ID R4WXK9_9BURK Unreviewed; 308 AA.
AC R4WXK9;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=2-dehydropantoate 2-reductase {ECO:0000256|ARBA:ARBA00019465, ECO:0000256|RuleBase:RU362068};
DE EC=1.1.1.169 {ECO:0000256|ARBA:ARBA00013014, ECO:0000256|RuleBase:RU362068};
DE AltName: Full=Ketopantoate reductase {ECO:0000256|ARBA:ARBA00032024, ECO:0000256|RuleBase:RU362068};
GN ORFNames=BRPE64_BCDS13290 {ECO:0000313|EMBL:BAN25990.1};
OS Caballeronia insecticola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN25990.1, ECO:0000313|Proteomes:UP000013966};
RN [1] {ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT Symbiont of the Bean Bug Riptortus pedestris.";
RL Genome Announc. 1:340-344(2013).
RN [2] {ECO:0000313|EMBL:BAN25990.1, ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RPE64 {ECO:0000313|EMBL:BAN25990.1};
RX PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA Peeters C., Kikuchi Y., Vandamme P.;
RT "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT bug Riptortus pedestris.";
RL Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of ketopantoate into
CC pantoic acid. {ECO:0000256|RuleBase:RU362068}.
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 ECO:0000256|RuleBase:RU362068};
CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis; (R)-
CC pantoate from 3-methyl-2-oxobutanoate: step 2/2.
CC {ECO:0000256|ARBA:ARBA00004994, ECO:0000256|RuleBase:RU362068}.
CC -!- SIMILARITY: Belongs to the ketopantoate reductase family.
CC {ECO:0000256|ARBA:ARBA00007870, ECO:0000256|RuleBase:RU362068}.
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; AP013059; BAN25990.1; -; Genomic_DNA.
DR AlphaFoldDB; R4WXK9; -.
DR STRING; 758793.BRPE64_BCDS13290; -.
DR KEGG; buo:BRPE64_BCDS13290; -.
DR PATRIC; fig|758793.3.peg.4238; -.
DR HOGENOM; CLU_031468_6_1_4; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000013966; Chromosome 2.
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; IPR003710; ApbA.
DR InterPro; IPR013752; KPA_reductase.
DR InterPro; IPR013332; KPR_N.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR NCBIfam; TIGR00745; apbA_panE; 1.
DR PANTHER; PTHR21708:SF26; 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|RuleBase:RU362068};
KW Oxidoreductase {ECO:0000256|RuleBase:RU362068};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655,
KW ECO:0000256|RuleBase:RU362068}.
FT DOMAIN 1..147
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 173..296
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 308 AA; 32442 MW; 2439923CB1AD71BC CRC64;
MGAGAIGGYF GARLLEAGRD VTFLVRERRA ERLRQCGLKV NSPEGDLAFQ CPPMVLAKDI
DGPYDLILLS CKAYDLQGAI DSFAPAVGPH TAILPLLNGM GHLDALDARF DPSNVLGGQC
VIAATLDAQG EILHLNNMHS MTIGERAGGR SARIDAIAAQ LGGAGFDLAV SDDILQSMWD
KWVFLATLAT GTCLMRAPVG DILEAPGGEA LLAQLFDECS GIAGDNAHPP GEAVVARARG
FFAERGSLMT ASMLRDLENG APIEADHIVG DLLARRRTPV AGLSALAVAY AHLKAYETRR
ARTSAAPR
//
