ID   A0A0D2DHT9_9EURO        Unreviewed;       623 AA.
AC   A0A0D2DHT9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=PV05_01943 {ECO:0000313|EMBL:KIW61872.1};
OS   Exophiala xenobiotica.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX   NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW61872.1, ECO:0000313|Proteomes:UP000054342};
RN   [1] {ECO:0000313|EMBL:KIW61872.1, ECO:0000313|Proteomes:UP000054342}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW61872.1,
RC   ECO:0000313|Proteomes:UP000054342};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL   Submitted (JAN-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}.
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DR   EMBL; KN847317; KIW61872.1; -; Genomic_DNA.
DR   RefSeq; XP_013322456.1; XM_013467002.1.
DR   AlphaFoldDB; A0A0D2DHT9; -.
DR   STRING; 348802.A0A0D2DHT9; -.
DR   GeneID; 25323851; -.
DR   HOGENOM; CLU_002865_5_1_1; -.
DR   OrthoDB; 2392848at2759; -.
DR   Proteomes; UP000054342; 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:SF78; GMC_OXRDTASE_N 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; PS00624; GMC_OXRED_2; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000054342}.
FT   DOMAIN          285..299
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         104..107
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         545..546
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   623 AA;  68975 MW;  7D9DE4A73AA311E3 CRC64;
     MPLHTKLPDD LKEVDVIIAG GGLAGCVVAS RLAEADRNLV ILVIEQGPNN YGMPEVVHPA
     LYPRNLFPSS KITLFWQTKK SPQLGNRSPI VPSGGTLGGG SAMNWMVYTR AQRSDFDSWK
     TPGWSADEML PFLKKLETYH GKGDKDRHGF DGPVNISKGT HVCGRAENAF VEAAAKLGYP
     EVSDLQNLDA NNAIERYYRY VGPNGRRQDA AHRYLHPKLQ SGDYPNLHVL VEKQVLKVLF
     DDNKRAVGVE YQTNPKYLAN PEYLATAYTA LRTVRARKLV VISAGANATP GILERSGIGD
     PQVLQRAGVP VVEDLPGVGE DYQDHHLSLW AYRTNLTPRE CINGFQDGRF NIDDAIKNTD
     ELLGTNAMDA QGKFRPTDAE VEALGPEFKK AWDRDFKNVP DRPLMILALY CCFYGDHSVL
     PDDAEYVSMA NWTAYPYSRG HIHITGPAMS DPVDFDTGWL TDAGDVDVKK HIWAYKITRE
     MWRRMPIFRG ELASNHPRFS PDSKAAVIEK ADGPIMTDDA ARIEYSPEDD KAIDQKVREV
     LSTTWHSLGT CKMAPREKKG VVDKDLNVYG VTGLKLADLS VPPENVGANT GNTAFVVGEK
     AADIFIKELG LGKDKSDLPQ ARL
//