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Database: UniProt
Entry: A0A428QKR2_9HYPO
LinkDB: A0A428QKR2_9HYPO
Original site: A0A428QKR2_9HYPO 
ID   A0A428QKR2_9HYPO        Unreviewed;       384 AA.
AC   A0A428QKR2;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   05-FEB-2025, entry version 18.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00013014};
DE            EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE   AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN   ORFNames=CEP54_004066 {ECO:0000313|EMBL:RSL65903.1};
OS   Fusarium duplospermum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium solani species complex.
OX   NCBI_TaxID=1325734 {ECO:0000313|EMBL:RSL65903.1, ECO:0000313|Proteomes:UP000288168};
RN   [1] {ECO:0000313|EMBL:RSL65903.1, ECO:0000313|Proteomes:UP000288168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL62584 {ECO:0000313|EMBL:RSL65903.1,
RC   ECO:0000313|Proteomes:UP000288168};
RA   Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA   Kasson M.;
RT   "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:RSL65903.1}.
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DR   EMBL; NKCI01000027; RSL65903.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428QKR2; -.
DR   STRING; 1325734.A0A428QKR2; -.
DR   OrthoDB; 73846at2759; -.
DR   Proteomes; UP000288168; Unassembled WGS sequence.
DR   GO; GO:0005739; C:mitochondrion; IEA:TreeGrafter.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:InterPro.
DR   GO; GO:0050661; F:NADP binding; IEA:TreeGrafter.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
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; IPR003710; ApbA.
DR   InterPro; IPR050838; Ketopantoate_reductase.
DR   InterPro; IPR013752; KPA_reductase.
DR   InterPro; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   NCBIfam; TIGR00745; apbA_panE; 1.
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:UP000288168}.
FT   DOMAIN          35..207
FT                   /note="Ketopantoate reductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02558"
FT   DOMAIN          245..370
FT                   /note="Ketopantoate reductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08546"
SQ   SEQUENCE   384 AA;  42746 MW;  D2CC195E21806FD8 CRC64;
     MTWSRRVSLC GLHTYLSTSF ILTRTMTVKA RQPRVHVLGL GSIGTFAAHS LAEVPPPLTP
     SITLLLHRPS LVDNFVGSGS KITIETREGD IIEHGNYNLE VWQDEQWHRH ESTQLGPVTD
     EVIDNLIVST KATQTASALR PLKHRLNASS YVLFLQNGSG MIEDVNKHVF TDEETRPNYI
     TGVTSHGVTL NSPFNIVHTG FAATSLSLVP RSGKGVENTG FTPYLLEALP LVPRLNATSY
     TFLDVFQIQL EKLTVNAFCN PLCALNDAKN GFLFTIPETR RAILTEISQV VYALPELRGV
     PGVLERFSVD RLEATVNGII QKTAETTCSM VVDLRRGQKT EIEFINGYWC RRGRKVGVPT
     PINDDLVRQI LHRQGDEELA KNYQ
//
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