ID A0A6P2DZT6_9BURK Unreviewed; 325 AA.
AC A0A6P2DZT6;
DT 07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT 07-OCT-2020, sequence version 1.
DT 18-JUN-2025, entry version 16.
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=E5CHR_00242 {ECO:0000313|EMBL:VTU16875.1};
OS Variovorax sp. PBL-E5.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Variovorax.
OX NCBI_TaxID=434014 {ECO:0000313|EMBL:VTU16875.1, ECO:0000313|Proteomes:UP000464400};
RN [1] {ECO:0000313|EMBL:VTU16875.1, ECO:0000313|Proteomes:UP000464400}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PBL-E5 {ECO:0000313|EMBL:VTU16875.1};
RA Werner J.;
RL Submitted (APR-2019) 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; LR594671; VTU16875.1; -; Genomic_DNA.
DR RefSeq; WP_162590877.1; NZ_LR594671.1.
DR AlphaFoldDB; A0A6P2DZT6; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000464400; 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:UP000464400}.
FT DOMAIN 3..104
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 198..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 325 AA; 33687 MW; FECB09BAAB7B0B74 CRC64;
MKVCIYGAGA IGGWLGAKLA QAGCEIDVVA RGATLAALQR DGLALVSGGA RTAVPVRTSA
DPKALGVQQV VIVAVKAPAL PVVAEQIAPL LGPATIVLTA MNGVPWWFLQ GGFGGPLAGA
QLEAIDPGGR IDAAIPARHV IGGVVHASCS LDAPGVVRHH FGNGLIVGEP SGEATPRAQA
LCELLVRAGL DARLSPQIQK DIWYKLWGNM TVNPISALTG ATTDLILNDD LVRGFISAIM
LEARDIGARI GVPIAETPED RHAVTRKLGA FKTSMLQDVE AGRAVELDAL VSSVRELGQR
AGVPTPFTDA LLGLARLQAR QRGLY
//
