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Identification
NameEnolase 2
Synonyms
  • 2-phospho-D-glycerate hydro-lyase 2
  • 2-phosphoglycerate dehydratase 2
Gene NameENO2
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
carbon-oxygen lyase activity
hydro-lyase activity
catalytic activity
lyase activity
binding
phosphopyruvate hydratase activity
ion binding
cation binding
metal ion binding
magnesium ion binding
Process
glucose metabolic process
metabolic process
glucose catabolic process
glycolysis
small molecule metabolic process
alcohol metabolic process
monosaccharide metabolic process
hexose metabolic process
Gene Properties
Chromosome Locationchromosome 8
LocusYHR174W
Gene Sequence>1314 bp ATGGCTGTCTCTAAAGTTTACGCTAGATCCGTCTACGACTCCCGTGGTAACCCAACCGTC GAAGTCGAATTAACCACCGAAAAGGGTGTTTTCAGATCCATTGTTCCATCTGGTGCCTCC ACCGGTGTCCACGAAGCTTTGGAAATGAGAGATGAAGACAAATCCAAGTGGATGGGTAAG GGTGTTATGAACGCTGTCAACAACGTCAACAACGTCATTGCTGCTGCTTTCGTCAAGGCT AACTTAGATGTTAAGGACCAAAAGGCCGTCGATGACTTCTTGTTGTCTTTGGATGGTACC GCCAACAAGTCCAAGTTGGGTGCTAACGCTATCTTGGGTGTCTCCATGGCCGCTGCTAGA GCCGCTGCTGCTGAAAAGAACGTCCCATTGTACCAACACTTGGCTGACTTGTCTAAGTCC AAGACCTCTCCATACGTTTTGCCAGTTCCATTCTTGAACGTTTTGAACGGTGGTTCCCAC GCTGGTGGTGCTTTGGCTTTGCAAGAATTCATGATTGCTCCAACTGGTGCTAAGACCTTC GCTGAAGCCATGAGAATTGGTTCCGAAGTTTACCACAACTTGAAGTCTTTGACCAAGAAG AGATATGGTGCTTCTGCCGGTAACGTCGGTGACGAAGGTGGTGTTGCTCCAAACATTCAA ACCGCTGAAGAAGCTTTGGACTTGATTGTTGACGCTATCAAGGCTGCTGGTCACGACGGT AAGGTCAAGATCGGTTTGGACTGTGCTTCCTCTGAATTCTTCAAGGACGGTAAGTACGAC TTGGACTTCAAGAACCCAGAATCTGACAAATCCAAGTGGTTGACTGGTGTCGAATTGGCT GACATGTACCACTCCTTGATGAAGAGATACCCAATTGTCTCCATCGAAGATCCATTTGCT GAAGATGACTGGGAAGCTTGGTCTCACTTCTTCAAGACCGCCGGTATTCAAATTGTTGCT GATGACTTGACTGTCACTAACCCAGCTAGAATTGCTACCGCTATCGAAAAGAAGGCTGCT GACGCTTTGTTGTTGAAGGTTAACCAAATCGGTACCTTGTCTGAATCCATCAAGGCTGCT CAAGACTCTTTCGCTGCCAACTGGGGTGTCATGGTTTCCCACAGATCTGGTGAAACTGAA GACACTTTCATTGCTGACTTGGTTGTCGGTTTGAGAACTGGTCAAATCAAGACTGGTGCT CCAGCTAGATCCGAAAGATTGGCTAAGTTGAACCAATTGTTGAGAATCGAAGAAGAATTG GGTGACAAGGCTGTCTACGCCGGTGAAAACTTCCACCACGGTGACAAGTTGTAA
Protein Properties
Pfam Domain Function
Protein Residues437
Protein Molecular Weight46913.69922
Protein Theoretical pI5.85
PDB Fileshow
Signalling Regions
  • None
Transmembrane Regions
  • None
Protein Sequence>Enolase 2 MAVSKVYARSVYDSRGNPTVEVELTTEKGVFRSIVPSGASTGVHEALEMRDEDKSKWMGK GVMNAVNNVNNVIAAAFVKANLDVKDQKAVDDFLLSLDGTANKSKLGANAILGVSMAAAR AAAAEKNVPLYQHLADLSKSKTSPYVLPVPFLNVLNGGSHAGGALALQEFMIAPTGAKTF AEAMRIGSEVYHNLKSLTKKRYGASAGNVGDEGGVAPNIQTAEEALDLIVDAIKAAGHDG KVKIGLDCASSEFFKDGKYDLDFKNPESDKSKWLTGVELADMYHSLMKRYPIVSIEDPFA EDDWEAWSHFFKTAGIQIVADDLTVTNPARIATAIEKKAADALLLKVNQIGTLSESIKAA QDSFAANWGVMVSHRSGETEDTFIADLVVGLRTGQIKTGAPARSERLAKLNQLLRIEEEL GDKAVYAGENFHHGDKL
References
External Links
ResourceLink
Saccharomyces Genome Database ENO2
Uniprot IDP00925
Uniprot NameENO2_YEAST
GenBank Gene IDJ01323
Genebank Protein ID171457
PDB ID
2ONE
General Reference
  • Holland, M. J., Holland, J. P., Thill, G. P., Jackson, K. A. (1981). "The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes." J Biol Chem 256:1385-1395.6256394
  • Johnston, M., Andrews, S., Brinkman, R., Cooper, J., Ding, H., Dover, J., Du, Z., Favello, A., Fulton, L., Gattung, S., et, a. l. .. (1994). "Complete nucleotide sequence of Saccharomyces cerevisiae chromosome VIII." Science 265:2077-2082.8091229
  • Norbeck, J., Blomberg, A. (1996). "Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae." FEMS Microbiol Lett 137:1-8.8935650
  • Norbeck, J., Blomberg, A. (1995). "Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides." Electrophoresis 16:149-156.7737086
  • Garrels, J. I., Futcher, B., Kobayashi, R., Latter, G. I., Schwender, B., Volpe, T., Warner, J. R., McLaughlin, C. S. (1994). "Protein identifications for a Saccharomyces cerevisiae protein database." Electrophoresis 15:1466-1486.7895733
  • Ficarro, S. B., McCleland, M. L., Stukenberg, P. T., Burke, D. J., Ross, M. M., Shabanowitz, J., Hunt, D. F., White, F. M. (2002). "Phosphoproteome analysis by mass spectrometry and its application to Saccharomyces cerevisiae." Nat Biotechnol 20:301-305.11875433
  • Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
  • Gruhler, A., Olsen, J. V., Mohammed, S., Mortensen, P., Faergeman, N. J., Mann, M., Jensen, O. N. (2005). "Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway." Mol Cell Proteomics 4:310-327.15665377
  • 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
  • Albuquerque, C. P., Smolka, M. B., Payne, S. H., Bafna, V., Eng, J., Zhou, H. (2008). "A multidimensional chromatography technology for in-depth phosphoproteome analysis." Mol Cell Proteomics 7:1389-1396.18407956