ID   PANE_LACLA              Reviewed;         312 AA.
AC   Q9CFY8;
DT   21-FEB-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 121.
DE   RecName: Full=2-dehydropantoate 2-reductase {ECO:0000250|UniProtKB:P0A9J4};
DE            EC=1.1.1.169 {ECO:0000250|UniProtKB:P0A9J4};
DE   AltName: Full=Ketopantoate reductase {ECO:0000250|UniProtKB:P0A9J4};
DE            Short=KPR {ECO:0000250|UniProtKB:P0A9J4};
GN   OrderedLocusNames=LL1323; ORFNames=L157055;
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403;
RX   PubMed=11337471; DOI=10.1101/gr.gr-1697r;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC       pantoic acid. {ECO:0000250|UniProtKB:P0A9J4}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
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:0000250|UniProtKB:P0A9J4};
CC   -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC       pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC       {ECO:0000250|UniProtKB:P0A9J4}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P0A9J4}.
CC   -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC       {ECO:0000305}.
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DR   EMBL; AE005176; AAK05421.1; -; Genomic_DNA.
DR   PIR; C86790; C86790.
DR   RefSeq; NP_267479.1; NC_002662.1.
DR   RefSeq; WP_010905887.1; NC_002662.1.
DR   AlphaFoldDB; Q9CFY8; -.
DR   SMR; Q9CFY8; -.
DR   STRING; 272623.L157055; -.
DR   PaxDb; Q9CFY8; -.
DR   EnsemblBacteria; AAK05421; AAK05421; L157055.
DR   KEGG; lla:L157055; -.
DR   PATRIC; fig|272623.7.peg.1427; -.
DR   eggNOG; COG1893; Bacteria.
DR   HOGENOM; CLU_031468_0_0_9; -.
DR   OMA; NYSSMYQ; -.
DR   UniPathway; UPA00028; UER00004.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008677; F:2-dehydropantoate 2-reductase activity; IEA:UniProtKB-EC.
DR   GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   Gene3D; 1.10.1040.10; -; 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; IPR013332; KPR_N.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   Pfam; PF02558; ApbA; 1.
DR   Pfam; PF08546; ApbA_C; 1.
DR   SUPFAM; SSF48179; SSF48179; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   TIGRFAMs; TIGR00745; apbA_panE; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; NADP; Oxidoreductase; Pantothenate biosynthesis;
KW   Reference proteome.
FT   CHAIN           1..312
FT                   /note="2-dehydropantoate 2-reductase"
FT                   /id="PRO_0000157313"
FT   ACT_SITE        187
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         7..12
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         105
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         131
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         195
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         260
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
FT   BINDING         273
FT                   /ligand="NADP(+)"
FT                   /ligand_id="ChEBI:CHEBI:58349"
FT                   /evidence="ECO:0000250|UniProtKB:P0A9J4"
SQ   SEQUENCE   312 AA;  34444 MW;  1C7FC4547F081BAD CRC64;
     MRITIAGAGA MGSRFGLMLH KGGNEVTLID GWPEHVKAIK EHGLRANYNG EELTAHLSVE
     LQSEISSKEK TDLIILFTKA MQLDKMLQDI KPLIDEHTKV LCLLNGIGHE DTIEKYVSKN
     NIFIGNTMWT AGLEGPGKAK LFGDGSVELQ NLISGEEETA KKLAEILSES GLNAKYSNNI
     HYSIYRKACV NGTMNGLCTI LDTNMAGLGE TKPAHDMVVT IVNEFAAVAK FENVNLDIAE
     VVQHVETCFD PSTIGLHYPS MYQDLIKNNR LTEIDYINGA VSRKGKKYNV ATPYCDFLTQ
     LVHSKEELLK AK