ID   A0A428QCB6_9HYPO        Unreviewed;       622 AA.
AC   A0A428QCB6;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 13.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=CEP54_005520 {ECO:0000313|EMBL:RSL62868.1};
OS   Fusarium duplospermum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL62868.1, ECO:0000313|Proteomes:UP000288168};
RN   [1] {ECO:0000313|EMBL:RSL62868.1, ECO:0000313|Proteomes:UP000288168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL62868.1,
RC   ECO:0000313|Proteomes:UP000288168};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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:RSL62868.1}.
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DR   EMBL; NKCI01000042; RSL62868.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428QCB6; -.
DR   STRING; 1325734.A0A428QCB6; -.
DR   Proteomes; UP000288168; 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   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:SF115; DEHYDROGENASE XPTC-RELATED; 1.
DR   PANTHER; PTHR11552; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 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; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Flavoprotein {ECO:0000256|PIRSR:PIRSR000137-2};
KW   Reference proteome {ECO:0000313|Proteomes:UP000288168};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..622
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5019488609"
FT   DOMAIN          303..317
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        556
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        599
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         50..51
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         118
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   622 AA;  68178 MW;  43E904FFCCDB0D73 CRC64;
     MTSLFSTTGV LRLMLLFGSV LGLKKPEHHT QHSMESVLDE YDYIVIGGGT SGLVVANRLS
     EDPSKTVLVV EYGDFANTIN VTVPYFTTLD QTPRLYNMTS VPQVHLDGRT SRMRLGSVVG
     GSSTINGMAW DRGSSVDYDS WEELGNPGWG WKSLLKYFRK SSRFSPPAEK YVEKYGYTWT
     AESYGHGPIK VGYPSWQWPG AAMQAEAWTE DLDADILRDG ADGKNVGLAW IPQNSGGKEA
     TRSSAETAYY QPASHRPNLH LLVRHYGAAI KFNGNITTGV DIASRDGRPW RCISSKNVIL
     AAGAINTPRI LQLSGIGPKK LLDSLDIDIV VDAPGVGANF QDHPTFNMIY EFNNKSVPTR
     DLMNDPDFYD AAWEEYIANK TGPFSHAWGN YISFSSLQDL DPDFEAIASS LADQEPLDHL
     PAIYAENPSL VKGFLEQRRV LQSQFRNPEA GILEIVFSGA VVVPVALQKP LSRGTIFINT
     TNAEPSISPL IDFNTAANPV DMHIVMRALT KARQFMAAES VASLEPVEVS PGLTLQDEVE
     IQTAMRKTFL SPSLDHPVGT AAMMPQEWGG VVDTNLRVYG VEGLWVVDAS VMPLLPAAHT
     QATVYAVAEY AADLIKKDSK HA
//