ID   A0A0P7BAK6_9HYPO        Unreviewed;       617 AA.
AC   A0A0P7BAK6;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=AK830_g3867 {ECO:0000313|EMBL:KPM42666.1};
OS   Neonectria ditissima.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX   NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM42666.1, ECO:0000313|Proteomes:UP000050424};
RN   [1] {ECO:0000313|EMBL:KPM42666.1, ECO:0000313|Proteomes:UP000050424}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R09/05 {ECO:0000313|EMBL:KPM42666.1,
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:KPM42666.1}.
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DR   EMBL; LKCW01000044; KPM42666.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0P7BAK6; -.
DR   STRING; 78410.A0A0P7BAK6; -.
DR   OrthoDB; 858083at2759; -.
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: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; 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|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..617
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5006135571"
FT   DOMAIN          116..139
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          308..322
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        553
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        596
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         118
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         126..129
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         267
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   617 AA;  65700 MW;  119E890ED54A6C2E CRC64;
     MSASTVAAIA AFLSIQGVLA SPYFPGQYKT NARQLLTSYD YVVVGGGASG LTVANRLSED
     SDITVLVIEA GDFDANEDFV TIPGLAGGAV GTKYDWNLTY TASESLGGRN VSIPQGKVVG
     GSTKLNRMVF DRGSKSDYDR WATLGNEGWN WDALLPYFKK NEKFTPPSDA LVAEYNITYD
     AAAHGTSGYM HSSYSPFFWP TTKNIIKALK ELKIPISKDQ ANGNALGGYF CPHNQDPVAI
     TRSSAREAYY NNFTKRQNLH LISGHQVTRI VTKKTSSAVK VTGVEFATSK TAARGTVQVK
     KEAILAAGAI HTPQILQISG IGDSKTLSSI NVKTVVDLPA VGQNFHDHVL LAVVNVITAP
     LTSSMLTSNA TFAAEARAQY DQKRQGPLTS PTGDFLAFLP LSTYSEASSS ISAQATSQDG
     TKFLPSGTPA EVIKGYKAQQ KLLNSKLLSK DSAVLEVIWS DGVMILGLQH PYSRGSVKAS
     SGCTFDAPIA DAGFLRNPLD VAILAEGVRF TRTIAATSAI TPLQPLEVVP GVNVTSDADL
     EQFIRSSAST LFHPGGSCKL GKREEGGVVD AELKVYGVQG LRVVDASVIP LLPASHTMTT
     VYAVAERAAD IIKRAQK
//