ID F9FG47_FUSOF Unreviewed; 369 AA.
AC F9FG47;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=FAD dependent oxidoreductase domain-containing protein {ECO:0000259|Pfam:PF01266};
GN ORFNames=FOXB_05376 {ECO:0000313|EMBL:EGU84129.1};
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:EGU84129.1};
RN [1] {ECO:0000313|EMBL:EGU84129.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU84129.1};
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 DAMOX/DASOX family.
CC {ECO:0000256|ARBA:ARBA00006730}.
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:EGU84129.1}.
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DR EMBL; AFQF01001720; EGU84129.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FG47; -.
DR STRING; 660025.F9FG47; -.
DR GO; GO:0003884; F:D-amino-acid oxidase activity; IEA:InterPro.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0046416; P:D-amino acid metabolic process; IEA:InterPro.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR023209; DAO.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR PANTHER; PTHR11530; D-AMINO ACID OXIDASE; 1.
DR PANTHER; PTHR11530:SF16; D-AMINO ACID OXIDASE (AFU_ORTHOLOGUE AFUA_5G11290); 1.
DR Pfam; PF01266; DAO; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51971; Nucleotide-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 5..298
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
SQ SEQUENCE 369 AA; 41373 MW; E3DD6A7DD64EAE4F CRC64;
MPFFVVIGAG VVGLTTVLEL RSRYPEAKIV VAAKYLPGDS APEYASAWGG ANWFPAATDD
GRQREWEALT YRKFKELSSS QPECGIRPMN IRWHYENPIE ESGILTSATG KLWFEDLVGG
LEKIEKEDLP PGTAFGFEMA SFVIDVQRYL PWLQTEAIRL KIEIHRRIFG HIDEAFRMYP
QTTAVFNCTG LGAMSLGGVE DNTMFPARGQ ILLVQGPERP IEKMYFRAPH RAGEATHIFP
RGERGGVILG GCRQKNNWSG EVDYAFAEVI KRRCCSLVPE LGKPEDLKIV KHGVGLRQKV
VHAWSSKLEV ISSSSIIMVQ AEWDFKLLGV WHIATYGLDE AGIIQVARVV IWLSYLEIVD
FSACRIVIP
//
