ID F9G713_FUSOF Unreviewed; 514 AA.
AC F9G713;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=Pyranose:oxygen 2-oxidoreductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FOXB_14445 {ECO:0000313|EMBL:EGU75039.1};
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:EGU75039.1};
RN [1] {ECO:0000313|EMBL:EGU75039.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU75039.1};
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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:EGU75039.1}.
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DR EMBL; AFQF01003568; EGU75039.1; -; Genomic_DNA.
DR AlphaFoldDB; F9G713; -.
DR STRING; 660025.F9G713; -.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR Gene3D; 3.30.410.40; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000172; GMC_OxRdtase_N.
DR InterPro; IPR007867; GMC_OxRtase_C.
DR PANTHER; PTHR42784; PYRANOSE 2-OXIDASE; 1.
DR PANTHER; PTHR42784:SF1; PYRANOSE 2-OXIDASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 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|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
FT DOMAIN 20..56
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 277..328
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00732"
FT DOMAIN 379..501
FT /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF05199"
SQ SEQUENCE 514 AA; 57478 MW; F66F7F8D0C14D94B CRC64;
MVHKPTPSPS SASDAVRWEE TDVLIVGSGP IGATFAHTLV KKGIKVTMID IGQQETRRIG
DHKKNSVAVQ KDISLFTNET LTHSVPRENC THSLCQLTRR DLSWNRPPGL LGRVMHSHDR
DYAKVKRPTD SAYVLNGQNP DQKSYGNLPA AAATRVVGGM GSHWTCCTPR QHKGIERSDL
FSDGEWNTLY GRAEKLFTKT DDAFDDSVRQ NLVKRVLTEA YPDREMKSMP LACKRKHDNK
EYVEWSCTAT ILGELSKPEY FYKGEERLFD MRPNTQCDKL ELDPDGQIAW ALINDLEANQ
QYYIHAKKYV VCAGAVLTPG ILHKSGLKPR LPALVYFPLS EKYPWHTQIH RDAFGYGEVP
SNIDQRLVVD LRWFGYMKPD QENYVTFSNK TKDQFGMPQP TFNFVLDEEA DERCKRMITD
MIEVARKLGG FLPGAEPKYL APGSALHICG TYRAGSTPAD SVVNKNGKAW GVNDLVLGGC
GVIPTQNACN PTLTAACFAL AAADKIIEDL HVDQ
//
