ID   A0A0P7BFU6_9HYPO        Unreviewed;       565 AA.
AC   A0A0P7BFU6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN   ORFNames=AK830_g4590 {ECO:0000313|EMBL:KPM41983.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM41983.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM41983.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM41983.1,
RC   ECO:0000313|Proteomes:UP000050424};
RA   Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT   "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT   ditissima.";
RL   Submitted (SEP-2015) 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, 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:KPM41983.1}.
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DR   EMBL; LKCW01000056; KPM41983.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7BFU6; -.
DR   STRING; 78410.A0A0P7BFU6; -.
DR   OrthoDB; 3073733at2759; -.
DR   Proteomes; UP000050424; 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; GLUCOSE-METHANOL-CHOLINE GMC OXIDOREDUCTASE; 1.
DR   PANTHER; PTHR11552:SF134; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN; 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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424}.
FT   DOMAIN          84..107
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   ACT_SITE        498
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        542
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         94..97
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         231
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         497..498
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   565 AA;  61885 MW;  02305A014DE267E5 CRC64;
     MASSTFDFVV VGGGPAGSAV AAGLARSAKK PSVLLLEAGG PNDDRNLRVD GQRWLTFMNK
     DLNWGYKTTP QEHCDNRELD YSRGKGLGGS SAINFGVYTV GARDDYEEWA RIVGDDTYRW
     DKIQPRYKTL EEFHGELPSG IDSKYAAPKA ENHGTSGPLK VGFAAEWEED LPPMLDLFED
     AGFPLNQDHN SGNPIGMSVL VNSSNKGLRS TASDLLTPAP ENLTIITSSP VQRVILDGNK
     AVGVESNGKK YLASKEVVLS AGSLENPKIL MHSGIGPRKQ LEEFGLPVIK DVPSVGQGLR
     DHMFCPLVYK RKEGDTARAP FYGDQKVMDE ALEQWKRDGT GPWTKFACEL GIGWFKLDKL
     VASDEFKALA AEEQAYLTKP TVPHYEVLTH FPIHWFIPGF PQDSLNCSCI LVFYYNAQSR
     GEVTLQSADP NTPLKFDPKF LSSPFDRRAA VEALRDAFRI AKHKGYADNN EAVIAGPQGD
     SDEDLLAYWR QTISSSWHMS GTVKMGKPGD ADAAVDSDFR LMGIDNLRVA DMSVVPVLAS
     CHVQSVAYVT GMTCAEKLIA EYGLS
//