value":"RING/U-box"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF50978","properties":[{"key":"EntryName","value":"WD40 repeat-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50236","properties":[{"key":"EntryName","value":"CHCR"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50089","properties":[{"key":"EntryName","value":"ZF_RING_2"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MAISWKSFDFFDVSLVAPPEAEATQLFEGNDVSSVCAGSDSLFIGSGDGSVSILGKNWKVVNKFQAHDAGQVTQMRQVEGTSVLVTVAEDLSNEPVLKAWALDKLVKKTNMPTCLSTITISNGRRQFPISAFAALDDLSQIAVGFANGAVTVIRGDLIHDLGTKQRIVYESEEPVTGVQLMEDEKLTTLFVSTTSRILKLGLSKRGQGLPPKTVEDSGCAVGCMTLDPVTGDIVVARDDAIYTYNMDGRGPPKVYESPKKMIAVHQDYMALACPPASSYEPDSIRRRFTNGADGLFDSSTFVLLEPDLRIIAHTETLISPVKFIFEVWGDIFTVTEQGKAYRYHEKPLQQRLDMIYQRNMFPLALELARNSGMDNKEQSAIYRKFGDHLYQKADYDGSMNQYIRAIDTTEPSQVIRKFLDTQRIHNLIKYLEELHDHRKATADHTTLLLNCYAKLKDKEKLEKFIESPGDLKFDLDTAISMCRQGGYYEQAAYLAKKHGETELVVDILIEDSKNYAGALEYIWHQDPAIAYPCLRKYARVLIEHCPQQATKLFSDYYTGRYRPKRTPIAVVESAAHSSNTFTSGAASAVQNLSNLFALPYISPASVTGTPGSAMPTVEGLPLDEDDYPPPKYTPPEPRTAFSSFIDHADEFIVFLEACLEESNIRTSDQTDLYTTLFEMYLYKAGEKKGLRREEWEAKAKKLIEGEHVPMESSNVLLLSHLSNFKDGTVLVKEQAGLLSDIFRSYTSARDTQGAMKALRKYGPDEPQLYPAALAYLTSDPKILEEAGQDELAGILAKIDKDGLMAPLQVIQTLVGQSAGGGFATMGMVKPYLQETITRERRQISSNRHRIKTLRTDTEKRRVEIEELNSKPAIFQATRCTECGQGLDLPTVHFLCKHSFHERCLRSGTEEDAECPKCATNNDMIRKIRRGQQEEVDKHELFKSALDRSEDKFGTIAEWYSHGVMDASQNAEHVP","length":974,"molWeight":108853,"crc64":"F87A57BD27EA96A6","md5":"39E63E962654E0A9FD66237C7F2B8A54"},"extraAttributes":{"countByCommentType":{"CATALYTIC ACTIVITY":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Repeat":1,"Domain":1},"uniParcId":"UPI0023260F75"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q207","uniProtkbId":"A0A9W8Q207_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144680.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"Eukaryotic translation initiation factor 3 subunit A"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"eIF3a"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"Eukaryotic translation initiation factor 3 110 kDa subunit homolog"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"eIF3 p110"}]},{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"Translation initiation factor eIF3, p110 subunit homolog"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"TIF32"},"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144680.1"}],"value":"LMH87_003554"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"RNA-binding component of the eukaryotic translation initiation factor 3 (eIF-3) complex, which is involved in protein synthesis of a specialized repertoire of mRNAs and, together with other initiation factors, stimulates binding of mRNA and methionyl-tRNAi to the 40S ribosome. The eIF-3 complex specifically targets and initiates translation of a subset of mRNAs involved in cell proliferation"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"Component of the eukaryotic translation initiation factor 3 (eIF-3) complex"}],"commentType":"SUBUNIT"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004496"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"Cytoplasm","id":"SL-0086"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"value":"Belongs to the eIF-3 subunit A family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144680.1"}],"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":340,"modifier":"EXACT"},"end":{"value":524,"modifier":"EXACT"}},"description":"PCI","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50250"}]},{"type":"Region","location":{"start":{"value":617,"modifier":"EXACT"},"end":{"value":667,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Region","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":1061,"modifier":"EXACT"}},"description":"Disordered","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":617,"modifier":"EXACT"},"end":{"value":667,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":833,"modifier":"EXACT"},"end":{"value":911,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":941,"modifier":"EXACT"},"end":{"value":953,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":981,"modifier":"EXACT"},"end":{"value":992,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":999,"modifier":"EXACT"},"end":{"value":1009,"modifier":"EXACT"}},"description":"Pro residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":1031,"modifier":"EXACT"},"end":{"value":1043,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023054"}],"id":"KW-0175","category":"Domain","name":"Coiled coil"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022490"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"id":"KW-0963","category":"Cellular component","name":"Cytoplasm"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022540"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"id":"KW-0396","category":"Molecular function","name":"Initiation factor"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022917"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"id":"KW-0648","category":"Biological process","name":"Protein biosynthesis"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022884"},{"evidenceCode":"ECO:0000256","source":"HAMAP-Rule","id":"MF_03000"}],"id":"KW-0694","category":"Molecular function","name":"RNA-binding"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144680.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144680.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4144680.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q207","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0016282","properties":[{"key":"GoTerm","value":"C:eukaryotic 43S preinitiation complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0033290","properties":[{"key":"GoTerm","value":"C:eukaryotic 48S preinitiation complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0071540","properties":[{"key":"GoTerm","value":"C:eukaryotic translation initiation factor 3 complex, eIF3e"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0071541","properties":[{"key":"GoTerm","value":"C:eukaryotic translation initiation factor 3 complex, eIF3m"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0043614","properties":[{"key":"GoTerm","value":"C:multi-eIF complex"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003729","properties":[{"key":"GoTerm","value":"F:mRNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0003743","properties":[{"key":"GoTerm","value":"F:translation initiation factor activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0001732","properties":[{"key":"GoTerm","value":"P:formation of cytoplasmic translation initiation complex"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0002188","properties":[{"key":"GoTerm","value":"P:translation reinitiation"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"FunFam","id":"1.25.40.860:FF:000003","properties":[{"key":"EntryName","value":"Eukaryotic translation initiation factor 3 subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"4.10.860.10:FF:000001","properties":[{"key":"EntryName","value":"Eukaryotic translation initiation factor 3 subunit A"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.25.40.860","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"4.10.860.10","properties":[{"key":"EntryName","value":"UVR domain"},{"key":"MatchStatus","value":"1"}]},{"database":"HAMAP","id":"MF_03000","properties":[{"key":"EntryName","value":"eIF3a"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR027512","properties":[{"key":"EntryName","value":"EIF3A"}]},{"database":"InterPro","id":"IPR054711","properties":[{"key":"EntryName","value":"eIF3a_PCI_TPR-like"}]},{"database":"InterPro","id":"IPR000717","properties":[{"key":"EntryName","value":"PCI_dom"}]},{"database":"PANTHER","id":"PTHR14005:SF0","properties":[{"key":"EntryName","value":"EUKARYOTIC TRANSLATION INITIATION FACTOR 3 SUBUNIT A"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR14005","properties":[{"key":"EntryName","value":"EUKARYOTIC TRANSLATION INITIATION FACTOR 3, THETA