{"entryType":"UniProtKB reviewed (Swiss-Prot)","primaryAccession":"W7E8S5","uniProtkbId":"VICK1_BIPV3","entryAudit":{"firstPublicDate":"2023-06-28","lastAnnotationUpdateDate":"2026-06-10","lastSequenceUpdateDate":"2014-04-16","entryVersion":36,"sequenceVersion":1},"annotationScore":4.0,"organism":{"scientificName":"Bipolaris victoriae (strain FI3)","commonName":"Victoria blight of oats agent","synonyms":["Cochliobolus victoriae"],"taxonId":930091,"lineage":["Eukaryota","Fungi","Dikarya","Ascomycota","Pezizomycotina","Dothideomycetes","Pleosporomycetidae","Pleosporales","Pleosporineae","Pleosporaceae","Bipolaris"]},"proteinExistence":"1: Evidence at protein level","proteinDescription":{"recommendedName":{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32929037"}],"value":"Copper amine oxidase vicK1"},"shortNames":[{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32929037"}],"value":"CAO vicK1"}],"ecNumbers":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929037"}],"value":"1.4.3.-"}]},"alternativeNames":[{"fullName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32929037"}],"value":"Victorin biosynthesis cluster protein K1"}}],"flag":"Precursor"},"genes":[{"geneName":{"evidences":[{"evidenceCode":"ECO:0000303","source":"PubMed","id":"32929037"}],"value":"VicK1"},"orfNames":[{"value":"COCVIDRAFT_21377"}]}],"comments":[{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929037"},{"evidenceCode":"ECO:0000305","source":"PubMed","id":"32929037"}],"value":"Copper amine oxidase, part of the gene cluster that mediates the biosynthesis of the secondary metabolite victorin, the molecular basis for Victoria blight of oats (PubMed:32929037). Within the pathway, vicK1 catalyzes the oxidative deamination of the N-terminal glycyl moiety of the hexapeptides in order to produce the active glyoxylate form victorins (PubMed:32929037). The pathway starts with the processing of the precursor vicA1 by several endopeptidases including kexin proteases as well as the cluster-specific S28 family peptidases vicPa and vicPb to produce 7 identical copies of the hexapeptide Gly-Leu-Lys-Leu-Ala-Phe. After being excised from the precursor peptide, the core peptides are cyclized and modified post-translationally by enzymes encoded within the gene cluster. The ustYa family oxidase vicYb is required for the formation of the macrocycle in victorin and the copper amine oxidases (CAOs) vicK1 and vicK2 are responsible for converting victorin to the active form by oxidizing the N-terminal glycyl residue in the peptides to glyoxylate. Relaxed substrate specificity of enzymes in the victorin biosynthetic pathway results in a metabolic grid that produces a set of analogs including victorinines B, C, E or HV-toxin M (Probable)"}],"commentType":"FUNCTION"},{"commentType":"COFACTOR","cofactors":[{"name":"Cu cation","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:23378"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"value":"Binds 1 copper ion per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"Ca(2+)","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:29108"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"value":"Binds 2 calcium ions per subunit."}]}},{"commentType":"COFACTOR","cofactors":[{"name":"L-topaquinone residue","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"cofactorCrossReference":{"database":"ChEBI","id":"CHEBI:79027"}}],"note":{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"value":"Contains 1 topaquinone per subunit."}]}},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929037"}],"value":"Mycotoxin biosynthesis"}],"commentType":"PATHWAY"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"value":"Homodimer; disulfide-linked"}],"commentType":"SUBUNIT"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12807"}],"value":"Topaquinone (TPQ) is generated by copper-dependent autoxidation of a specific tyrosyl residue"}],"commentType":"PTM"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000269","source":"PubMed","id":"32929037"}],"value":"Leads to the accumu-lation of new glycine-containing victorin derivatives"}],"commentType":"DISRUPTION PHENOTYPE"},{"texts":[{"evidences":[{"evidenceCode":"ECO:0000305"}],"value":"Belongs to the copper/topaquinone oxidase family"}],"commentType":"SIMILARITY"}],"features":[{"type":"Signal","location":{"start":{"value":1,"modifier":"EXACT"},"end":{"value":20,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000255"}]},{"type":"Chain","location":{"start":{"value":21,"modifier":"EXACT"},"end":{"value":709,"modifier":"EXACT"}},"description":"Copper amine oxidase vicK1","featureId":"PRO_5004891358"},{"type":"Active