ID A0A1M7U5I1_9BRAD Unreviewed; 344 AA.
AC A0A1M7U5I1;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 18-JUN-2025, entry version 28.
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=SAMN05444170_3632 {ECO:0000313|EMBL:SHN78289.1};
OS Bradyrhizobium erythrophlei.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1437360 {ECO:0000313|EMBL:SHN78289.1, ECO:0000313|Proteomes:UP000184096};
RN [1] {ECO:0000313|Proteomes:UP000184096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GAS401 {ECO:0000313|Proteomes:UP000184096};
RA Varghese N., Submissions S.;
RL Submitted (NOV-2016) 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; LT670849; SHN78289.1; -; Genomic_DNA.
DR RefSeq; WP_072819684.1; NZ_LT670849.1.
DR AlphaFoldDB; A0A1M7U5I1; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000184096; Chromosome i.
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:UP000184096}.
FT DOMAIN 3..104
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 197..317
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 344 AA; 36620 MW; 6AB9C74BE825FD97 CRC64;
MKICVFGAGA IGGYMAGELA LAGHDVSAIA RGPHLAAVQS HGLKLIVDGQ TRTVDLPASD
DPAAFGPQDV VICALKAQQA HANAGAFAPL LGPKTAVLTA MNGIPWWYFY KEGGRHDGHH
LQSVDPGAAQ WNAIGPERAI GCVVDPACEV VAPGVIEHRL FKRFTIGEPD GSTSDRILAL
RDALVSAGFD APIRDTIRWS IWLKLWGNVC FNPISALTLA TLDRVTSEPG LRALCKSIMA
EAEAITASLG LTIPKQMMER RLNAAGSVIG HKISMLQDLE RGRSMEIDAL VTAVQEMGRL
VKIATPTIDA VLALVQERGR QAGLYSNDIS QVDGNDACSD YRLD
//