ID   F9G173_FUSOF            Unreviewed;       465 AA.
AC   F9G173;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=FOXB_12405 {ECO:0000313|EMBL:EGU77107.1};
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:EGU77107.1};
RN   [1] {ECO:0000313|EMBL:EGU77107.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU77107.1};
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 ketopantoate reductase family.
CC       {ECO:0000256|ARBA:ARBA00007870}.
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:EGU77107.1}.
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DR   EMBL; AFQF01003065; EGU77107.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9G173; -.
DR   STRING; 660025.F9G173; -.
DR   PaxDb; 5507-FOXG_03586P0; -.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR   InterPro; IPR008927; 6-PGluconate_DH-like_C_sf.
DR   InterPro; IPR013328; 6PGD_dom2.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   PANTHER; PTHR43765; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE-RELATED; 1.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; 6-phosphogluconate dehydrogenase C-terminal domain-like; 1.
PE   3: Inferred from homology;
FT   DOMAIN          146..256
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          305..428
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
FT   REGION          31..74
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        52..74
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   465 AA;  52680 MW;  0477F2B1000F48BD CRC64;
     MQPRATAQIG RKSTRWLRNS PNFGYTRLFA SAVPPTEQKK PEAVPPELGS APSRPWQSSS
     IQAGSVTPTS TSPSSQFYVP SVVIPAEAAK SGPVHKIHIL GEDVRSRFIA HALCSVYDSV
     ETVPFREMPK SRYRNVEKVQ PERTRKNAYV EKNAAMPKDD VVPQSDRSHI DELIVTGRGF
     EAVKAIVSVK DRIDDKTSIC LLNDGMGVLE RVREEIFDGT QPEPNFYLGH MSHALGFNRN
     RDSVKQFKSG RTVFTKADPV LNAEKELYIP AEQQPSMMHS LRRVKELNTT FSTYEHWLRF
     KLPSIMFTAA VEPVCVLLDL PYQGLLENRN AQKMMNQLLG EMALVTENMP EVQDSPDLIK
     FLRGEGLKKF CYRRITGKSN APSDLLTRIN KGLQTDINYQ NGYFLKRARI LGIDTPTNQL
     MVQMIKARRI EQQQKLRSII PVQEASPNDV RKKTQRRMLK NGLLL
//