ID J1EPJ4_9BURK Unreviewed; 325 AA.
AC J1EPJ4;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=PMI14_01021 {ECO:0000313|EMBL:EJE54059.1};
OS Acidovorax sp. CF316.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1144317 {ECO:0000313|EMBL:EJE54059.1, ECO:0000313|Proteomes:UP000004811};
RN [1] {ECO:0000313|EMBL:EJE54059.1, ECO:0000313|Proteomes:UP000004811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF316 {ECO:0000313|EMBL:EJE54059.1,
RC ECO:0000313|Proteomes:UP000004811};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(R)-pantoate + NADP(+) = 2-dehydropantoate + H(+) + NADPH;
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:ARBA00000784};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994}.
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:EJE54059.1}.
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DR EMBL; AKJX01000038; EJE54059.1; -; Genomic_DNA.
DR RefSeq; WP_007850521.1; NZ_AKJX01000038.1.
DR AlphaFoldDB; J1EPJ4; -.
DR PATRIC; fig|1144317.3.peg.961; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000004811; Unassembled WGS sequence.
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 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; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR21708:SF42; 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 4: Predicted;
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000004811}.
FT DOMAIN 4..105
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 325 AA; 33590 MW; 3E53E73730092DB7 CRC64;
MKACIYGAGA IGGWIGLALA QAGSEVSLVA RGATLAALQE HGLRLRRPDG SVAATPVRAS
DSPAALGVQD LVVIAVKAPG LPEVARALAP LIGPQTVVLT AMNGVPWWFL DGCGGAAQGR
TLESVDPGGA IARAIPAGQV LGSVVHTSCS LEAPGFVKQH FGNRLIVGEP DGSASPRLQA
LADALQRGGI EVETSTNIQK DIWFKLWGNL TVNPISALTG ATTDRILDDD LVRGFVSAVM
LEAKAIGAKL GLPIDQQPED RHAVTRKLGA FKTSMLQDVE AGKPVEIDAL VGAVHELGQI
TGIPTPHTAA LLGLSRLMAR TRGLY
//
