ID   F9FVP6_FUSOF            Unreviewed;       801 AA.
AC   F9FVP6;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00623};
GN   ORFNames=FOXB_10477 {ECO:0000313|EMBL:EGU79048.1};
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:EGU79048.1};
RN   [1] {ECO:0000313|EMBL:EGU79048.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU79048.1};
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, ECO:0000256|RuleBase:RU003968}.
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:EGU79048.1}.
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DR   EMBL; AFQF01002717; EGU79048.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FVP6; -.
DR   STRING; 660025.F9FVP6; -.
DR   PaxDb; 5507-FOXG_05670P0; -.
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   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
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; PF16010; CDH-cyt; 1.
DR   Pfam; PF12831; FAD_oxidored; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF49344; CBD9-like; 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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..801
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal
FT                   domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003390059"
FT   DOMAIN          312..335
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   REGION          204..225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          761..785
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   801 AA;  85165 MW;  CB2AA21A086880B9 CRC64;
     MRFTLSSMAG LLGLASAQGL RSSAYTDPKT GIDFQRFVDD GYSLGIAVPE TLGKDLIAQM
     VFPREKEGWG GISFRGGMVG GLLFVAWPNG DDIVTSFRMA NSYANPDVYT NTTVKATPIP
     DGTFINSTHV SYTFLCEGCV VEKTTSLTGE SPVVGYAWSS IDVDTPSDPE SALSYHGAGF
     GQFGLDIKNA ASAKFATWAD MAKETTPAPG TGTPGVPGNS TTLPPTTSNV TYDVIVVGGG
     PAGIIAAERL AESGASVLLI ERGPANTVAL GNAAQALPWN NTLTPYDIPA LGSSMTSMSG
     TKFCSDTAST AGCLLGGSSS INGLNFIHPP ERDFQRWPKG WSWSDLSKAA DRLYERNPGS
     TSPSDDGKYY DDRTYTILSG YLSAKGWKEV DSIEEPNEKH LVYSRPSWSI KNNMRAGPAR
     TYMPFAKNLP NFTLKLETKV IQPIRSGSKI TGVLTQGANG SKQIINVKAG GKVVLAAGAM
     STPRLLWNAG IGKSDALAIV KQGASKTGVT LPAASDFIDL PVGHHLQDHA QVMLQFKTKS
     NFTAYKFNNI ATEPVKSDLE LYYQGSGPIT QAAQRMHLWT SAKGADGRVR YLQGTASAMA
     DGIITVRTFL THGTSTVGEL GITAGGNTVL NTKPWLIDQE DRKAMADFVQ YWLDLTSGSN
     STLSYITPGA TVDDILATKM ISGDHWMGSA KMGVDDGRKA NGSAVVDLNT KVYGTDNLFV
     VDASMHPDLP TGNTQAIIMV AAEHAAEKIA ALKVGGSNST VPEPISSAPT PVPTPGSKCK
     RGLRHRRAAR VPMDFRRRSL Y
//