ID A0A315AN02_9BURK Unreviewed; 338 AA.
AC A0A315AN02;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 18-JUN-2025, entry version 21.
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=B9Z51_11455 {ECO:0000313|EMBL:PUE09661.1};
OS Limnohabitans sp. T6-5.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Limnohabitans.
OX NCBI_TaxID=1100724 {ECO:0000313|EMBL:PUE09661.1, ECO:0000313|Proteomes:UP000251804};
RN [1] {ECO:0000313|EMBL:PUE09661.1, ECO:0000313|Proteomes:UP000251804}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T6-5 {ECO:0000313|EMBL:PUE09661.1,
RC ECO:0000313|Proteomes:UP000251804};
RA Kasalicky V., Mehrshad M., Andrei S.-A., Salcher M., Kratochvilova H.,
RA Simek K., Ghai R.;
RT "Unexpected and diverse lifestyles within the genus Limnohabitans.";
RL Submitted (APR-2017) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PUE09661.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NERV01000002; PUE09661.1; -; Genomic_DNA.
DR RefSeq; WP_108375017.1; NZ_NERV01000002.1.
DR AlphaFoldDB; A0A315AN02; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000251804; Unassembled WGS sequence.
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:UP000251804}.
FT DOMAIN 13..114
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 207..325
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 338 AA; 35012 MW; 81EC0236F68589DC CRC64;
MNDQGNDVKF NKIAIVGAGA IGGWIGVHLA QAGAQLSVLA RGDTLTALQK NGLQLHQGGT
LHTVPVTASN DAAALGVQDL VVISVKAPAL ASVAAQVGPL IGPHTVVLTA MNGVPWWFLQ
GFGGPVADRS LNSVDPDGTI ARALPAQHII GCVVHASCSV DAPGLIRHHF GDGLIVGEPS
GQATPRAQAL QALLQQAGFN ATLSPQIQKD IWYKLWGNMT VNPVSAITGA TTDLIMDDPL
VRAFISSVML EAKAIGACIG IPIEQQPEDR HVVTRKLGAF RTSMLQDVKA GKPVELDALV
GAVRELGQLT GVPTPFTDAL LGLSRLHARG LGLYPAGA
//
