Enolase (P0A6P9)

Identification
Name:Enolase
Synonyms:
  • 2-phospho-D-glycerate hydro-lyase
  • 2-phosphoglycerate dehydratase
Gene Name:eno
Enzyme Class:
Biological Properties
General Function:Involved in magnesium ion binding
Specific Function:Catalyzes the reversible conversion of 2- phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation
Cellular Location:Cytoplasm, cytoskeleton. Secreted. Cell surface.
SMPDB Pathways:
  • Gluconeogenesis from L-malic acid PW000819
  • fructose metabolism PW000913
  • glycerol metabolism PW000914
  • glycerol metabolism II PW000915
  • glycerol metabolism III (sn-glycero-3-phosphoethanolamine) PW000916
  • glycerol metabolism IV (glycerophosphoglycerol) PW000917
  • glycerol metabolism V (glycerophosphoserine) PW000918
  • glycolysis and pyruvate dehydrogenase PW000785
  • superpathway of D-glucarate and D-galactarate degradation PW000795
KEGG Pathways:
KEGG Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Phospho-D-glyceric acid ↔ 1.0Water + 1.0Phosphoenolpyruvic acid
ReactionCard
SMPDB Reactions:
1.0Thumb → 1.0Thumb+1.02-Phosphoglyceric acid+1.0Thumb
1.0Phosphoenolpyruvic acid → 1.0Water + 1.02-Phosphoglyceric acid + 1.02-Phosphoglyceric acid
ReactionCard
1.02-Phosphoglyceric acid+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Phosphoglyceric acid + 1.02-Phosphoglyceric acid ↔ 1.0Water + 1.0Phosphoenolpyruvic acid
ReactionCard
EcoCyc Reactions:
1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.02-Phospho-D-glyceric acid ↔ 1.0Water + 1.0Phosphoenolpyruvic acid
ReactionCard
Complex Reactions:
1.0Thumb → 1.0Thumb+1.0Thumb
1.02-Phospho-D-glyceric acid → 1.0Phosphoenolpyruvic acid + 1.0Water
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB041292-Phospho-D-glyceric acidMetaboCard
ECMDB214192-Phosphoglyceric acidMetaboCard
ECMDB00263Phosphoenolpyruvic acidMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Component
macromolecular complex
phosphopyruvate hydratase complex
protein complex
Function
binding
carbon-oxygen lyase activity
catalytic activity
cation binding
hydro-lyase activity
ion binding
lyase activity
magnesium ion binding
metal ion binding
phosphopyruvate hydratase activity
Process
alcohol metabolic process
glucose catabolic process
glucose metabolic process
glycolysis
hexose metabolic process
metabolic process
monosaccharide metabolic process
small molecule metabolic process
Gene Properties
Blattner:b2779
Gene OrientationCounterclockwise
Centisome Percentage:62.60
Left Sequence End2904665
Right Sequence End2905963
Gene Sequence:
>1299 bp
ATGACACTCACGCTCAATAGACAACTTCTCACCTCACGCCAGATTCTGGTGGCCTTTAGC
GGCGGGCTTGACTCCACCGTTCTGCTGCATCAGTTGGTGCAGTGGCGGACGGAAAATCCG
GGTGTCGCTCTGCGCGCTATTCATGTGCATCACGGTTTAAGTGCCAATGCCGATGCCTGG
GTTACGCATTGCGAAAACGTCTGCCAACAGTGGCAGGTGCCGCTGGTGGTCGAACGCGTA
CAACTTGCGCAAGAAGGACTGGGCATTGAGGCCCAGGCGCGGCAGGCACGTTATCAGGCA
TTTGCCCGCACCTTGTTGCCCGGTGAAGTGCTGGTCACCGCGCAACATCTCGACGATCAA
TGTGAAACCTTTCTGCTGGCGCTAAAACGCGGCAGTGGCCCTGCCGGGCTTTCGGCTATG
GCGGAAGTCTCGGAGTTTGCCGGAACGCGGCTTATTCGCCCGTTGCTCGCCCGCACGCGG
GGGGAACTGGTGCAGTGGGCGCGTCAGTATGATTTACGCTGGATTGAAGACGAAAGTAAT
CAGGACGACTCATACGATCGTAACTTTCTGCGCCTGCGCGTAGTGCCGTTATTGCAGCAG
CGTTGGCCGCATTTTGCCGAAGCAACGGCCCGCAGCGCCGCACTTTGTGCTGAACAAGAG
AGCCTGCTGGATGAACTGCTGGCAGATGATTTAGCACACTGTCAATCGCCGCAGGGGACG
CTGCAGATTGTGCCAATGCTGGCGATGAGTGATGCCCGCCGCGCGGCGATTATCCGCCGC
TGGCTGGCAGGGCAGAATGCACCGATGCCTTCCCGCGACGCGTTGGTGAGGATCTGGCAG
GAAGTGGCGCTGGCGCGGGAAGATGCCTCACCCTGTTTACGTTTGGGCGCGTTTGAAATC
CGACGCTATCAGTCGCAACTGTGGTGGATTAAATCCGTCACCGGGCAAAGCGAAAACATT
