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
//