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
//