ID   H1VTQ8_COLHI            Unreviewed;      1284 AA.
AC   H1VTQ8;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Glucose-methanol-choline oxidoreductase {ECO:0000313|EMBL:CCF43616.1};
GN   ORFNames=CH063_03116 {ECO:0000313|EMBL:CCF43616.1};
OS   Colletotrichum higginsianum (strain IMI 349063) (Crucifer anthracnose
OS   fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum destructivum species complex.
OX   NCBI_TaxID=759273 {ECO:0000313|EMBL:CCF43616.1, ECO:0000313|Proteomes:UP000007174};
RN   [1] {ECO:0000313|Proteomes:UP000007174}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMI 349063 {ECO:0000313|Proteomes:UP000007174};
RX   PubMed=22885923; DOI=10.1038/ng.2372;
RA   O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA   Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA   Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA   Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA   Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA   Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA   Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA   Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA   Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA   Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA   van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA   Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA   Ma L.-J., Vaillancourt L.J.;
RT   "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT   by genome and transcriptome analyses.";
RL   Nat. Genet. 44:1060-1065(2012).
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DR   EMBL; CACQ02006234; CCF43616.1; -; Genomic_DNA.
DR   STRING; 759273.H1VTQ8; -.
DR   EnsemblFungi; CCF43616; CCF43616; CH063_03116.
DR   VEuPathDB; FungiDB:CH63R_05171; -.
DR   eggNOG; ENOG502QSPJ; Eukaryota.
DR   HOGENOM; CLU_002483_0_0_1; -.
DR   Proteomes; UP000007174; Unassembled WGS sequence.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   4: Predicted;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT   DOMAIN          74..106
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          558..622
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..51
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1284 AA;  141209 MW;  3A10A36E63D1ECCC CRC64;
     MAEQDQEVNG QGYATNGRNG AANGRSEPNG YESAFEETTE PFEGYDKSGG MFDPATGTYP
     RISRPVELIR PSYDVVVIGS GYGGAVAASR MARGNKQVCL LERGKEKWPG EFPSGIAASS
     KELHTTNAAT DGVLGSLGLH GVGHDPTGLY HLIVGDGQNA FVANGLGGTS LLNANVFLPA
     DDGVLSLPMW PEQLKGDELK PYYERAAEVL EPKKYPQDFP KLAKLETLEK QAKLMGWGDK
     FDRVPQTTRF EDGENSTGVY MRASTLSGQD TTGLNDGSKS TTLVNYLSDA WNWGAEMFCQ
     CEVRYVTEAE DREGYIVHFA WHGGKRANFK DIFYEDLMWV HAKELVFFGA GSIGTTEILL
     RSKKFGLQMS NDVGHGMSGN GDILAFGYNT SEYVNGIGRP DPPPNRPVGP CITGIIDCRH
     DLDNPLDGFV IEEGAVPAAL APFYRLMLTY LPYRKFPSNI SIKGMFGHVA AAYGSRIFGP
     YFAEGSTEKT QCYLIMSHDS TQATMQLHKD RIMINYSGVG KSHRAKKLAG YLAKLTNLIG
     GIYVDSPFYA AFGEKEITVH AIGGARISND DTGASGGVND KGQLFVGEGR EVHKGLVVCD
     GTIVPAALGV NPFATITALA ERSVEKVAEE FGINVDLKTK NGSLNLFAEP AYNQFEHEDD
     NFQVARVREI IKTARDDKTP GIAFTEMMDG WIHFGEDAET LDFERATETA KSRGEYARFF
     LSARSWNTHN LVNDKEHEAN LTGTFTCPAL GGTSMVQGGK FQLFNDDPRS PDTMNLTYNF
     LVSQKDGSKL HFNGYKVVNS DVVFNPLNLW KATTTLYCTI TEVDDQDQPM PDHVRGKGVI
     HIRPTKFLQE CTTMEATGST LYAKVASTAN FLGYFTAKAA GAFLTPFIPQ QWPSLPFHSY
     QNPTPWSEEM TVEANDRVKT KLYMWGPQGL SGQAADDAPI LLLIPGAAVD HQIFALPTID
     KNAVGYFRRK GYRVYSMVHR VGKTVVAQQN WTTFDARRDI QAALKKIREK HGIKDKPDGS
     GPSHMTYVVA HCAGSVALAS GLLDGTIPRQ WLSGVTASQV FMNPKFAKVN KIKASMPISM
     ANIYSLAQGK WFDCTSTPRD GYVQQAINQV LRFYPVGHRH EICNSVVCHR SSLVFGRLWS
     HKGLNEATHS QLENFVGGTS MASLNHLMFQ GTHDYATDSQ NENLVTPQNI ARLKGLPIFL
     FSGADNDVYA PDNTDISFTT LSEANGGGFY ERQVFKGRGH LDAWMSPTAH KDVFPRVLHH
     IENVQRGKYD ALRKVIAKPE GLKY
//