ID X0BFU7_FUSOX Unreviewed; 546 AA.
AC X0BFU7;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=FOQG_14470 {ECO:0000313|EMBL:EXK81040.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK81040.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK81040.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK81040.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) 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; KI979336; EXK81040.1; -; Genomic_DNA.
DR AlphaFoldDB; X0BFU7; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_011025_2_1_1; -.
DR Proteomes; UP000030663; 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 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; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR PIRSF; PIRSF000137; Alcohol_oxidase; 2.
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:UP000030663};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..546
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004936294"
FT DOMAIN 278..292
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT BINDING 113
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 121..124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT BINDING 240
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ SEQUENCE 546 AA; 58419 MW; 1D6360A10D037237 CRC64;
MRFSSLSGMS ALTLAALTAP ASCKPADSTY DYIVVGGGPA GLITAERLSE ANKKVLLLER
GHGPTVATGS NHTLSWDSSL TPIDVPGLSS AVGGLDLWNE YMCDDTAALA ACVLGGGVTV
NYMVFVHPPA RDFDDKWPKG WKWNDVAPAA DRLYARNQGT LVPSKNNERY DQGLYNTLSG
FFDKLGWKSV DMIKQPNEKH EVYSWPSWNV KNALRAGPVR TYLPLAQKRN NFTLRMGSKV
IRVVRSGSRA TGVEVETAAG KKEIVKLSKN GRVVLSAGAL TTPRLLFNSG IGPKKQILTA
KKTGVTLPAE RNWINLPVGE NLMDHPIFTF TVKTGGAWGM LDTDSVLNGT DTKNIDLYEQ
KSSGVLTQGR HRMIFFSSNK GSDGVTRYFQ GSCAAGGDGI ASIKVYMTHG LTSTGVLGMT
EEGKTVIEKS PYLQTDGDVE AAKAFVQDMV EKITDSSSGF VLQKETNTTA IIKAVTSGNH
YAGTTKMGTD DGRKGGSSVV DTNAKVYGMD NLFVSDAGIH PDLPTGNIQT IVMVAAEAAV
AKILAC
//