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Database: UniProt
Entry: A0A1M7U5I1_9BRAD
LinkDB: A0A1M7U5I1_9BRAD
Original site: A0A1M7U5I1_9BRAD 
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
//
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