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Database: UniProt
Entry: W9XX74_9EURO
LinkDB: W9XX74_9EURO
Original site: W9XX74_9EURO 
ID   W9XX74_9EURO            Unreviewed;       614 AA.
AC   W9XX74;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=A1O1_08022 {ECO:0000313|EMBL:EXJ81955.1};
OS   Capronia coronata CBS 617.96.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Capronia.
OX   NCBI_TaxID=1182541 {ECO:0000313|EMBL:EXJ81955.1, ECO:0000313|Proteomes:UP000019484};
RN   [1] {ECO:0000313|EMBL:EXJ81955.1, ECO:0000313|Proteomes:UP000019484}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 617.96 {ECO:0000313|EMBL:EXJ81955.1,
RC   ECO:0000313|Proteomes:UP000019484};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA   Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA   Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA   Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Capronia coronata CBS 617.96.";
RL   Submitted (MAR-2013) 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:EXJ81955.1}.
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DR   EMBL; AMWN01000007; EXJ81955.1; -; Genomic_DNA.
DR   RefSeq; XP_007727076.1; XM_007728886.1.
DR   AlphaFoldDB; W9XX74; -.
DR   STRING; 1182541.W9XX74; -.
DR   GeneID; 19162875; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_6_1_1; -.
DR   OrthoDB; 858083at2759; -.
DR   Proteomes; UP000019484; 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: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|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019484}.
FT   DOMAIN          93..116
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   ACT_SITE        542
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        585
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         99
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         103..106
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         244
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         541..542
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   614 AA;  67926 MW;  BD20BEF70EEFE166 CRC64;
     MESFSALPKD FATSKFDYLI VGGGTAGLVV AARLSENPNV VVGVIEAGFS ALDEPLVSIP
     GNFGRTIGTK YDWAFATVPQ EGLKGASLPW PRGKMLGGTS GMNFLVWNRG AKEDYDAWEQ
     LGNEGWNWEQ LKYYFKKSER MNQPPASFES HHQTFFKPED HGRSGPVSTA YPSHIAPTHK
     YWHSTLKNMG INTNKSHFGG SNIGAWTSVA CLDPQTQTRS YSASAYYRPN ARRENLHVLT
     EAHVLEIVMS ETQRGGDFTA TGVKIKYQGS VFTIPCSKEV IVCGGSVGSP QLLELSGVGN
     PAILKKAGIT PRVANINVGE NLQEHMMTMT VFEIDTDIVT PDNYADPKFL EEALRLYETQ
     KSGLLTCTPA SMAYLPLSKM IPAPEVGQFL RRAEDLASSH PRDSTLHKLD KMLSRQFLPQ
     YSLGQVEYMF DHSNYSPFYV SEPGKKYASM MQILQYPFTR GSIHIDASSP HDKVVIDPKY
     YQGEGSLDLD IMIKAQAYGD TIWRHEPMRS IIKKRVWPPE TLKGQTTDWA AWVPAHTTTD
     WHPVGTCSML PRDAGGVVDA KLKVYGTTNV RVVDASVFPL HVSAHIQATI YAVAEKAADM
     IKETSGQPQL MGKL
//
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