2-dehydropantoate 2-reductase (P0A9J4)

Identification
Name:2-dehydropantoate 2-reductase
Synonyms:
  • Ketopantoate reductase
  • KPA reductase
  • KPR
Gene Name:panE
Enzyme Class:
Biological Properties
General Function:Involved in oxidation-reduction process
Specific Function:Catalyzes the NADPH-dependent reduction of ketopantoate into pantoic acid
Cellular Location:Cytoplasm (Potential)
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Dehydropantoate + 1.0Hydrogen ion + 1.0NADPH ↔ 1.0NADP + 1.0(R)-Pantoate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0(R)-Pantoate + 1.0NADP ↔ 1.02-Dehydropantoate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
SMPDB Reactions:
1.02-dehydropantoate+1.0NADPH+1.0Thumb+1.0Thumb+1.0Thumb → 1.0Thumb+1.0(R)-pantoate+1.0Thumb
1.02-dehydropantoate + 1.0NADPH + 1.0Hydrogen ion + 1.02-Dehydropantoate + 1.0NADPH → 1.0NADP + 1.0(R)-pantoate + 1.0(R)-Pantoate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Dehydropantoate + 1.0Hydrogen ion + 1.0NADPH ↔ 1.0NADP + 1.0(R)-Pantoate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0(R)-Pantoate + 1.0NADP ↔ 1.02-Dehydropantoate + 1.0NADPH + 1.0Hydrogen ion
ReactionCard
1.0Thumb+1.0Thumb ← 1.0Thumb+1.0Thumb+1.0Thumb
1.0(R)-Pantoate + 1.0NADP ← 1.0Hydrogen ion + 1.02-Dehydropantoate + 1.0NADPH
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0(R)-Pantoate + 1.0NADP → 1.02-Dehydropantoate + 1.0NADPH
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB20016(R)-PantoateMetaboCard
ECMDB040432-DehydropantoateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00217NADPMetaboCard
ECMDB04111NADPHMetaboCard
GO Classification:
Component
cell part
cytoplasm
intracellular part
Function
binding
catalytic activity
coenzyme binding
cofactor binding
NADP or NADPH binding
nucleotide binding
oxidoreductase activity
Process
cellular metabolic process
coenzyme biosynthetic process
coenzyme metabolic process
cofactor metabolic process
metabolic process
oxidation reduction
pantothenate biosynthetic process
Gene Properties
Blattner:b0425
Gene OrientationCounterclockwise
Centisome Percentage:9.54
Left Sequence End442828
Right Sequence End443739
Gene Sequence:
>912 bp
ATGAAAATTACCGTATTGGGATGCGGTGCCTTAGGGCAATTATGGCTTACAGCACTTTGC
AAACAGGGTCATGAAGTTCAGGGCTGGCTGCGCGTACCGCAACCTTATTGTAGCGTGAAT
CTGGTTGAGACAGATGGTTCGATATTTAACGAATCGCTGACCGCCAACGATCCCGATTTT
CTCGCCACCAGCGATCTGCTCCTGGTGACGCTGAAAGCATGGCAGGTTTCCGATGCCGTC
AAAAGCCTCGCGTCCACACTGCCTGTAACTACGCCAATACTGTTAATTCACAACGGCATG
GGCACCATCGAAGAGTTGCAAAACATTCAGCAGCCATTACTGATGGGCACCACCACCCAT
GCAGCCCGCCGCGACGGCAATGTCATTATTCATGTGGCAAACGGTATCACGCATATTGGC
CCGGCACGGCAACAGGACGGGGATTACAGTTATCTGGCGGATATTTTGCAAACCGTGTTG
CCTGACGTTGCCTGGCATAACAATATTCGCGCCGAGCTGTGGCGCAAGCTGGCAGTCAAC
TGCGTGATTAATCCACTGACTGCCATCTGGAATTGCCCGAACGGTGAATTACGTCATCAT
CCGCAAGAAATTATGCAGATATGCGAAGAAGTCGCGGCGGTGATCGAACGCGAAGGGCAT
CATACTTCAGCAGAAGATTTGCGTGATTACGTGATGCAGGTGATTGATGCCACAGCGGAA
AATATCTCGTCGATGTTGCAGGATATCCGCGCGCTGCGCCACACTGAAATCGACTATATC