SUBUNIT"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF22591","properties":[{"key":"EntryName","value":"eIF3a_PCI_TPR-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01399","properties":[{"key":"EntryName","value":"PCI"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00088","properties":[{"key":"EntryName","value":"PINT"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50250","properties":[{"key":"EntryName","value":"PCI"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MPPPPHQKPENVLKRAHELIGVGQPPAALTLLHEHITSKRSRNVPIASLEPVMLLLVELSVEQKKGKLAKDALYQYKNISQNTNIATIELVLKKFIQLAVEKVTAAQQKADEVQSSLEATTGGDSNVEDLEATETPESILLATVSGEQSRDRTDRAIVTPWLKFLWEAYRTVLDILRNNARLEILYQSTASQAFDFCLKYTRKTEFRRLCELLRNHVQTAAKYSSQMHAINLNDADTLQRHLETRFQQLNVAVELELWQEAFRSVEDIHTLLNLSKRPPKNVMMANYYEKLTRIFLVGENYLFHAAAWSRYYNLLRHSAVLVASGQGKKADNPPATEADLQKAASFVLLSALAIPVISTSRSRGAMIDFDEARKNKNSRLTHLLGMTQAPTRSRLFRDALSKSLLQRARPEIKELYNILEVDFHPLSICQKISPILSKIGADSEMERYILPLQQVILTRLFQQLSQVYDTVDLEFVQTLAQFPEPFQITRPTIEKFIMNGNKKGDLAIRMDHATGVLSFDSDIFSSSKAGHSGSAAGSAEADGGAVQRLQSTPSEIVRSQLTRLARSLFTTCHYIDPEFNKERLAARNAALSRAKAGAEKEHLAILARKDVIQKRKEEASEAQARKDKENARQKRLKEQALQEAEDKRLENDQREREARRMKEERDKVRRAEVEQQIKELKMDGKRLDINLDDIENLDTNRLREIKLSQLEREKHDVKEKLRVTGKRIDHLERAYRKEEGKKLAEDYEQQCEVDRAIYDKNTAKKLKDSEELHKANVELKNRLTRLVPIYESFRENLHERRRDEFEKRRRDAEKELEKQIALRKKEFRDRKLREKREREEKERELREAEERAAREKEEQRERDELRKAELTKLKEQRDKERQEMLEKAALQQRREDEALARRKAEKERPLRGAEPAPDSDARRPPVIGGGSWREREASKNAAAPPASAPAPAARTMERTDSQERPSAGGPPRLNLAGSKPSWRERQAAKEASGETSDSAPPPRNFPPRGAPIERGGSARGDAPPPRRTESQEPAAPEQPPSRAAGGGAGGKWVPPHLRNKA","length":1061,"molWeight":121101,"crc64":"0FF37C866C01C747","md5":"110824C08C23495626C754CF00E5B21E"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"SUBUNIT":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1,"Region":2,"Compositional bias":6},"uniParcId":"UPI002310952C"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q235","uniProtkbId":"A0A9W8Q235_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2023-11-08","entryVersion":12,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144725.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00021792"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"value":"ATP-dependent DNA helicase II subunit 2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00012551"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"value":"3.6.4.12"}]}},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144725.1"}],"value":"LMH87_003597"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"value":"Involved in non-homologous end joining (NHEJ) DNA double strand break repair"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00024890"}],"value":"Single-stranded DNA-dependent ATP-dependent helicase. Involved in non-homologous end joining (NHEJ) DNA double strand break repair. DNA-binding is sequence-independent but has a high affinity to nicks in double-stranded DNA and to the ends of duplex DNA. Binds to naturally occurring chromosomal ends, and therefore provides chromosomal end protection. Required also for telomere recombination to repair telomeric ends in the absence of telomerase. KU70, of the KU70/KU80 heterodimer, binds to the stem loop of TLC1, the RNA component of telomerase. Involved in telomere maintenance. Interacts with telomeric repeats and subtelomeric sequences thereby controlling telomere length and protecting against subtelomeric rearrangement. Maintains telomeric chromatin, which is involved in silencing the expression of genes located at the telomere. Required for mating-type switching"}],"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":"3.6.4.12","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00047995"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}]}},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004574"}],"value":"Chromosome, telomere","id":"SL-0276"}},{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004123"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"value":"Nucleus","id":"SL-0191"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00007726"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"value":"Belongs to the ku80 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144725.1"}],"value":"The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data"}],"commentType":"CAUTION"}],"features":[{"type":"Domain","location":{"start":{"value":6,"modifier":"EXACT"},"end":{"value":220,"modifier":"EXACT"}},"description":"VWFA","evidences":[{"evidenceCode":"ECO:0000259","source":"PROSITE","id":"PS50234"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022840"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0067","category":"Ligand","name":"ATP-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022454"}],"id":"KW-0158","category":"Cellular