site","location":{"start":{"value":365,"modifier":"EXACT"},"end":{"value":365,"modifier":"EXACT"}},"description":"Proton acceptor","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}]},{"type":"Active site","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"Schiff-base intermediate with substrate; via topaquinone","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}]},{"type":"Binding site","location":{"start":{"value":496,"modifier":"EXACT"},"end":{"value":496,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:23378"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Cu cation","id":"ChEBI:CHEBI:23378"}},{"type":"Binding site","location":{"start":{"value":498,"modifier":"EXACT"},"end":{"value":498,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:23378"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Cu cation","id":"ChEBI:CHEBI:23378"}},{"type":"Binding site","location":{"start":{"value":505,"modifier":"EXACT"},"end":{"value":505,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":506,"modifier":"EXACT"},"end":{"value":506,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":507,"modifier":"EXACT"},"end":{"value":507,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":548,"modifier":"EXACT"},"end":{"value":548,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":641,"modifier":"EXACT"},"end":{"value":641,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":645,"modifier":"EXACT"},"end":{"value":645,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"2"}},{"type":"Binding site","location":{"start":{"value":651,"modifier":"EXACT"},"end":{"value":651,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":652,"modifier":"EXACT"},"end":{"value":652,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:29108"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Ca(2+)","id":"ChEBI:CHEBI:29108","label":"1"}},{"type":"Binding site","location":{"start":{"value":662,"modifier":"EXACT"},"end":{"value":662,"modifier":"EXACT"}},"description":"","featureCrossReferences":[{"database":"ChEBI","id":"CHEBI:23378"}],"evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}],"ligand":{"name":"Cu cation","id":"ChEBI:CHEBI:23378"}},{"type":"Modified residue","location":{"start":{"value":448,"modifier":"EXACT"},"end":{"value":448,"modifier":"EXACT"}},"description":"2',4',5'-topaquinone","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P12807"}]},{"type":"Disulfide bond","location":{"start":{"value":383,"modifier":"EXACT"},"end":{"value":408,"modifier":"EXACT"}},"description":"","evidences":[{"evidenceCode":"ECO:0000250","source":"UniProtKB","id":"P19801"}]}],"keywords":[{"id":"KW-0106","category":"Ligand","name":"Calcium"},{"id":"KW-0186","category":"Ligand","name":"Copper"},{"id":"KW-1015","category":"PTM","name":"Disulfide bond"},{"id":"KW-0479","category":"Ligand","name":"Metal-binding"},{"id":"KW-0560","category":"Molecular function","name":"Oxidoreductase"},{"id":"KW-1185","category":"Technical term","name":"Reference proteome"},{"id":"KW-0732","category":"Domain","name":"Signal"},{"id":"KW-0801","category":"PTM","name":"TPQ"}],"references":[{"referenceNumber":1,"citation":{"id":"23357949","citationType":"journal article","authors":["Condon B.J.","Leng Y.","Wu D.","Bushley K.E.","Ohm R.A.","Otillar R.","Martin J.","Schackwitz W.","Grimwood J.","MohdZainudin N.","Xue C.","Wang R.","Manning V.A.","Dhillon B.","Tu Z.J.","Steffenson B.J.","Salamov A.","Sun H.","Lowry S.","LaButti K.","Han J.","Copeland A.","Lindquist E.","Barry K.","Schmutz J.","Baker S.E.","Ciuffetti L.M.","Grigoriev I.V.","Zhong S.","Turgeon B.G."],"citationCrossReferences":[{"database":"PubMed","id":"23357949"},{"database":"DOI","id":"10.1371/journal.pgen.1003233"}],"title":"Comparative genome structure, secondary metabolite, and effector coding capacity across Cochliobolus pathogens.","publicationDate":"2013","journal":"PLoS Genet.","firstPage":"E1003233","lastPage":"E1003233","volume":"9"},"referencePositions":["NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]"],"referenceComments":[{"value":"FI3","type":"STRAIN"}]},{"referenceNumber":2,"citation":{"id":"32929037","citationType":"journal article","authors":["Kessler S.C.","Zhang X.","McDonald M.C.","Gilchrist C.L.M.","Lin Z.","Rightmyer A.","Solomon P.S.","Turgeon B.G.","Chooi Y.H."],"citationCrossReferences":[{"database":"PubMed","id":"32929037"},{"database":"DOI","id":"10.1073/pnas.2010573117"}],"title":"Victorin, the host-selective cyclic peptide toxin from the oat pathogen Cochliobolus victoriae, is ribosomally encoded.","publicationDate":"2020","journal":"Proc. Natl. Acad. Sci. U.S.A.","firstPage":"24243","lastPage":"24250","volume":"117"},"referencePositions":["FUNCTION","DISRUPTION