AATGGTTTTCTCTTACGCCGCGCCCGCGCGCATGGGATTGCCGTACCGGAAAACACCCGC
CTGTTTGAAATGGTAAAAAGAAAGGAGAGTGAATATGAGCGCATCGGCACTGGTTTGCCT
CGCCCCTGGTAG
Protein Properties
Pfam Domain Function:
Protein Residues:303
Protein Molecular Weight:33871
Protein Theoretical pI:6
PDB File:1KS9
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>2-dehydropantoate 2-reductase
MKITVLGCGALGQLWLTALCKQGHEVQGWLRVPQPYCSVNLVETDGSIFNESLTANDPDF
LATSDLLLVTLKAWQVSDAVKSLASTLPVTTPILLIHNGMGTIEELQNIQQPLLMGTTTH
AARRDGNVIIHVANGITHIGPARQQDGDYSYLADILQTVLPDVAWHNNIRAELWRKLAVN
CVINPLTAIWNCPNGELRHHPQEIMQICEEVAAVIEREGHHTSAEDLRDYVMQVIDATAE
NISSMLQDIRALRHTEIDYINGFLLRRARAHGIAVPENTRLFEMVKRKESEYERIGTGLP
RPW
References
External Links:
ResourceLink
Uniprot ID:P0A9J4
Uniprot Name:PANE_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674565
PDB ID:1KS9
Ecogene ID:EG13271
Ecocyc:EG13271
ColiBase:b0425
Kegg Gene:b0425
EchoBASE ID:EB3056
CCDB:PANE_ECOLI
BacMap:16128410
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Ciulli, A., Abell, C. (2005). "Biophysical tools to monitor enzyme-ligand interactions of enzymes involved in vitamin biosynthesis." Biochem Soc Trans 33:767-771. Pubmed: 16042595
  • Ciulli, A., Chirgadze, D. Y., Smith, A. G., Blundell, T. L., Abell, C. (2007). "Crystal structure of Escherichia coli ketopantoate reductase in a ternary complex with NADP+ and pantoate bound: substrate recognition, conformational change, and cooperativity." J Biol Chem 282:8487-8497. Pubmed: 17229734
  • Ciulli, A., Lobley, C. M., Tuck, K. L., Smith, A. G., Blundell, T. L., Abell, C. (2007). "pH-tuneable binding of 2'-phospho-ADP-ribose to ketopantoate reductase: a structural and calorimetric study." Acta Crystallogr D Biol Crystallogr 63:171-178. Pubmed: 17242510
  • Ciulli, A., Williams, G., Smith, A. G., Blundell, T. L., Abell, C. (2006). "Probing hot spots at protein-ligand binding sites: a fragment-based approach using biophysical methods." J Med Chem 49:4992-5000. Pubmed: 16884311
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Lobley, C. M., Ciulli, A., Whitney, H. M., Williams, G., Smith, A. G., Abell, C., Blundell, T. L. (2005). "The crystal structure of Escherichia coli ketopantoate reductase with NADP+ bound." Biochemistry 44:8930-8939. Pubmed: 15966718
  • Matak-Vinkovic, D., Vinkovic, M., Saldanha, S. A., Ashurst, J. L., von Delft, F., Inoue, T., Miguel, R. N., Smith, A. G., Blundell, T. L., Abell, C. (2001). "Crystal structure of Escherichia coli ketopantoate reductase at 1.7 A resolution and insight into the enzyme mechanism." Biochemistry 40:14493-14500. Pubmed: 11724562
  • Zheng, R., Blanchard, J. S. (2000). "Identification of active site residues in E. coli ketopantoate reductase by mutagenesis and chemical rescue." Biochemistry 39:16244-16251. Pubmed: 11123955
  • Zheng, R., Blanchard, J. S. (2000). "Kinetic and mechanistic analysis of the E. coli panE-encoded ketopantoate reductase." Biochemistry 39:3708-3717. Pubmed: 10736170