ID S0E533_GIBF5 Unreviewed; 463 AA.
AC S0E533;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 02-APR-2025, entry version 40.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0008006|Google:ProtNLM};
GN ORFNames=FFUJ_05716 {ECO:0000313|EMBL:CCT69800.1};
OS Gibberella fujikuroi (strain CBS 195.34 / IMI 58289 / NRRL A-6831) (Bakanae
OS and foot rot disease fungus) (Fusarium fujikuroi).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=1279085 {ECO:0000313|EMBL:CCT69800.1, ECO:0000313|Proteomes:UP000016800};
RN [1] {ECO:0000313|Proteomes:UP000016800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 195.34 / IMI 58289 / NRRL A-6831
RC {ECO:0000313|Proteomes:UP000016800};
RX PubMed=23825955; DOI=10.1371/journal.ppat.1003475;
RA Wiemann P., Sieber C.M., von Bargen K.W., Studt L., Niehaus E.M.,
RA Espino J.J., Huss K., Michielse C.B., Albermann S., Wagner D.,
RA Bergner S.V., Connolly L.R., Fischer A., Reuter G., Kleigrewe K., Bald T.,
RA Wingfield B.D., Ophir R., Freeman S., Hippler M., Smith K.M., Brown D.W.,
RA Proctor R.H., Munsterkotter M., Freitag M., Humpf H.U., Guldener U.,
RA Tudzynski B.;
RT "Deciphering the cryptic genome: genome-wide analyses of the rice pathogen
RT Fusarium fujikuroi reveal complex regulation of secondary metabolism and
RT novel metabolites.";
RL PLoS Pathog. 9:E1003475-E1003475(2013).
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; HF679028; CCT69800.1; -; Genomic_DNA.
DR RefSeq; XP_023431880.1; XM_023578959.1.
DR AlphaFoldDB; S0E533; -.
DR STRING; 1279085.S0E533; -.
DR EnsemblFungi; CCT69800; CCT69800; FFUJ_05716.
DR GeneID; 35399195; -.
DR VEuPathDB; FungiDB:FFUJ_05716; -.
DR HOGENOM; CLU_031468_3_0_1; -.
DR Proteomes; UP000016800; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:TreeGrafter.
DR GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR Gene3D; 1.10.1040.10; N-(1-d-carboxylethyl)-l-norvaline Dehydrogenase, domain 2; 1.
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; IPR050838; Ketopantoate_reductase.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR43765:SF2; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR43765; 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.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000016800}.
FT DOMAIN 146..255
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 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..163
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..11
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..75
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 463 AA; 52362 MW; 9D094BCA758F6E3D CRC64;
MQTRPTTQIA RKSTRWLRGS PSFGYTRLFA SAVPPTEQKK PEAVPPELGS TPSRPWKSSS
TQAGSVTPTS TSPSSQFYVP SVVIPAEAAK SGPVHKIHIL GEDVRSRFIA HALCSVYDSV
ETVPFREMPK SRYRNIEKVQ PERTRKSAYV EKNAATPESD AVAQSDRSHI DELIVTGRGF
EAVKAIASIK DRIDDKTSIC LLNDGMGVLE QVREQLFNGT QPEPNFYLGH MSHALAFNRN
RDSVKELRSG RTVFTKADPV LTAEKELYIP VEQQPSMMHS LRRVKELNTT FSNYEHWLRF
KLPSVMFTAA VEPVCVLLDL SYQGLLENGN AQRMMNKLLG EMAIVTENMP EVQNSPDLIK
FLRGEGLKKF CYRRITGKSK APSDLLTRIS KGLQTDINYQ NGYFLKRARI LGIDTPTNQL
MVQMIKARRI EQNKKLRSFI PIQEASPNDV RKKFQHKFKN DFL
//
