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Database: UniProt
Entry: U7Q0W5_SPOS1
LinkDB: U7Q0W5_SPOS1
Original site: U7Q0W5_SPOS1 
ID   U7Q0W5_SPOS1            Unreviewed;       642 AA.
AC   U7Q0W5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=HMPREF1624_01862 {ECO:0000313|EMBL:ERT00635.1};
OS   Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS   disease fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX   NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERT00635.1, ECO:0000313|Proteomes:UP000018087};
RN   [1] {ECO:0000313|Proteomes:UP000018087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 58251 / de Perez 2211183
RC   {ECO:0000313|Proteomes:UP000018087};
RX   PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA   Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA   Goldberg J., Young S., Zeng Q., Birren B.W.;
RT   "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT   58251).";
RL   Genome Announc. 2:E0044614-E0044614(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}.
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DR   EMBL; KI440843; ERT00635.1; -; Genomic_DNA.
DR   AlphaFoldDB; U7Q0W5; -.
DR   STRING; 1391915.U7Q0W5; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_4_1_1; -.
DR   OrthoDB; 3382025at2759; -.
DR   Proteomes; UP000018087; 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   GO; GO:0009058; P:biosynthetic process; IEA:UniProt.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
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:SF80; 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.
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:UP000018087};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           21..642
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004687378"
FT   DOMAIN          380..394
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   BINDING         155..158
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   642 AA;  68237 MW;  986E5EAA260EA174 CRC64;
     MRGALFSLAA TALIVGGASA GRMLDGSIAV DRAASDNVTY DYIVIGSGPG GGPLACDLAR
     AGYSTLLIEA GDDQGDNPVY SELANFNTAG NDPDSRWDFW VKHSDDPVRE MAFAHYTYRT
     TNGSFYVGTE PPAGATPLGI QYPRAGTLGG CAMHNGGVCS LPADDDWNIV VNMTGDTSWE
     APKMRKYLVK VEKNQYLPTG TEGHGFDGWL ATAVQPTRWA RDIALPATRV LKQMAALTGQ
     NASDVANLVD KDILGDYPHK DTLSSFYNMA QHQDKGGKRS SPNNYIKATL KDPKNYPLTV
     RLNTLATRVL FQQPHAGNAT SRVEGTGVGA GAALPVARGV EIMSGPSLYR ADPRHTNANV
     TKKGPVSKVW ARREVIVSGG AFNSPQILKL SGVGPAAELS KLSIPIVKDL PGVGERLADN
     YEGSLLALGQ QPVGGGFITL LFKTPNADGP NRNIFTWCGA FSFEGFWPGF PTDYGPNEYE
     CAMVLINPHS QAGTVKLASA DPQVPPDINL NFFLNNGTED LQHLADAAKL LRTAWQAAGD
     PVLPFNEKHP CPGTGAGNCT DEAQRALLKT QAYSHHASSS CAIGSDTDPL AVLDSKFRVR
     GVQGLRVVDA SAFPRVPGAF PVLPTIMLSA KAAEEILADA KK
//
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