ID A0A848H3B3_9BURK Unreviewed; 335 AA.
AC A0A848H3B3;
DT 29-SEP-2021, integrated into UniProtKB/TrEMBL.
DT 29-SEP-2021, sequence version 1.
DT 18-JUN-2025, entry version 15.
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=HHL11_16195 {ECO:0000313|EMBL:NML45295.1};
OS Ramlibacter agri.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Ramlibacter.
OX NCBI_TaxID=2728837 {ECO:0000313|EMBL:NML45295.1, ECO:0000313|Proteomes:UP000541185};
RN [1] {ECO:0000313|EMBL:NML45295.1, ECO:0000313|Proteomes:UP000541185}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G-1-2-2 {ECO:0000313|EMBL:NML45295.1,
RC ECO:0000313|Proteomes:UP000541185};
RA Dahal R.H.;
RT "Ramlibacter sp. G-1-2-2 isolated from soil.";
RL Submitted (APR-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}.
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:NML45295.1}.
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DR EMBL; JABBFX010000001; NML45295.1; -; Genomic_DNA.
DR RefSeq; WP_169419375.1; NZ_JABBFX010000001.1.
DR AlphaFoldDB; A0A848H3B3; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000541185; Unassembled WGS sequence.
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:UP000541185}.
FT DOMAIN 3..171
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 335 AA; 35739 MW; 211ABDD1986BA663 CRC64;
MKIAIIGAGA IGGYVGARLA LAGEDVTFLA RGANLQALRA NGITLRQEGS EQVARNIRAT
NDYGEAGPQD IVVLATKAHQ VAAVAGELPK LFGPDTVVVT MQNGIPFWYF HRLGGPMEGT
AVRSVDADGS LARRIPPERV LGCVVYPATE LVAPGVVRHI EGDRFPLGEL DGSSSERVHR
VAGCFVRAGL KAPVLDDIRA EIWLKLWGNL TFNPISALTH ATLVDICQDP LARSLAADMM
REAQAVAGKL GITFRVPLDK RIAGAEKVGK HKTSMLQDVE AGREPEIDAL VGSVVELARL
TDTPTPHIDA LYALVKLLAK TMGENGHARV RMESV
//
