ID   A0A0W0G550_9AGAR        Unreviewed;       610 AA.
AC   A0A0W0G550;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=WG66_3713 {ECO:0000313|EMBL:KTB43708.1};
OS   Moniliophthora roreri.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX   NCBI_TaxID=221103 {ECO:0000313|EMBL:KTB43708.1, ECO:0000313|Proteomes:UP000054988};
RN   [1] {ECO:0000313|EMBL:KTB43708.1, ECO:0000313|Proteomes:UP000054988}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCA 2952 {ECO:0000313|EMBL:KTB43708.1,
RC   ECO:0000313|Proteomes:UP000054988};
RA   Aime M.C., Diaz-Valderrama J.R., Kijpornyongpan T., Phillips-Mora W.;
RT   "Draft genome sequence of Moniliophthora roreri, the causal agent of frosty
RT   pod rot of cacao.";
RL   Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KTB43708.1}.
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DR   EMBL; LATX01001102; KTB43708.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0W0G550; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   Proteomes; UP000054988; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   Gene3D; 3.30.560.10; Glucose Oxidase, domain 3; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054988}.
FT   DOMAIN          92..115
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          285..299
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         23..24
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   610 AA;  66559 MW;  8D66910002813FD3 CRC64;
     MPIVQIGYFV STKLDCLVIG GGTSGLVVAT RLSEDPTVTV GVIEAGANHA GDPSVDIPGN
     MTKNARNPKY DWEFYTEPQV YAHNRKIQSS RGKGLGGSSG LNNLAFVRPV SEELDAFEKL
     GNPGWNWNNV LGFMKKSEHL CVPPLSEGEK KSYAVDPDPA YHGTDGPIAV SFPPYVSPIH
     NKILDSLETL GLPRNNEPNA GRNVGSYLVS TSVDPVTATR SYAASAYLHP HLTRNNLFVL
     TEAFATKIHF DGANNGLKRA VAVDFIKEGQ SYQVKVAKEI ILSAGTFQTP QILETSGIGD
     PRILEPLGIQ CIIKLPGVGE NLQDHMKAPT VVQVQQDLQT PELLRNPDEL NIQQELYKEK
     KGILAGMLSS CFAFLPGNLI ADSEHVKAWK NLANVESSAP EVFAKTHPDV LRGIKKQYKI
     LEQWIDDPVH PLAQLLNING HFPVVGLTPD NSKRYMTLIV AYTHPFSRGS VHITSADAQV
     RPAIQPNYLS NRADLEILSK AIEFTLQLYQ TPPLSDLIVA PVAPPFFKSD DAEKVNEFAR
     EILSTVHHPV GTASMMPQED GGVVDHNLLV YGTSNLRVID CSIIPLQISC NIVTLAYAIG
     EKASFRGRSV
//