ID A0A0B6S0M0_BURPL Unreviewed; 344 AA.
AC A0A0B6S0M0;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 18-JUN-2025, entry version 38.
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 Name=panE3 {ECO:0000313|EMBL:AJK49203.1};
GN ORFNames=BGL_2c11250 {ECO:0000313|EMBL:AJK49203.1};
OS Burkholderia plantarii.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=41899 {ECO:0000313|EMBL:AJK49203.1, ECO:0000313|Proteomes:UP000031838};
RN [1] {ECO:0000313|Proteomes:UP000031838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1 {ECO:0000313|Proteomes:UP000031838};
RA Voget S., Streit W.R., Jaeger K.E., Daniel R.;
RL Submitted (MAR-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AJK49203.1, ECO:0000313|Proteomes:UP000031838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1 {ECO:0000313|EMBL:AJK49203.1,
RC ECO:0000313|Proteomes:UP000031838};
RX PubMed=26476653;
RA Knapp A., Voget S., Gao R., Zaburannyi N., Krysciak D., Breuer M.,
RA Hauer B., Streit W.R., Muller R., Daniel R., Jaeger K.E.;
RT "Mutations improving production and secretion of extracellular lipase by
RT Burkholderia glumae PG1.";
RL Appl. Microbiol. Biotechnol. 100:1265-1273(2016).
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; CP002581; AJK49203.1; -; Genomic_DNA.
DR RefSeq; WP_052498433.1; NZ_CP002581.1.
DR AlphaFoldDB; A0A0B6S0M0; -.
DR KEGG; bgp:BGL_2c11250; -.
DR HOGENOM; CLU_031468_6_1_4; -.
DR UniPathway; UPA00028; UER00004.
DR Proteomes; UP000031838; Chromosome 2.
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.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:AJK49203.1};
KW Pantothenate biosynthesis {ECO:0000256|ARBA:ARBA00022655};
KW Reference proteome {ECO:0000313|Proteomes:UP000031838}.
FT DOMAIN 23..126
FT /note="Ketopantoate reductase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02558"
FT DOMAIN 218..337
FT /note="Ketopantoate reductase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF08546"
SQ SEQUENCE 344 AA; 35250 MW; 79BBD9DDB6EC2A34 CRC64;
MSQTPSRQAP LPTTGGAAPA RRIGIVGIGA IGGHFAARLA LAGHRVSALA RGATLRALAD
TGLRYTGAGD DAERVIAIEA HQHAEAMGEQ DLLVIALKSQ ALPGLAASLA PLVGPHTVVL
PVGNGLPWWF CLPAGGPLAG LRLASVDPDG AIERTLPFAQ VLGGSVMASC SSPAPGVVRH
HSGNRITIGE PAGGGSERAA GWATLLSDAG LPTVASDDIR RDLWIKLLGN ACSNPLSVLT
QAGTDRLVND AGTLAVYERL MGECLAIGRA AGLTIEIDIA QRIAQTRQLG AVKTSMLQDL
EAGRSLELDA ILGAPLECAA RLGIDAPWLR AIEALTRLRA NAAP
//
