ID   F9G3C1_FUSOF            Unreviewed;       659 AA.
AC   F9G3C1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN   ORFNames=FOXB_13153 {ECO:0000313|EMBL:EGU76337.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU76337.1};
RN   [1] {ECO:0000313|EMBL:EGU76337.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU76337.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
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:EGU76337.1}.
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DR   EMBL; AFQF01003296; EGU76337.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9G3C1; -.
DR   STRING; 660025.F9G3C1; -.
DR   PaxDb; 5507-FOXG_04733P0; -.
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   Pfam; PF13450; NAD_binding_8; 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;
FT   DOMAIN          361..375
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
SQ   SEQUENCE   659 AA;  72401 MW;  1C375B81D6DC3938 CRC64;
     MSDSSTIHVL EATVGSVSER GEAIPEEELD TLDGYEYVVV GSGAGGGPLA ANLARNGHRV
     LLLEAGDDQG SNLNQQVPAF HSKSTEDEKM RWDYFVKHYA DEKDAQKDSK MTWETPMGTL
     YIGLNPPSGS KPKGILYPRA GTLGGCTAHN AMITIYPHEN DWSNIASLTG DDSWQPDNMR
     QYFKRLERCE YLPNGTPGHG FTGWLGTDRA DLRLALGDFK ILSIISAAAT AMGNTILGLI
     PEKVTQLLGL LLRDMNSIDP RRDMTEGIYQ IPLAMSHGKR SGVRNFLVET AKMYPLDIRT
     GCLATRVIFD ESSLANSTPK ATGVEFLEGS SLYKADPRSS SSTNGTKRRV LISREVILAA
     GAFGTPQLLK LSGVGPMDEL QKFGIRVVKD MQGVGTNLQD RYEIPVITKI EDDFPIITKC
     TFGEPEDPCL ADWYLQRGPY LSNGLPIGIV KKSSQADADP DLFIFGGPTF FRGYYPGYSE
     VTTSDKRHFT WAVLKAHTHN QDGTVMLTSS NPRDVPDINF NYFTTSQSET EKSERDLGAI
     AEGIAFARRI MDDVLPIATG PLEEALPGRH LDSTEQVKEF IRNEAWGHHA SCSCPIGSDG
     DPKAVLDSRF RVRGVSNLRV VDASVFPRIP GFFIVLPIYM VSEKATDVIL EDIGERSRV
//