PHENOTYPE","CATALYTIC ACTIVITY","PATHWAY"]}],"uniProtKBCrossReferences":[{"database":"EMBL","id":"KI969034","properties":[{"key":"ProteinId","value":"EUN20452.1"},{"key":"Status","value":"-"},{"key":"MoleculeType","value":"Genomic_DNA"}]},{"database":"RefSeq","id":"XP_014550026.1","properties":[{"key":"NucleotideSequenceId","value":"XM_014694540.1"}]},{"database":"AlphaFoldDB","id":"W7E8S5","properties":[{"key":"Description","value":"-"}]},{"database":"SMR","id":"W7E8S5","properties":[{"key":"Description","value":"-"}]},{"database":"GeneID","id":"26252699","properties":[{"key":"Description","value":"-"}]},{"database":"HOGENOM","id":"CLU_015739_0_0_1","properties":[{"key":"Description","value":"-"}]},{"database":"OrthoDB","id":"5859at28556","properties":[{"key":"Description","value":"-"}]},{"database":"Proteomes","id":"UP000054337","properties":[{"key":"Component","value":"Unassembled WGS sequence"}]},{"database":"GO","id":"GO:0005886","properties":[{"key":"GoTerm","value":"C:plasma membrane"},{"key":"GoEvidenceType","value":"IEA:TreeGrafter"}]},{"database":"GO","id":"GO:0005507","properties":[{"key":"GoTerm","value":"F:copper ion binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0008131","properties":[{"key":"GoTerm","value":"F:primary methylamine oxidase activity"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0048038","properties":[{"key":"GoTerm","value":"F:quinone binding"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"GO","id":"GO:0009308","properties":[{"key":"GoTerm","value":"P:amine metabolic process"},{"key":"GoEvidenceType","value":"IEA:InterPro"}]},{"database":"Gene3D","id":"3.10.450.40","properties":[{"key":"EntryName","value":"-"},{"key":"MatchStatus","value":"2"}]},{"database":"Gene3D","id":"2.70.98.20","properties":[{"key":"EntryName","value":"Copper amine oxidase, catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"InterPro","id":"IPR000269","properties":[{"key":"EntryName","value":"Cu_amine_oxidase"}]},{"database":"InterPro","id":"IPR015798","properties":[{"key":"EntryName","value":"Cu_amine_oxidase_C"}]},{"database":"InterPro","id":"IPR036460","properties":[{"key":"EntryName","value":"Cu_amine_oxidase_C_sf"}]},{"database":"InterPro","id":"IPR016182","properties":[{"key":"EntryName","value":"Cu_amine_oxidase_N-reg"}]},{"database":"InterPro","id":"IPR015800","properties":[{"key":"EntryName","value":"Cu_amine_oxidase_N2"}]},{"database":"InterPro","id":"IPR015328","properties":[{"key":"EntryName","value":"DUF1965"}]},{"database":"PANTHER","id":"PTHR10638:SF20","properties":[{"key":"EntryName","value":"AMINE OXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"PANTHER","id":"PTHR10638","properties":[{"key":"EntryName","value":"COPPER AMINE OXIDASE"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF01179","properties":[{"key":"EntryName","value":"Cu_amine_oxid"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF02727","properties":[{"key":"EntryName","value":"Cu_amine_oxidN2"},{"key":"MatchStatus","value":"1"}]},{"database":"Pfam","id":"PF09248","properties":[{"key":"EntryName","value":"DUF1965"},{"key":"MatchStatus","value":"1"}]},{"database":"PRINTS","id":"PR00766","properties":[{"key":"EntryName","value":"CUDAOXIDASE"}]},{"database":"SUPFAM","id":"SSF49998","properties":[{"key":"EntryName","value":"Amine oxidase catalytic domain"},{"key":"MatchStatus","value":"1"}]},{"database":"SUPFAM","id":"SSF54416","properties":[{"key":"EntryName","value":"Amine oxidase N-terminal region"},{"key":"MatchStatus","value":"2"}]}],"sequence":{"value":"MKLFLLFTLTLVNIFSVSLQEPIQNQPAGNNTITSPHRNVWRALSEAEFSGVSAVLVHQLNLTTSRGGNRIIQIDYLYPNKSDVLLFLDHNGEEPKRYARATVQFGSPEVPYLQEYRIGPLPATNTTAVEPLRFPFNGKVQGKTKITSLDADGIDAFLPQLSSVVEDITRKLWNTTLAEGGVSFNLGKASFNSDSTQTIWLGFLNNATTGFDSSTLLPLGVSMQLDITSRDYNDWFVLYWFYNNKLYTPTSFNETVYSSDFQPPLANIDGPWTSTNKQEPTFLLDDLPPPKAISRGKNRYNLDTEENYVQWMDFSFYFSSHTDRGLSLFNVVYKSKRIIYELSLQEALAHYAGVEPVPSEAVYFDTQTGMGRSMISLIKGYDCPDYATYLNSSFSSRTGVTITPDAICLFESDSQFPLRRHTSQAFGYASAARNVVFTVRWIATVGNYDYLFDYDFFYDGAIEVKVRASGYIQGAYYAGNEEYGFKIHDALSGSMHDHVMTFKADLDIYGEKNSVQKVEVVPETTIYPWSQGQPHNTMKLNRGFVTSETDSSIDWAADDAISYTIVNKDSPNKYGEYPGYRFRRVAPAIHLTVKNSTSGGKALHYATHDLFITQQKDNEPCAADRNNAYNIDDPLVDFEKFLDGESLEQEDLVLWINMGMHHTPHTEDLPNTIMTSAYSGIRFEPFNYLESGDPSVKSAQQARIILSNS","length":709,"molWeight":79874,"crc64":"CE3D3450E9550D39","md5":"9BD648759359BE5C1773173C58667BD7"},"extraAttributes":{"countByCommentType":{"FUNCTION":1,"COFACTOR":3,"PATHWAY":1,"SUBUNIT":1,"PTM":1,"DISRUPTION PHENOTYPE":1,"SIMILARITY":1},"countByFeatureType":{"Signal":1,"Chain":1,"Active site":2,"Binding site":11,"Modified residue":1,"Disulfide bond":1},"uniParcId":"UPI0003E9C336"}}