component","name":"Chromosome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022763"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0227","category":"Biological process","name":"DNA damage"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023172"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0233","category":"Biological process","name":"DNA recombination"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023204"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0234","category":"Biological process","name":"DNA repair"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023125"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0238","category":"Molecular function","name":"DNA-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022806"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0347","category":"Molecular function","name":"Helicase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022801"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0378","category":"Molecular function","name":"Hydrolase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022741"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0547","category":"Ligand","name":"Nucleotide-binding"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023242"},{"evidenceCode":"ECO:0000256","source":"PIRNR","id":"PIRNR016570"}],"id":"KW-0539","category":"Cellular component","name":"Nucleus"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022895"}],"id":"KW-0779","category":"Cellular component","name":"Telomere"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144725.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144725.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4144725.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056048395.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056194692.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q235","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80890756","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_003597","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0000781","properties":[{"key":"GoTerm","value":"C:chromosome, telomeric region"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0043564","properties":[{"key":"GoTerm","value":"C:Ku70:Ku80 complex"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0005524","properties":[{"key":"GoTerm","value":"F:ATP binding"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0003684","properties":[{"key":"GoTerm","value":"F:damaged DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0003678","properties":[{"key":"GoTerm","value":"F:DNA helicase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-EC"}]},{"database":"GO","id":"GO:0003690","properties":[{"key":"GoTerm","value":"F:double-stranded DNA binding"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0042162","properties":[{"key":"GoTerm","value":"F:telomeric repeat DNA binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006310","properties":[{"key":"GoTerm","value":"P:DNA recombination"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0006303","properties":[{"key":"GoTerm","value":"P:double-strand break repair via nonhomologous end joining"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0000723","properties":[{"key":"GoTerm","value":"P:telomere maintenance"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd00873","properties":[{"key":"EntryName","value":"KU80"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"3.40.50.410:FF:000073","properties":[{"key":"EntryName","value":"ATP-dependent DNA helicase II subunit 2"},{"key":"MatchStatus","value":"1"}]},{"database":"FunFam","id":"1.10.1600.10:FF:000002","properties":[{"key":"EntryName","value":"X-ray repair cross-complementing protein 5"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.10.1600.