{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"A0A1B5L6A5","uniProtkbId":"USTE_USTVR","entryAudit":{"firstPublicDate":"2020-02-26","lastAnnotationUpdateDate":"2026-09-02","lastSequenceUpdateDate":"2016-11-02","entryVersion":25,"sequenceVersion":1},"annotationScore":2.0,"organism":{"scientificName":"Ustilaginoidea virens","commonName":"Rice false smut fungus","synonyms":["Villosiclava virens"],"taxonId":1159556,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Sordariomycetes","Hypocreomycetidae","Hypocreales","Clavicipitaceae","Ustilaginoidea"]},"proteinExistence":"3: Inferred from homology","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31050129"}],"value":"Probable O-methyltransferase ustE"},"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"2.1.1.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31050129"}],"value":"Ustilaginoidins biosynthesis cluster protein E"}}]},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"31050129"}],"value":"ustE"},"orfNames":[{"value":"UVI_02036190"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"31050129"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31050129"}],"value":"Probable O-methyltransferase; part of the gene cluster that mediates the biosynthesis of ustilaginoidins, dimeric gamma-naphthopyrones isolated from different fungal species (PubMed:31050129). The first step in the biosynthesis of ustilaginoidins is the production of gamma-naphthopyrone precursor YWA1 by the non-reducing polyketide synthase ustP, via condensation of one acetyl-CoA starter unit with 6 malonyl-CoA units (PubMed:31050129). YWA1 is then probably substrate of the ustZ to yield norrubrofusarin via a dehydration reaction (Probable). A key enzyme in the biosynthetic pathway is the laccase ustL, which catalyzes the oxidative dimerization of norrubrofusarin to ustilaginoidin A (PubMed:31050129). It can produce the M- and P-atropisomers in varying amounts, depending on the reaction conditions (PubMed:31050129). For the biosynthesis of 3-methylustilaginoid in derivatives such as chaetochromin A, a methylated derivative of YWA1 is required (Probable). The C-methylation is considered to be catalyzed by ustM, the phosphopantetheine attachment site of which indicates that it acts on the growing polyketide chain before release of the product (Probable). For the biosynthesis of chaetochromin A, it is assumed that saturation of the D2 double bond takes place before dimerization, and is probably catalyzed by an external reductase because no candidate gene was identified within the cluster (Probable)"}],"commentType":"FUNCTION"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305","source":"PubMed","id":"31050129"}],"value":"Secondary metabolite biosynthesis"}],"commentType":"PATHWAY"},{"commentType":"SUBCELLULAR LOCATION","subcellularLocations":[{"location":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Membrane","id":"SL-0162"},"topology":{"evidences":[{"evidenceCode":"ECO:0000255"}],"value":"Multi-pass membrane protein","id":"SL-9909"}}]},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the class VI-like SAM-binding methyltransferase superfamily. Isoprenylcysteine carboxyl methyltransferase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Chain","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":284,"modifier":"EXACT"}},"description":"Probable O-methyltransferase ustE","featureId":"PRO_0000448925"},{"type":"Transmembrane","location":{"start":{"value":88,"modifier":"EXACT"},"end":{"value":108,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":157,"modifier":"EXACT"},"end":{"value":177,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Transmembrane","location":{"start":{"value":215,"modifier":"EXACT"},"end":{"value":235,"modifier":"EXACT"}},"description":"Helical","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Glycosylation","location":{"start":{"value":22,"modifier":"EXACT"},"end":{"value":22,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00498"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":29,"modifier":"EXACT"},"end":{"value":29,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00498"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":205,"modifier":"EXACT"},"end":{"value":205,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00498"}],"featureId":""},{"type":"Glycosylation","location":{"start":{"value":264,"modifier":"EXACT"},"end":{"value":264,"modifier":"EXACT"}},"description":"N-linked (GlcNAc...) asparagine","evidences":[{"evidenceCode":"ECO:0000255","source":"PROSITE-ProRule","id":"PRU00498"}],"featureId":""}],"keywords":[{"id":"KW-0325","category":"PTM","name":"Glycoprotein"},{"id":"KW-0472","category":"Cellular component","name":"Membrane"},{"id":"KW-0489","category":"Molecular function","name":"Methyltransferase"},{"id":"KW-0949","category":"Ligand","name":"S-adenosyl-L-methionine"},{"id":"KW-0808","category":"Molecular function","name":"Transferase"},{"id":"KW-0812","category":"Domain","name":"Transmembrane"},{"id":"KW-1133","category":"Domain","name":"Transmembrane helix"}],"references":[{"referenceNumber":1,"citation":{"id":"27151791","citationType":"journal article","authors":["Kumagai T.","Ishii T.","Terai G.","Umemura M.","Machida M.","Asai K."],"citationCrossReferences":[{"database":"PubMed","id":"27151791"},{"database":"DOI","id":"10.1128/genomea.00306-16"}],"title":"Genome sequence of Ustilaginoidea virens IPU010, a rice pathogenic fungus causing false smut.","publicationDate":"2016","journal":"Genome Announc.","firstPage":"0","lastPage":"0","volume":"4"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"IPU010","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"31050129","citationType":"journal article","authors":["Obermaier S.","Thiele W.","Fuertges L.","Mueller M."],"citationCrossReferences":[{"database":"PubMed","id":"31050129"},{"database":"DOI","id":"10.1002/anie.201903759"}],"title":"Enantioselective phenol coupling by laccases in the biosynthesis of fungal dimeric naphthopyrones.","publicationDate":"2019","journal":"Angew. 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Ed.","firstPage":"9125","lastPage":"9128","volume":"58"},"referencePositions":["FUNCTION","PATHWAY"],"referenceComments":[{"value":"IPU010","type":"STRAIN"}]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"BBTG02000019","properties":[{"key":"ProteinId","value":"GAO19109.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"AlphaFoldDB","id":"A0A1B5L6A5","properties":[{"key":"Description","value":"-"}]},{"database":"GlyCosmos","id":"A0A1B5L6A5","properties":[{"key":"glycosylation","value":"4 sites, No reported glycans"}]},{"database":"GO","id":"GO:0016020","properties":[{"key":"GoTerm","value":"C:membrane"},{"key":"GoEvidenceType","value":"IEA:UniProtKB-SubCell"}]},{"database":"Gene3D","id":"1.20.120.1630","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR010721","properties":[{"key":"EntryName","value":"UstE-like"}]},{"database":"PANTHER","id":"PTHR32251","properties":[{"key":"EntryName","value":"3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR32251:SF15","properties":[{"key":"EntryName","value":"3-OXO-5-ALPHA-STEROID 4-DEHYDROGENASE (DUF1295)"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF06966","properties":[{"key":"EntryName","value":"DUF1295"},{"key":"MatchStatus","value":"1"}]},{"database":"PROSITE","id":"PS50244","properties":[{"key":"EntryName","value":"S5A_REDUCTASE"},{"key":"MatchStatus","value":"1"}]}],"sequence":{"value":"MADAKAVAKAELKSKDFVPRGNKSSSPLNTTLYLGLRALDCYIQYLILSRATGSFIIKFFGGSIIPHGPPVEAGFMHIEKLGLSGYRLLLLFMDILAAAKHFWFVLTVAEEAWTLTGAIVVGLDNIFFDTLNNLLFLCAATSAASSKAGGETLANPYLATGFIIFAVGLVTECVCEIDRKVFKKNPMNKGKPYTGGLFSLVRHPNYTAFTIWRSGLALASGGMIYGMSIAMFFMWDFSNRAVPALDEYCTKRVSYGPRDSTSTNWSRIWLLMTSSLVRRYVGRV","length":284,"molWeight":31284,"crc64":"ABE3E94CBCAD10BE","md5":"2D92BBC382ECF2ACC02CB31DE7257B91"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"PATHWAY":1,"SUBCELLULAR LOCATION":1,"SIMILARITY":1},"countByFeatureType":{"Chain":1,"Transmembrane":3,"Glycosylation":4},"uniParcId":"UPI000616934A"}}