ID X0BHE0_FUSOX Unreviewed; 640 AA.
AC X0BHE0;
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_17059 {ECO:0000313|EMBL:EXK78253.1};
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:EXK78253.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK78253.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK78253.1,
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 -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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DR EMBL; JH658532; EXK78253.1; -; Genomic_DNA.
DR AlphaFoldDB; X0BHE0; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_002865_4_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:SF80; -; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000030663};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..640
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012497658"
FT DOMAIN 352..366
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 640 AA; 70299 MW; 4AD93B7B14E366AB CRC64;
MKLASWSILA GLATALPTNP PDQYEYIIIG SGPGGGTLAA NLARAGHSVF LIEAGGDQGN
TPLQRIPAMA DQVAEHPSMS WSFYVNHYQN ETQARRDSKY AYRLSNGTLW SGLNPPEGAE
PLGILYPRGA TLGGSAQLNA MNFALPPDND WDAIAELTGD ESWRFHKMRE LFIEIENCTY
APEGTPGHGF DGFIQSNRNN ISYITNRPGV VQSLKHAFEQ TEGIQVEDAA EVGRLMQRDI
NRLDKDRYSP GIYQIPLHVD SIRQRNGAWR HLHETMTART ANGSSWYPLT VSTHSLATRV
LLKEGRNGKP QAYGVEYLKG EGLYSADKRY DESESGRLIN VTASREVIVA GGTFNTPQIL
KLSGIGPREE LESLDIPVIM DLPAVGKYLQ DNYEGGVTVE ASVPWENNPF GNCPFTLEAN
DTCYQEWNQS HTGAYGEGAA PISLLYRSSV SETNDTDLYL FGAAGTVFRG YFPGYSTWQA
PPTSWFWSIV KMQPGNQAGT ITLRSKDPRQ APEINFNYFA EKGDRDLQAI QEGVEHTMRI
FNATGKPYAP FKVVEPRPGV SIRQGIMDDA FSHHATSSCR MGPAGDRNYC VDSEFKVNGV
DGLRVVDASI FPRTPGGFPA APTFMISQKA FGVIIGSIRG
//