ID A0A7H0HCH7_9BURK Unreviewed; 325 AA.
AC A0A7H0HCH7;
DT 10-FEB-2021, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2021, sequence version 1.
DT 18-JUN-2025, entry version 17.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024};
GN ORFNames=H9L24_14370 {ECO:0000313|EMBL:QNP58243.1};
OS Paenacidovorax monticola.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Paenacidovorax.
OX NCBI_TaxID=1926868 {ECO:0000313|EMBL:QNP58243.1, ECO:0000313|Proteomes:UP000516057};
RN [1] {ECO:0000313|EMBL:QNP58243.1, ECO:0000313|Proteomes:UP000516057}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KACC 19171 {ECO:0000313|EMBL:QNP58243.1,
RC ECO:0000313|Proteomes:UP000516057};
RA Hyun D.-W., Bae J.-W.;
RT "Genome sequence of Acidovorax monticola KACC 19171T.";
RL Submitted (AUG-2020) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|ARBA:ARBA00002919}.
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|ARBA:ARBA00048793};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870}.
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DR EMBL; CP060790; QNP58243.1; -; Genomic_DNA.
DR RefSeq; WP_187735235.1; NZ_CP060790.1.
DR AlphaFoldDB; A0A7H0HCH7; -.
DR KEGG; amon:H9L24_14370; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000516057; Chromosome.
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:UniProtKB-UniPathway.
DR FunFam; 1.10.1040.10:FF:000017; 2-dehydropantoate 2-reductase; 1.
DR FunFam; 3.40.50.720:FF:000307; 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; IPR013752; KPA_reductase.
DR InterPro; IPR051402; KPR-Related.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; NF005089; PRK06522.1-4; 1.
DR PANTHER; PTHR21708:SF45; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000516057}.
FT DOMAIN 4..169
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..318
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 325 AA; 34233 MW; 02D29D5363D90F96 CRC64;
MKACIYGAGA IGGWLGLALA QAGSDVSLVA RGATLQALQA HGLRLTRPDG SQAQAAVRAS
DDPAALGVQD LVVIAVKAPA LPDVARRIAP LIGPGTMVLT AMNGVPWWFT EGCEGPARGQ
ALTSVDADGG IARAIPSGQV IGGVVHASCS LDGPGQVRQH FGNKLILGEP GGQDSERLVR
LAEWLARGGI EVERSPRIQR DIWFKLWGNL TMNPISALTG ATTDRILDDD LVRGFVSAVM
LEAKAIGARL GLPIDQQPED RHAVTRKLGA FKTSMLQDVE GRKPMEIDAL VGAVHELGRL
TQVPTPHTDA LLGLVRLMAR TRGLY
//