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"2.40.290.10","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"1.25.40.240","properties":[{"key":"EntryName","value":"Ku, C-terminal domain"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.410","properties":[{"key":"EntryName","value":"von Willebrand factor, type A domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR006164","properties":[{"key":"EntryName","value":"DNA_bd_Ku70/Ku80"}]},{"database":"InterPro","id":"IPR024193","properties":[{"key":"EntryName","value":"Ku80"}]},{"database":"InterPro","id":"IPR036494","properties":[{"key":"EntryName","value":"Ku_C_sf"}]},{"database":"InterPro","id":"IPR005161","properties":[{"key":"EntryName","value":"Ku_N"}]},{"database":"InterPro","id":"IPR014893","properties":[{"key":"EntryName","value":"Ku_PK_bind"}]},{"database":"InterPro","id":"IPR016194","properties":[{"key":"EntryName","value":"SPOC-like_C_dom_sf"}]},{"database":"InterPro","id":"IPR002035","properties":[{"key":"EntryName","value":"VWF_A"}]},{"database":"InterPro","id":"IPR036465","properties":[{"key":"EntryName","value":"vWFA_dom_sf"}]},{"database":"PANTHER","id":"PTHR12604","properties":[{"key":"EntryName","value":"KU AUTOANTIGEN DNA HELICASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR12604:SF4","properties":[{"key":"EntryName","value":"X-RAY REPAIR CROSS-COMPLEMENTING PROTEIN 5"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02735","properties":[{"key":"EntryName","value":"Ku"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF03731","properties":[{"key":"EntryName","value":"Ku_N"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF08785","properties":[{"key":"EntryName","value":"Ku_PK_bind"},{"key":"MatchStatus","value":"1"}]},{"database":"PIRSF","id":"PIRSF016570","properties":[{"key":"EntryName","value":"Ku80"},{"key":"MatchStatus","value":"1"}]},{"database":"SMART","id":"SM00559","properties":[{"key":"EntryName","value":"Ku78"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF101420","properties":[{"key":"EntryName","value":"C-terminal domain of Ku80"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF100939","properties":[{"key":"EntryName","value":"SPOC domain-like"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53300","properties":[{"key":"EntryName","value":"vWA-like"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50234","properties":[{"key":"EntryName","value":"VWFA"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MADKEATVFILDLGASMGKSHSGRKECDLDWSMRYVWDKITDIVSANRKTLCVGVVGLRTDGTINKLMDEDGYENISVLQELGPMTMTSLKTLQSSIKPSKTFAGDAISAIVVAVDMIDTFTKKLKWNRKIVMITDAQSGIDPDDIEDIAHKINDSNINLTVLGVDFDDPEYGFKEEDKSSTKAENEKTLKALASQCTDGVFASIVEAIDEIDTPRVKQVKPYKSYDGTLVLGDPEKFPSALTINVERYFKTHLARPIAASTVVLKSEQEGTQSTQTLDEEAMDGVEFSAVKQARTYKVNAPDAPGGKKDVEFESLAKGFEYGRTAVHITESEHNITKLETIKSFSIVGFIPWDKYEPFLSMGEVCVTHARKFDEKSELAMSSLVWGLNELESYAVARLVTKDGKDPTLVLLAPGLEPELECLYDIPLPFAEDVRAYRFPPLDQVITVTGQTLTTHRLLPTDELTEAMSDFVDSMDLDSYGIDDKGEPAEFAPVDETYNPIIHRINNAVKQRAVHSDKPIEDIPSVLLRYANPPQDLIDRVQDRIEDLIKEADVKKVPPKAKGRRNREAVKPISGLDVDALLGEDSKGQITPENAVPDFKRAMATSEEMSDIQDAAKQMADVIESLVTDSFGDSKYAQAVECIGVMREELINMEEPEMYNTFVRDLKKSLLSGSLGGDRRDFWFKLRWSRLGLIEQSQSDVSKVTADEADEFYKSR","length":716,"molWeight":79731,"crc64":"E130DF4709437D94","md5":"42BA6DAB6E01A0E019F6320E7D6FF823"},"extraAttributes":{"countByCommentType":{"FUNCTION":2,"CATALYTIC ACTIVITY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":1},"uniParcId":"UPI00231636A2"}},{"entryType":"UniProtKB unreviewed (TrEMBL)","primaryAccession":"A0A9W8Q261","uniProtkbId":"A0A9W8Q261_AKAMU","entryAudit":{"firstPublicDate":"2023-11-08","lastAnnotationUpdateDate":"2026-11-04","lastSequenceUpdateDate":"2023-11-08","entryVersion":13,"sequenceVersion":1},"annotationScore":3.0,"organism":{"scientificName":"Akanthomyces muscarius","commonName":"Entomopathogenic fungus","synonyms":["Lecanicillium muscarium"],"taxonId":2231603,"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144340.1"},{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Cordycipitaceae","Akanthomyces"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"Alpha-1,3/1,6-mannosyltransferase