Identification
NameEnolase 1
Synonyms
  • 2-phospho-D-glycerate hydro-lyase 1
  • 2-phosphoglycerate dehydratase 1
Gene NameENO1
Enzyme Class
Biological Properties
General FunctionInvolved in magnesium ion binding
Specific Function2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O
Cellular LocationCytoplasm
SMPDB PathwaysNot Available
KEGG Pathways
Glycolysis / Gluconeogenesisec00010 Map00010
Methane metabolismec00680 Map00680
SMPDB ReactionsNot Available
KEGG Reactions
2-phospho-D-glyceric acidPhosphoenolpyruvic acid + water
Metabolites
YMDB IDNameView
YMDB00276Phosphoenolpyruvic acidShow
YMDB006752-phospho-D-glyceric acidShow
YMDB00890waterShow
YMDB009852-phospho-d-glycerateShow
GO Classification
Component
macromolecular complex
protein complex
phosphopyruvate hydratase complex
Function
cation binding
metal ion binding
magnesium ion binding
carbon-oxygen lyase activity
hydro-lyase activity
catalytic activity
lyase activity
binding
phosphopyruvate hydratase activity
ion binding
Process
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
glucose metabolic process
metabolic process
glucose catabolic process
glycolysis
Gene Properties
Chromosome Locationchromosome 7
LocusYGR254W
Gene Sequence>1314 bp ATGGCTGTCTCTAAAGTTTACGCTAGATCCGTCTACGACTCCCGTGGTAACCCAACCGTC GAAGTCGAATTAACCACCGAAAAGGGTGTTTTCAGATCCATTGTCCCATCTGGTGCTTCT ACCGGTGTCCACGAAGCTTTGGAAATGAGAGATGGTGACAAATCCAAGTGGATGGGTAAG GGTGTTTTGCACGCTGTTAAGAACGTCAACGATGTCATTGCTCCAGCTTTCGTTAAGGCT AACATTGATGTTAAGGACCAAAAGGCCGTCGATGACTTCTTGATTTCTTTGGACGGTACT GCCAACAAATCCAAGTTGGGTGCTAACGCTATCTTGGGTGTTTCTTTGGCTGCTTCCAGA GCTGCCGCTGCTGAAAAGAATGTCCCATTATACAAGCACTTGGCTGACTTGTCTAAGTCC AAGACCTCTCCATACGTTTTGCCAGTTCCATTCTTGAACGTTTTGAACGGTGGTTCCCAC GCTGGTGGTGCTTTGGCTTTGCAAGAATTTATGATTGCTCCAACTGGTGCTAAGACCTTC GCTGAAGCTTTGAGAATTGGTTCCGAAGTTTACCACAACTTGAAGTCTTTGACCAAGAAG AGATACGGTGCTTCTGCCGGTAACGTCGGTGACGAAGGTGGTGTTGCTCCAAACATTCAA ACTGCTGAAGAAGCTTTGGACTTGATTGTTGACGCTATCAAGGCCGCTGGTCACGACGGT AAGGTCAAGATCGGTTTGGACTGTGCTTCCTCTGAATTCTTCAAGGACGGTAAGTACGAC TTGGACTTCAAGAATCCAAACTCTGACAAATCCAAGTGGTTGACTGGTCCTCAATTGGCT GACTTGTACCACTCCTTGATGAAGAGATACCCAATTGTCTCCATCGAAGATCCATTTGCT GAAGATGACTGGGAAGCTTGGTCTCACTTCTTCAAGACCGCTGGTATTCAAATTGTTGCT GATGACTTGACTGTCACCAACCCAAAGAGAATTGCTACCGCTATCGAAAAGAAGGCTGCC GACGCTTTGTTGTTGAAGGTCAACCAAATCGGTACCTTGTCTGAATCCATCAAAGCTGCT CAAGACTCTTTCGCTGCCGGTTGGGGTGTTATGGTTTCCCACAGATCTGGTGAAACTGAA GACACTTTCATTGCTGACTTGGTCGTCGGTTTGAGAACTGGTCAAATCAAGACTGGTGCT CCAGCTAGATCCGAAAGATTGGCTAAATTGAACCAATTGTTGAGAATCGAAGAAGAATTG GGTGACAACGCTGTTTTCGCTGGTGAAAACTTCCACCACGGTGACAAATTATAA
Protein Properties
Pfam Domain Function
Protein Residues437
Protein Molecular Weight46815.69922
Protein Theoretical pI6.6
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Enolase 1 MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDGDKSKWMGK GVLHAVKNVNDVIAPAFVKANIDVKDQKAVDDFLISLDGTANKSKLGANAILGVSLAASR AAAAEKNVPLYKHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTF AEALRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDG KIKIGLDCASSEFFKDGKYDLDFKNPNSDKSKWLTGPQLADLYHSLMKRYPIVSIEDPFA EDDWEAWSHFFKTAGIQIVADDLTVTNPKRIATAIEKKAADALLLKVNQIGTLSESIKAA QDSFAAGWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEEL GDNAVFAGENFHHGDKL
References
External Links
ResourceLink
Saccharomyces Genome Database ENO1
Uniprot IDP00924
Uniprot NameENO1_YEAST
GenBank Gene IDJ01322
Genebank Protein ID171455
PDB ID
2ONE
General Reference
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  • Tettelin, H., Agostoni Carbone, M. L., Albermann, K., Albers, M., Arroyo, J., Backes, U., Barreiros, T., Bertani, I., Bjourson, A. J., Bruckner, M., Bruschi, C. V., Carignani, G., Castagnoli, L., Cerdan, E., Clemente, M. L., Coblenz, A., Coglievina, M., Coissac, E., Defoor, E., Del Bino, S., Delius, H., Delneri, D., de Wergifosse, P., Dujon, B., Kleine, K., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Nature 387:81-84.9169869
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  • Chi, A., Huttenhower, C., Geer, L. Y., Coon, J. J., Syka, J. E., Bai, D. L., Shabanowitz, J., Burke, D. J., Troyanskaya, O. G., Hunt, D. F. (2007). "Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry." Proc Natl Acad Sci U S A 104:2193-2198.17287358
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  • Lebioda, L., Stec, B. (1988). "Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor." Nature 333:683-686.3374614
  • Lebioda, L., Stec, B., Brewer, J. M. (1989). "The structure of yeast enolase at 2.25-A resolution. An 8-fold beta + alpha-barrel with a novel beta beta alpha alpha (beta alpha)6 topology." J Biol Chem 264:3685-3693.2645275
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  • Larsen, T. M., Wedekind, J. E., Rayment, I., Reed, G. H. (1996). "A carboxylate oxygen of the substrate bridges the magnesium ions at the active site of enolase: structure of the yeast enzyme complexed with the equilibrium mixture of 2-phosphoglycerate and phosphoenolpyruvate at 1.8 A resolution." Biochemistry 35:4349-4358.8605183
  • Zhang, E., Brewer, J. M., Minor, W., Carreira, L. A., Lebioda, L. (1997). "Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution." Biochemistry 36:12526-12534.9376357
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