ID B2WPV1_PYRTR Unreviewed; 597 AA.
AC B2WPV1;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE SubName: Full=Isoamyl alcohol oxidase {ECO:0000313|EMBL:EDU46167.1};
GN ORFNames=PTRG_12011 {ECO:0000313|EMBL:EDU46167.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU46167.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the oxygen-dependent FAD-linked oxidoreductase
CC family. {ECO:0000256|ARBA:ARBA00005466}.
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DR EMBL; DS231639; EDU46167.1; -; Genomic_DNA.
DR RefSeq; XP_001942342.1; XM_001942307.1.
DR AlphaFoldDB; B2WPV1; -.
DR STRING; 426418.B2WPV1; -.
DR EnsemblFungi; EDU46167; EDU46167; PTRG_12011.
DR GeneID; 6350329; -.
DR eggNOG; ENOG502QWB6; Eukaryota.
DR HOGENOM; CLU_018354_4_4_1; -.
DR InParanoid; B2WPV1; -.
DR OMA; NEADWGN; -.
DR OrthoDB; 1641938at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR Gene3D; 3.30.465.10; -; 2.
DR InterPro; IPR012951; BBE.
DR InterPro; IPR016166; FAD-bd_PCMH.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR006094; Oxid_FAD_bind_N.
DR InterPro; IPR006093; Oxy_OxRdtase_FAD_BS.
DR PANTHER; PTHR13878; GULONOLACTONE OXIDASE; 1.
DR PANTHER; PTHR13878:SF91; L-GULONOLACTONE OXIDASE 3; 1.
DR Pfam; PF08031; BBE; 1.
DR Pfam; PF01565; FAD_binding_4; 1.
DR SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR PROSITE; PS51387; FAD_PCMH; 1.
DR PROSITE; PS00862; OX2_COVAL_FAD; 1.
PE 3: Inferred from homology;
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..597
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002785051"
FT DOMAIN 118..304
FT /note="FAD-binding PCMH-type"
FT /evidence="ECO:0000259|PROSITE:PS51387"
SQ SEQUENCE 597 AA; 65679 MW; DF023599BBAAAB95 CRC64;
MSMGAAWRSQ ILHILLLVYV PLAACQCKCT PSQACWPTAD EWSQFNQTIS GKLIKTAPVM
LPCYVGPSYD AEQCAQLNDT LFYDPKFEAQ HPVGYDYPLN ETCPPPTVTD APASECQLGN
SPVYAINATM EADIQNGIRF AKEKNLRVVI KSSGHDFVQR SKGFYGLSIW LYHFRGGFTF
NEPVSISGGR HAQTWNGTSL TINGAYAWSD IYPNAWEKGV IVVGGNQNGP CSTGGWTQGG
GHSPVTRNFG MGGDQVLSAK VILASGELVE ASPDINPDLF FAIRGGGPGT YGVVTQLTVK
TYPNRNVNLF YIVLGAQGTE TVSKFLDAMT GVYSSFPSLS QKGFAGYGYW VANSANGLHE
HKFTNVWYQA FTITGKTAEQ SQKLFQSFED KVLSYNSTQL GIQVNITKSS YVDYGKYFAN
KTGTNAGVGG ISALSSRFLD TNALSGDKKR LRAAMDVMGG EPGKPVYHTL VHHGLETTHG
LQINDSAVQP GWYRSVVLDI FERDVVDFSY INNIEPFTYI RSKVEPVYRI LSPSVGTYMN
EADWGNVQWK EDFYGVHFDR LSMVKQKYDP DGVFYCITCV GSENWVVKED GTLCKSI
//
