ID A0A858SRS6_9RHOB Unreviewed; 327 AA.
AC A0A858SRS6;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, 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=G3256_05265 {ECO:0000313|EMBL:QJF50608.1};
OS Roseobacter ponti.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Rhodobacterales; Roseobacteraceae; Roseobacter.
OX NCBI_TaxID=1891787 {ECO:0000313|EMBL:QJF50608.1, ECO:0000313|Proteomes:UP000503308};
RN [1] {ECO:0000313|EMBL:QJF50608.1, ECO:0000313|Proteomes:UP000503308}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 106830 {ECO:0000313|EMBL:QJF50608.1,
RC ECO:0000313|Proteomes:UP000503308};
RA Hollensteiner J., Schneider D., Poehlein A., Daniel R.;
RT "Genome sequence of Roseobacter ponti.";
RL Submitted (FEB-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; CP048788; QJF50608.1; -; Genomic_DNA.
DR RefSeq; WP_169639826.1; NZ_CP048788.1.
DR AlphaFoldDB; A0A858SRS6; -.
DR KEGG; rpon:G3256_05265; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000503308; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
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:UP000503308}.
FT DOMAIN 3..170
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..316
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 327 AA; 34630 MW; E4A8F98C63298199 CRC64;
MKICIFGAGA IGGYMGVKLA QAGADVSLVA RGPHLAAMKA SGLSLIEEGE KTTVEVNASD
DPADLGVQDY VIVTLKAHSV PPVVPKMQPL IGPQTTIVSG VNGVPWWYFH KLGGPLEGTR
LETVDPGNAQ WDGFGPDQVL GCVVYPAAEV SEPGVVRHIE GNRFSLGEPD GSRSDRAKAL
SEALSSAGLK APVRPRLRDE IWVKLWGNLS FNPISALTHA TLDVLCTDPG TRAVARDMMI
EAQQIAEKLG VKFPIDVDRR IDGGAAVGAH RTSMLQDLDA GRPMEIDALL GSVQELGRIT
DTETPVIDTV LALTKLRAKT AGLYGQT
//
