ID   X0BE97_FUSOX            Unreviewed;       640 AA.
AC   X0BE97;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   SubName: Full=Choline dehydrogenase {ECO:0000313|EMBL:EXK80136.1};
GN   ORFNames=FOQG_15310 {ECO:0000313|EMBL:EXK80136.1};
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:EXK80136.1, ECO:0000313|Proteomes:UP000030663};
RN   [1] {ECO:0000313|EMBL:EXK80136.1, ECO:0000313|Proteomes:UP000030663}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54005 {ECO:0000313|EMBL:EXK80136.1,
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; JH658451; EXK80136.1; -; Genomic_DNA.
DR   AlphaFoldDB; X0BE97; -.
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:SF100; DEHYDROGENASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_5G00630)-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   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..640
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5004936870"
FT   DOMAIN          122..387
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          493..630
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   BINDING         294
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   640 AA;  68938 MW;  2BF92AF98893B2E6 CRC64;
     MRHAFFAGLL AAPASVCAVA LTGYEYIVVG SGAGGGPLAA RLALAGHKTL LIEAGDDYAS
     LNYTVPAYSA NASEDPEISW NFFVRHYADD ERQARDYKTT YDTPNGEYTG LNPPEGAEIK
     GTLYPRTQAL GGCTAHNALI AVYPHQSDFE YIASLTGDES WSADNMRKYF VKAEDNNYRP
     AGEAGHGYDG WLSTETAPLS IPLNDEQLLS ILSGGAVALS EMTGKNITMD GLIADDANAD
     TLARDQEPGF YQIPLSTKDA SRIGPRELIL SVRDAKHPNG TKKYPLDVRT NCYVTKVTFD
     DSKPPRANGV EFLDGKHLYK ASPLATGAAG TPGNATASRE VVVAGGVYNT PQILKLSGIG
     PADELKKFDI PVISDLPGVG TNLQDHYEIS VQGTLENNFT SFDGCTFGLF TDEDPCVDRW
     RAPVDGDHGI YSSSGLAASM FYKSSTAEKD NFDIFAFGGP VNFRGYFPQY AVNATIEHNW
     FSWAILKAHP RNNAGEVLLQ SADPLDMPAI TFNYFDTGNG DYSADLQALY EAVELTRSAL
     ASQAVNVTEV LPGADVTSQK DIETYVKDVA WGHHASSTCP IGADDDKMAV LDSKFRVRGV
     AGLRVVDASV YPRIPGTFTA VSTYMVAEKA ADIMLAELEE
//