GTGCCGTGGCAGACGTGGCTTCAACCGCTGGAATTACCGGCGGGGCTGGGAAGTGTACAG
CTTAATGCGGGAGGCGATATTCGCCCTCCGCGTGCAGACGAAGCGGTCAGCGTGCGTTTC
AAAGCGCCAGGATTGCTGCATATTGTCGGGCGTAACGGCGGACGTAAGCTAAAGAAAATC
TGGCAAGAGCTGGGCGTGCCGCCGTGGCTACGTGACACCACGCCACTGCTGTTTTATGGC
GAAACGCTGATTGCGGCGGCAGGGGTATTTGTGACGCAAGAAGGTGTGGCTGAAGGTGAG
AATGGCGTAAGTTTTGTCTGGCAGAAAACGCTTAGTTAA
Protein Properties
Pfam Domain Function:
Protein Residues:432
Protein Molecular Weight:45655
Protein Theoretical pI:5
PDB File:1E9I
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Enolase
MSKIVKIIGREIIDSRGNPTVEAEVHLEGGFVGMAAAPSGASTGSREALELRDGDKSRFL
GKGVTKAVAAVNGPIAQALIGKDAKDQAGIDKIMIDLDGTENKSKFGANAILAVSLANAK
AAAAAKGMPLYEHIAELNGTPGKYSMPVPMMNIINGGEHADNNVDIQEFMIQPVGAKTVK
EAIRMGSEVFHHLAKVLKAKGMNTAVGDEGGYAPNLGSNAEALAVIAEAVKAAGYELGKD
ITLAMDCAASEFYKDGKYVLAGEGNKAFTSEEFTHFLEELTKQYPIVSIEDGLDESDWDG
FAYQTKVLGDKIQLVGDDLFVTNTKILKEGIEKGIANSILIKFNQIGSLTETLAAIKMAK
DAGYTAVISHRSGETEDATIADLAVGTAAGQIKTGSMSRSDRVAKYNQLIRIEEALGEKA
PYNGRKEIKGQA
References
External Links:
ResourceLink
Uniprot ID:P0A6P9
Uniprot Name:ENO_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:4902929
PDB ID:1E9I
Ecogene ID:EG10258
Ecocyc:EG10258
ColiBase:b2779
Kegg Gene:b2779
EchoBASE ID:EB0254
CCDB:ENO_ECOLI
BacMap:16130686
General Reference:
  • Bernstein, J. A., Lin, P. H., Cohen, S. N., Lin-Chao, S. (2004). "Global analysis of Escherichia coli RNA degradosome function using DNA microarrays." Proc Natl Acad Sci U S A 101:2758-2763. Pubmed: 14981237
  • 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
  • Boel, G., Pichereau, V., Mijakovic, I., Maze, A., Poncet, S., Gillet, S., Giard, J. C., Hartke, A., Auffray, Y., Deutscher, J. (2004). "Is 2-phosphoglycerate-dependent automodification of bacterial enolases implicated in their export?" J Mol Biol 337:485-496. Pubmed: 15003462
  • Chandran, V., Luisi, B. F. (2006). "Recognition of enolase in the Escherichia coli RNA degradosome." J Mol Biol 358:8-15. Pubmed: 16516921
  • Dannelly, H. K., Duclos, B., Cozzone, A. J., Reeves, H. C. (1989). "Phosphorylation of Escherichia coli enolase." Biochimie 71:1095-1100. Pubmed: 2513001
  • 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
  • Kuhnel, K., Luisi, B. F. (2001). "Crystal structure of the Escherichia coli RNA degradosome component enolase." J Mol Biol 313:583-592. Pubmed: 11676541
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Morita, T., Kawamoto, H., Mizota, T., Inada, T., Aiba, H. (2004). "Enolase in the RNA degradosome plays a crucial role in the rapid decay of glucose transporter mRNA in the response to phosphosugar stress in Escherichia coli." Mol Microbiol 54:1063-1075. Pubmed: 15522087
  • Py, B., Higgins, C. F., Krisch, H. M., Carpousis, A. J. (1996). "A DEAD-box RNA helicase in the Escherichia coli RNA degradosome." Nature 381:169-172. Pubmed: 8610017
  • Taghbalout, A., Rothfield, L. (2007). "RNaseE and the other constituents of the RNA degradosome are components of the bacterial cytoskeleton." Proc Natl Acad Sci U S A 104:1667-1672. Pubmed: 17242352
  • Weng, M., Makaroff, C. A., Zalkin, H. (1986). "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase." J Biol Chem 261:5568-5574. Pubmed: 3514618
  • Wilkins, M. R., Gasteiger, E., Tonella, L., Ou, K., Tyler, M., Sanchez, J. C., Gooley, A. A., Walsh, B. J., Bairoch, A., Appel, R. D., Williams, K. L., Hochstrasser, D. F. (1998). "Protein identification with N and C-terminal sequence tags in proteome projects." J Mol Biol 278:599-608. Pubmed: 9600841
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842