ID A0A3M7M6A7_9PLEO Unreviewed; 339 AA.
AC A0A3M7M6A7;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 05-FEB-2025, entry version 17.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|RuleBase:RU362068};
GN ORFNames=GMOD_00000038 {ECO:0000313|EMBL:RMZ70006.1};
OS Pyrenophora seminiperda CCB06.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=1302712 {ECO:0000313|EMBL:RMZ70006.1, ECO:0000313|Proteomes:UP000265663};
RN [1] {ECO:0000313|EMBL:RMZ70006.1, ECO:0000313|Proteomes:UP000265663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCB06 {ECO:0000313|EMBL:RMZ70006.1,
RC ECO:0000313|Proteomes:UP000265663};
RC TISSUE=Mycelium {ECO:0000313|EMBL:RMZ70006.1};
RX PubMed=24475219; DOI=10.1371/journal.pone.0087045;
RA Soliai M.M., Meyer S.E., Udall J.A., Elzinga D.E., Hermansen R.A.,
RA Bodily P.M., Hart A.A., Coleman C.E.;
RT "De novo Genome Assembly of the Fungal Plant Pathogen Pyrenophora
RT semeniperda.";
RL PLoS ONE 9:E87045-E87045(2014).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + NADPH + H(+);
CC Xref=Rhea:RHEA:16233, ChEBI:CHEBI:11561, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15980, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC EC=1.1.1.169; Evidence={ECO:0000256|RuleBase:RU362068};
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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DR EMBL; KE747824; RMZ70006.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M7M6A7; -.
DR OrthoDB; 3609at2759; -.
DR Proteomes; UP000265663; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:InterPro.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR FunFam; 3.40.50.720:FF:000609; 2-dehydropantoate 2-reductase; 1.
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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708:SF26; 2-DEHYDROPANTOATE 2-REDUCTASE; 1.
DR PANTHER; PTHR21708; PROBABLE 2-DEHYDROPANTOATE 2-REDUCTASE; 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, ECO:0000256|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Reference proteome {ECO:0000313|Proteomes:UP000265663}.
FT DOMAIN 5..158
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 201..327
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 339 AA; 37215 MW; 15471570F40175A2 CRC64;
MPIHILIVGA GAIGAFYASR LAVVPGISVS VICRSNYKAV KANGFQVTSP QYGDYTFVPA
NTFANPEEAR KSAIEWDYIV VSTKALPDVS DDSTILEGLV SDKTAIVLIQ NGLGVEEPYA
KRFPQAAICS AVTIATCAQP EHGQIKHNRW TRINSGPYLP HLDTGEAKPT DAHITEQNDA
FIALLKEGGI KDAEAYSHAK LQLVRWHKIA INASMNPTSV LTMCLPNNVM SLDPELQRHL
KGVMNEILET APKILGQPMP KEFATPDAII RSTQKNTSGS RPSMAVDWKA GKKMEIEVIL
GNPLRIARAR GYEMPRLQSL YAMVRMAQEV RDQKKDIKL
//
