ID   W9CDP2_SCLBF            Unreviewed;       547 AA.
AC   W9CDP2;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=SBOR_5666 {ECO:0000313|EMBL:ESZ93963.1};
OS   Sclerotinia borealis (strain F-4128).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Sclerotiniaceae; Sclerotinia.
OX   NCBI_TaxID=1432307 {ECO:0000313|EMBL:ESZ93963.1, ECO:0000313|Proteomes:UP000019487};
RN   [1] {ECO:0000313|EMBL:ESZ93963.1, ECO:0000313|Proteomes:UP000019487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F-4157 {ECO:0000313|Proteomes:UP000019487};
RX   PubMed=24459262; DOI=10.1128/genomeA.01175-13;
RA   Mardanov A.V., Beletsky A.V., Kadnikov V.V., Ignatov A.N., Ravin N.V.;
RT   "Draft genome sequence of Sclerotinia borealis, a psychrophilic plant
RT   pathogenic fungus.";
RL   Genome Announc. 2:E0117513-E0117513(2014).
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:ESZ93963.1}.
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DR   EMBL; AYSA01000277; ESZ93963.1; -; Genomic_DNA.
DR   AlphaFoldDB; W9CDP2; -.
DR   STRING; 1432307.W9CDP2; -.
DR   HOGENOM; CLU_002865_6_3_1; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000019487; 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:SF123; GMC OXIDOREDUCTASE (AFU_ORTHOLOGUE AFUA_2G01770)-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|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019487}.
FT   DOMAIN          85..108
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          258..272
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        490
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        528
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         222
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   547 AA;  58716 MW;  55382D6E43A2C246 CRC64;
     MAETSNYHYI IIGGGIAGSV VASRLHEKHP SLSILLIEAG PDVSDNPLVT DSANGPFLVG
     SELDWGYSTV PQRHLNNRAL PNNAGKALGG GSAINAGGWI RGDANDYNAW GKLVNDPRWS
     YAGFLPYFHR TEQYHKAGLD TQHGYEGPLY TQSVSSTDRN YPLRENIRKA WESIGINYNA
     DANSGSPQGL GELVENRKDG QRQVASTAYP LTGVQVMTST LVARVLMDTQ GLIPRATAVE
     LADGRKIVAT KEIIISAGAF RTPQILLLSG IGTKGELAIH GIQQIVDAPY VGKNLHDHMS
     VAQWWKLKNP EAGYALGSPL FNNPNFKKGT PMDWVVTYTV PHEGLKAALA KDEGIVDDMH
     PLLSPARSHV ECFTVYVGVN KSDPIIPMDG SHVTTVVLGG LPTSRGSVKL ASTDPTAAPV
     IDPNYFSTEA DRYVLRTGLR KIMEAMLSTA EGQALIETET VAAGEKSLDW KAEDAELDER
     IKARGKTVYH PAGTAAMGKV VDSSLCVYGV QGLRVVDASV LPLPIAAHYQ ACIYALAEQA
     AEIIGAS
//