ID   X0BHW4_FUSOX            Unreviewed;       617 AA.
AC   X0BHW4;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623, ECO:0000259|PROSITE:PS00624};
GN   ORFNames=FOQG_13894 {ECO:0000313|EMBL:EXK81725.1};
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:EXK81725.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK81725.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK81725.1,
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|ARBA:ARBA00001974,
CC         ECO:0000256|PIRSR:PIRSR000137-2};
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR   EMBL; JH658423; EXK81725.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0BHW4; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_002865_6_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   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:SF210; GLUCOSE-METHANOL-CHOLINE OXIDOREDUCTASE N-TERMINAL DOMAIN-CONTAINING PROTEIN-RELATED; 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|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030663}.
FT   DOMAIN          96..119
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          279..293
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   ACT_SITE        535
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   ACT_SITE        580
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-1"
FT   BINDING         102
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         243
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         534..535
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   617 AA;  67252 MW;  BCB7F5F3FF70063A CRC64;
     MSVNPSLRTV DQFTQLVFDF IVIGGGTAGL AVAARLAEAD ASYTVGVIEA GGPVQNDPDV
     DIPGHYGRNL GGSYDWHLET LPQEGLGGRT LPWPRGKCVG GTSALNYMAW NRASRDDYDA
     WEALGNQGWG WDSLLPFFKR SETFHPPSEK LQREFEISHD ADTFGDSGPI HISYPTSYSP
     SHTLWHKTLN ALGVETNPSH VGGSNVGVWT CVNAVEPSAA RRSYSIDYAT GSRNLHILTN
     ATVDEILINQ ALVATGVRFT YGGVEYDVSA RREVILSAGS VKSPQILELS GIGNPSVLSS
     AGVSVKVESP QVGENLQEHI MLATIFEVDP SLANRDDLMR DEKLSAAAKE EYTTKADGPL
     TVLPVSLCYV PFAHFVPKNT LASLYEDADK VSVFDSDKQD ILRERLDGNS KLGQIEYIFD
     LGNWNPNFKG EEGKKYGTML QILQYPFSVG SIHIRPSDHA TAEDSPAIDP KYYEGLHGNL
     DMEAMKQCLQ FVDKIVHTAP LSNIIRSSAS PSTAIIKDDK RLGEWITQNT ITDWHPVGTC
     AMGGRAGIEG GVVDERLRVY GVHGLRVVDA SVMPLQISAH IQATVYAIAE KAAHMIVEDA
     RSADREGREL VTKQARL
//