ALG2"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"2.4.1.132"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"2.4.1.257"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase"}}]},"genes":[{"orfNames":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144340.1"}],"value":"LMH87_003228"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00003142"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"Mannosylates Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate"}],"commentType":"FUNCTION"},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"a beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29515"},{"database":"Rhea","id":"RHEA-COMP:19511"},{"database":"Rhea","id":"RHEA-COMP:19513"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57527"},{"database":"ChEBI","id":"CHEBI:58189"},{"database":"ChEBI","id":"CHEBI:58472"},{"database":"ChEBI","id":"CHEBI:132510"}],"ecNumber":"2.4.1.132","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045103"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:29516"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045103"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}]}]},{"commentType":"CATALYTIC ACTIVITY","reaction":{"name":"an alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP-alpha-D-mannose = an alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-alpha-D-GlcNAc-diphospho-di-trans,poly-cis-dolichol + GDP + H(+)","reactionCrossReferences":[{"database":"Rhea","id":"RHEA:29519"},{"database":"Rhea","id":"RHEA-COMP:19513"},{"database":"Rhea","id":"RHEA-COMP:19515"},{"database":"ChEBI","id":"CHEBI:15378"},{"database":"ChEBI","id":"CHEBI:57527"},{"database":"ChEBI","id":"CHEBI:58189"},{"database":"ChEBI","id":"CHEBI:132510"},{"database":"ChEBI","id":"CHEBI:132511"}],"ecNumber":"2.4.1.257","evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045104"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}]},"physiologicalReactions":[{"directionType":"left-to-right","reactionCrossReference":{"database":"Rhea","id":"RHEA:29520"},"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00045104"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}]}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004922"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"Protein modification; protein glycosylation"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00004586"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"Endoplasmic reticulum membrane","id":"SL-0097"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"value":"Belongs to the glycosyltransferase group 1 family"}],"commentType":"SIMILARITY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144340.1"}],"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":82,"modifier":"EXACT"},"end":{"value":270,"modifier":"EXACT"}},"description":"Glycosyltransferase subfamily 4-like N-terminal","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF13439"}]},{"type":"Domain","location":{"start":{"value":381,"modifier":"EXACT"},"end":{"value":476,"modifier":"EXACT"}},"description":"Glycosyl transferase family 1","evidences":[{"evidenceCode":"ECO:0000259","source":"Pfam","id":"PF00534"}]},{"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":"Compositional bias","location":{"start":{"value":7,"modifier":"EXACT"},"end":{"value":25,"modifier":"EXACT"}},"description":"Low complexity","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]},{"type":"Compositional bias","location":{"start":{"value":31,"modifier":"EXACT"},"end":{"value":41,"modifier":"EXACT"}},"description":"Basic and acidic residues","evidences":[{"evidenceCode":"ECO:0000256","source":"SAM","id":"MobiDB-lite"}]}],"keywords":[{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022824"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"id":"KW-0256","category":"Cellular component","name":"Endoplasmic reticulum"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022676"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"id":"KW-0328","category":"Molecular function","name":"Glycosyltransferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00023136"}],"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"evidences":[{"evidenceCode":"ECO:0000313","source":"Proteomes","id":"UP001144673"}],"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022679"},{"evidenceCode":"ECO:0000256","source":"RuleBase","id":"RU367136"}],"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022692"}],"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"evidences":[{"evidenceCode":"ECO:0000256","source":"ARBA","id":"ARBA00022989"}],"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"CI-BB5318Q51BL3B","citationType":"journal