ID   A0A1Z5TVF2_HORWE        Unreviewed;       667 AA.
AC   A0A1Z5TVF2;
DT   27-SEP-2017, integrated into UniProtKB/TrEMBL.
DT   27-SEP-2017, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=BTJ68_00097 {ECO:0000313|EMBL:OTA39986.1};
OS   Hortaea werneckii EXF-2000.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Teratosphaeriaceae; Hortaea.
OX   NCBI_TaxID=1157616 {ECO:0000313|EMBL:OTA39986.1, ECO:0000313|Proteomes:UP000194280};
RN   [1] {ECO:0000313|EMBL:OTA39986.1, ECO:0000313|Proteomes:UP000194280}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EXF-2000 {ECO:0000313|EMBL:OTA39986.1,
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   -!- 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}.
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:OTA39986.1}.
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DR   EMBL; MUNK01000001; OTA39986.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Z5TVF2; -.
DR   STRING; 1157616.A0A1Z5TVF2; -.
DR   VEuPathDB; FungiDB:BTJ68_00097; -.
DR   InParanoid; A0A1Z5TVF2; -.
DR   OrthoDB; 3382025at2759; -.
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:SF213; DEHYDROGENASE, PUTATIVE-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.
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:UP000194280};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..667
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5013142834"
FT   DOMAIN          245..379
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          487..633
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   BINDING         286
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   667 AA;  72208 MW;  09504B312B10258A CRC64;
     MFNIMRFLTF LSLLAGTALA APRARQSEDY EYIVVGSGPG GGPLASRLAR AGHSTLLIEA
     GHDQGTNANY SVPGYQGLVS QDPKMRWDMY CNHYQDLEQA KRDPKLSYDI GNGEIYTGLN
     PPDGAEPLGV LYPRAGTLGG CNAHNALIWV EPHASDWSNI QSITGDDTWN PDNMHDVYLR
     DRVHDWQPVH PTDPTILARD LVLTRHLLGG AATKGLGSIP VLDGLTGILP TLLVNPNGDF
     PDRDSKEGLF QIPLITQGGA RKSVRERIID TINEGYPLTV KSNTFVTKVD FDQINGTSRA
     TGVQYLEGSY LYRASPLSGG EGTPGSATAS KEVILSGGTY NTVQMLKLSG IGPRSELESH
     GIEVISDLPG VGTNMQDRYE IPLSAVHPDD FAILDGCTFD MKSHDKCYTQ WRNHLNILAA
     RGAYATNGLA AAMAQVSTTS PTGDVDLYIF GGPVNFVGYF PQWGDFAVSD HKHFSWYALK
     AHSQNHAGTV TLRSTDPLDP PEINFNYFDE GTTANGEDEK DLQSLVEAIR TGREALDNYN
     DYPFLGGSGF SEERPGANVT SDEDLKQYIK DQAWGHHACC TAKIGSDDDP FAVLDSKFRV
     RGVAGLRVVD ASVFPRIPGV FIQAPIMMIS EKAADAILGN EDARRDGGDD GSGLLGLDLD
     LGLNLGL
//