ID F9FJ87_FUSOF Unreviewed; 638 AA.
AC F9FJ87;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE RecName: Full=Glucose-methanol-choline oxidoreductase N-terminal domain-containing protein {ECO:0000259|PROSITE:PS00624};
GN ORFNames=FOXB_06466 {ECO:0000313|EMBL:EGU83035.1};
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:EGU83035.1};
RN [1] {ECO:0000313|EMBL:EGU83035.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU83035.1};
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:EGU83035.1}.
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DR EMBL; AFQF01001985; EGU83035.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FJ87; -.
DR STRING; 660025.F9FJ87; -.
DR PaxDb; 5507-FOXG_01233P0; -.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..638
FT /note="Glucose-methanol-choline oxidoreductase N-terminal
FT domain-containing protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003383123"
FT DOMAIN 351..365
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
SQ SEQUENCE 638 AA; 69915 MW; 62D13D9B49CF81A3 CRC64;
MILNRLKFAL AAVLTGSSTT LATEPDIYDY VIIGSGPGGG SLAANLAREG HSVFLIEAGG
DNHTSILEQL PALARTAAET PGHSWQFFVN HYDDFDSARR DPKYTYIQTN GSYYVGLDPP
EGARPAGLYY PRGSTLGGSA QVNAMNFAWC PDNEWDHIAN LTGDSSWGHE HMRRHLMNIE
NCTYVPEGTP GHGFDGYLVN DQSNATVNIG SPNVANFFSQ MFRETEGIDV EDPAEMTELL
LRDLNGLDPR RYENGRMYST PVAIDPSTAA RSGAGIYINQ VIDAGHPLTV SFHSLATRVL
TKQGRNKKPR AYGVEYMVGE GLYSADGRYN PEQTGEILEV HAKHEVIVSG GAFNTPQILM
LSGIGPREEL EAWDIPVVVD LPAVGSNLHD NYEVPVQIRG EENWLIPRES PCTGTFDDED
PCFVLWRDNA SGPYAARDSS YGAVWRSSQS WDNDSDLMFL SSPGLSGLVG FYPGYSTGER
AGNDPAEWMH AVVKMQTSNS AGTVRLNSSD PRIRPNINFN YFTESAERDL DAIVEGIELL
RRAFDATGVP YTQLSPGPEN LRQSIQDLAF SHHASSTCAI GADDDENSCL DSRFRVRGVD
NLRVVDASVF PRSPGGMPNG PTWTISRKAF ETLLEDNH
//
