ID A0A515DGA1_9BURK Unreviewed; 330 AA.
AC A0A515DGA1;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 18-JUN-2025, entry version 20.
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=EUB48_20540 {ECO:0000313|EMBL:QDL39446.1};
OS Rhodoferax sediminis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Comamonadaceae; Rhodoferax.
OX NCBI_TaxID=2509614 {ECO:0000313|EMBL:QDL39446.1, ECO:0000313|Proteomes:UP000316798};
RN [1] {ECO:0000313|EMBL:QDL39446.1, ECO:0000313|Proteomes:UP000316798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHu59-6-5 {ECO:0000313|EMBL:QDL39446.1,
RC ECO:0000313|Proteomes:UP000316798};
RA Jin L.;
RT "Genomic insights into a novel species Rhodoferax sp.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP035503; QDL39446.1; -; Genomic_DNA.
DR RefSeq; WP_142820914.1; NZ_CP035503.1.
DR AlphaFoldDB; A0A515DGA1; -.
DR KEGG; rhf:EUB48_20540; -.
DR OrthoDB; 9796561at2; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000316798; Chromosome.
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 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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000316798}.
FT DOMAIN 10..175
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 203..322
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 330 AA; 34594 MW; C56BA7BAA537CA0E CRC64;
MTEKVISKAC IYGAGAIGGW IGAGLAGAGC RLSVVARGAT LQALQQHGLR VQRGDAVTAT
PVQASSDPFD LGVQDLVVIA VKAPALLDVA RQIGPLIGRD TIVLTAMNGV PWWFLQGFGG
AYAGTRLQAV DATGEIAQAI PASHVVGCVV HASCSLNAPG FVNHRFGNTL IVGEPSGAVT
ARVQQLAALL QRAGIDTVIA EQIQKDTWYK LWGNMTVNPI SLLTGATTDL IMGDELVRNF
ISSVMLEARE IGARIGVPIA ERPEDRHAVT MKLGAFKTSM LQDVEAGRAV ELDALVTVVR
ELGQITGVAT PYTDALLGLA RLRARGLGLY
//