article","authors":["Erdos Z.","Studholme D.J.","Raymond B.","Sharma M."],"title":"De-novo genome assembly for Akanthomyces muscarius, a biocontrol agent of insect agricultural pests.","publicationDate":"2023","journal":"Access Microbiol","firstPage":"0","lastPage":"0","volume":"0"},"referencePositions":["NUCLEOTIDE SEQUENCE"],"referenceComments":[{"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144340.1"}],"value":"Ve6","type":"STRAIN"}],"evidences":[{"evidenceCode":"ECO:0000313","source":"EMBL","id":"KAJ4144340.1"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"JAJHUN010000011","properties":[{"key":"ProteinId","value":"KAJ4144340.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_056048010.1","properties":[{"key":"NucleotideSequenceId","value":"XM_056203576.1"}]},{"database":"AlphaFoldDB","id":"A0A9W8Q261","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"80890387","properties":[{"key":"Description","value":"-"}]},{"database":"KEGG","id":"amus:LMH87_003228","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP001144673","properties":[{"key":"Component","value":"Chromosome 2"}]},{"database":"GO","id":"GO:0005789","properties":[{"key":"GoTerm","value":"C:endoplasmic reticulum membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"GO","id":"GO:0004378","properties":[{"key":"GoTerm","value":"F:GDP-Man:Man(1)GlcNAc(2)-PP-Dol alpha-1,3-mannosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0102704","properties":[{"key":"GoTerm","value":"F:GDP-Man:Man(2)GlcNAc(2)-PP-Dol alpha-1,6-mannosyltransferase activity"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-UniRule"}]},{"database":"GO","id":"GO:0009101","properties":[{"key":"GoTerm","value":"P:glycoprotein biosynthetic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"CDD","id":"cd03805","properties":[{"key":"EntryName","value":"GT4_ALG2-like"},{"key":"MatchStatus","value":"1"}]},{"database":"Gene3D","id":"3.40.50.2000","properties":[{"key":"EntryName","value":"Glycogen Phosphorylase B"},{"key":"MatchStatus","value":"2"}]},{"database":"InterPro","id":"IPR027054","properties":[{"key":"EntryName","value":"ALG2"}]},{"database":"InterPro","id":"IPR001296","properties":[{"key":"EntryName","value":"Glyco_trans_1"}]},{"database":"InterPro","id":"IPR028098","properties":[{"key":"EntryName","value":"Glyco_trans_4-like_N"}]},{"database":"PANTHER","id":"PTHR45918","properties":[{"key":"EntryName","value":"ALPHA-1,3/1,6-MANNOSYLTRANSFERASE ALG2"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR45918:SF1","properties":[{"key":"EntryName","value":"ALPHA-1,3_1,6-MANNOSYLTRANSFERASE ALG2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF13439","properties":[{"key":"EntryName","value":"Glyco_transf_4"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF00534","properties":[{"key":"EntryName","value":"Glycos_transf_1"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF53756","properties":[{"key":"EntryName","value":"UDP-Glycosyltransferase/glycogen phosphorylase"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MEEDQTPQRQQQQPRRAANPFAQQQPKRKMGPMERAARKSLREDYARRQAENAERLLREPLPKYVPKPVSGCHVFFHPDLGIGGAERLVVDAAVGLQEKGAKVVVYTNHCDPNHCFDECRNGTLDVRVKGSWLVPRSFFGRFTILCAILRQIHLMLHIWITGELEDLSPSIFIVDQLSAGLPWLRLLVSPKTGIVFYCHFPDLLLVQGRHASLLKRLYRIPFDRLEEWSMSFADAVALNSNFTKSVVQLTWPELLEKTTARVIYPCVDTAAKEDELLVGAGDAAPPPLFPSGDVRVLLSINRFERKKDIGLAIRAFASIPDDERRGVRLVLAGGYDRRVAENVEYHRELQSLANEFDLAHDTIDAADNPTARRPADTAAPVLFLLSVPADLKTALLRAATLLVYTPSNEHFGIVPLEAMLARVPVLAANTGGPTETVVEGETGWLRDPYEPLAWSAVMRRALALPAAEAARMGDEGSRRVKDTFGRDHMATTLMNVVREIVVARRNSDADNTMIIVVVGTVFSLSLAAMSLGIALWMMHDMKKNAALREGAAGVGRMF","length":558,"molWeight":62035,"crc64":"88295651259C7685","md5":"8BC2AD67CB4589BABEA151C9156D85D1"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"CATALYTIC ACTIVITY":2,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1,"CAUTION":1},"countByFeatureType":{"Domain":2,"Region":1,"Compositional bias":2},"uniParcId":"UPI00230DAEF9"}}]}