ID   A0A1Z5SQL0_HORWE        Unreviewed;       580 AA.
AC   A0A1Z5SQL0;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=BTJ68_14260 {ECO:0000313|EMBL:OTA23126.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA23126.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA23126.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA23126.1,
RC   ECO:0000313|Proteomes:UP000194280};
RA   Sinha S., Flibotte S., Neira M., Lenassi M., Gostincar C., Stajich J.E.,
RA   Nislow C.E.;
RT   "The recent genome duplication of the halophilic yeast Hortaea werneckii:
RT   insights from long-read sequencing.";
RL   Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
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:OTA23126.1}.
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DR   EMBL; MUNK01000318; OTA23126.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5SQL0; -.
DR   STRING; 1157616.A0A1Z5SQL0; -.
DR   VEuPathDB; FungiDB:BTJ68_14260; -.
DR   InParanoid; A0A1Z5SQL0; -.
DR   OrthoDB; 3714148at2759; -.
DR   Proteomes; UP000194280; 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:SF111; 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.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000194280};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           22..580
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012803352"
FT   DOMAIN          146..169
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          331..345
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          26..60
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..60
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   580 AA;  63148 MW;  50457EBC51B6D6BE CRC64;
     MRHFSCVKAL ACLLILGECG GSWNPGQNSR SHDEHISPPH HTPLGHTNGR HNQQGNKHTS
     TSNHLVDYAI VGGGPAGLVL AEQLSQDESV SVVLLEAGPD GTNAETINVP ALAPFNSIPT
     PNQYFWNFTS QPDPNLAGRT PVLNQGRTWG GGSAVNYMEY CRGAPSVFDE WADLSGDEEL
     RWEALLEDFR ATTHWAPGAS DQYDQLVDLD AYGEGPLEVS RFASTGGFDP YFFEALKEGL
     DLPEIDVNSG HGLGVSYSTE SIRVSNRTRA YALPAYGWQM ADRPNVQMLQ NAWASKIGFD
     GKRAVNVTYY TGPDNEESHT ITAREIILTA GAIGSPRLLM LSGVGPKDHL EEVGIPVIHD
     SPSVGQNLKD HHFSVLEVEV TSEVESIWQY LNNATFAAEA HAEYATNSSG FLARNDAGSF
     AMARVPDEIF HAVNASFHPS LPSDRGHLLY QYVNAAFVPN SPNVSIASPF VALAQPEAAG
     SLRLASPDFR IPPLIQSNYF GSPGDKAAIL HGYKTLRELL QSEIMKPVVL REVFPGPDIT
     TDEDLWAAIQ QTAQTFYHPH GSLALGEVVD GDWRVRVWKG
//