FOG00295
EOG8JM664
ENO1
sce:ENO1;ENO2;ERR2;ERR3

Genes: 45

Protein description
Enolase. and local duplications; sce/vpo have ohnologs; 137-138 insertion in ctg clade starting with pta, suggets independent duplication in ctg clade?


SGD Description
Enolase I, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression repressed in response to glucose; protein abundance increases in response to DNA replication stress; N-terminally propionylated in vivo; ENO1 has a paralog, ENO2, that arose from the whole genome duplication|Enolase II, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; expression induced in response to glucose; ENO2 has a paralog, ENO1, that arose from the whole genome duplication|Enolase, a phosphopyruvate hydratase; catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate; complements the growth defect of an ENO1 ENO2 double mutant|Enolase, a phosphopyruvate hydratase; catalyzes the conversion of 2-phosphoglycerate to phosphoenolpyruvate; complements the growth defect of an ENO1 ENO2 double mutant in glucose


PomBase Description
enolase (predicted)


AspGD Description
Phosphopyruvate hydratase


References

Payton M, et al. (1976 May). Agar as a carbon source and its effect on the utilization of other carbon sources by acetate non-utilizing (acu) mutants of Aspergillus nidulans.

Chin CC, et al. (1981 Feb 10). The amino acid sequence of yeast enolase.

Holland MJ, et al. (1981 Feb 10). The primary structures of two yeast enolase genes. Homology between the 5' noncoding flanking regions of yeast enolase and glyceraldehyde-3-phosphate dehydrogenase genes.

Lebioda L, et al. (1988 Jun 16). Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor.

Lebioda L, et al. (1989 Mar 5). 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.

Stec B, et al. (1990 Jan 5). Refined structure of yeast apo-enolase at 2.25 A resolution.

Sundstrom P, et al. (1992 Nov). Molecular cloning of cDNA and analysis of protein secondary structure of Candida albicans enolase, an abundant, immunodominant glycolytic enzyme.

Franklyn KM, et al. (1993 Jul 15). Cloning and nucleotide sequence analysis of the Candida albicans enolase gene.

Mason AB, et al. (1993 May). Molecular cloning and characterization of the Candida albicans enolase gene.

Norbeck J, et al. (1995 Jan). Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides.

Larsen TM, et al. (1996 Apr 9). 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.

Poyner RR, et al. (1996 Feb 6). Toward identification of acid/base catalysts in the active site of enolase: comparison of the properties of K345A, E168Q, and E211Q variants.

Norbeck J, et al. (1996 Mar 15). Protein expression during exponential growth in 0.7 M NaCl medium of Saccharomyces cerevisiae.

Clutterbuck AJ, et al. (1997 Jun). The validity of the Aspergillus nidulans linkage map.

Zhang E, et al. (1997 Oct 14). Mechanism of enolase: the crystal structure of asymmetric dimer enolase-2-phospho-D-glycerate/enolase-phosphoenolpyruvate at 2.0 A resolution.

Brewer JM, et al. (2000 Oct 5). The H159A mutant of yeast enolase 1 has significant activity.

Grandier-Vazeille X, et al. (2001 Aug 21). Yeast mitochondrial dehydrogenases are associated in a supramolecular complex.

Poyner RR, et al. (2002 May 15). Functional and structural changes due to a serine to alanine mutation in the active-site flap of enolase.

Sims PA, et al. (2003 Jul 15). Reverse protonation is the key to general acid-base catalysis in enolase.

Brewer JM, et al. (2003 May). Enzymatic function of loop movement in enolase: preparation and some properties of H159N, H159A, H159F, and N207A enolases.

Lemaire M, et al. (2004 Oct). Enolase and glycolytic flux play a role in the regulation of the glucose permease gene RAG1 of Kluyveromyces lactis.

Chi A, et al. (2007 Feb 13). Analysis of phosphorylation sites on proteins from Saccharomyces cerevisiae by electron transfer dissociation (ETD) mass spectrometry.

Hynes MJ, et al. (2007 May). Transcriptional control of gluconeogenesis in Aspergillus nidulans.

Kim Y, et al. (2007 Sep). Proteome map of Aspergillus nidulans during osmoadaptation.

Flipphi M, et al. (2009 Mar). Biodiversity and evolution of primary carbon metabolism in Aspergillus nidulans and other Aspergillus spp.

Masuo S, et al. (2010 Dec). Global gene expression analysis of Aspergillus nidulans reveals metabolic shift and transcription suppression under hypoxia.

Cho SJ, et al. (2010 Jun). Possible Roles of LAMMER Kinase Lkh1 in Fission Yeast by Comparative Proteome Analysis.

Oh YT, et al. (2010 Mar). Proteomic analysis of early phase of conidia germination in Aspergillus nidulans.

Wendland J, et al. (2011 Dec). Genome evolution in the eremothecium clade of the Saccharomyces complex revealed by comparative genomics.

Pusztahelyi T, et al. (2011 Feb). Comparison of transcriptional and translational changes caused by long-term menadione exposure in Aspergillus nidulans.

Etxebeste O, et al. (2012). GmcA is a putative glucose-methanol-choline oxidoreductase required for the induction of asexual development in Aspergillus nidulans.

Starita LM, et al. (2012 Jan). Sites of ubiquitin attachment in Saccharomyces cerevisiae.

Wartenberg D, et al. (2012 Jul 16). Proteome analysis of the farnesol-induced stress response in Aspergillus nidulans--The role of a putative dehydrin.

Shimanuki M, et al. (2013). Klf1, a C2H2 zinc finger-transcription factor, is required for cell wall maintenance during long-term quiescence in differentiated G0 phase.

Martins I, et al. (2013 Dec 6). Proteomic alterations induced by ionic liquids in Aspergillus nidulans and Neurospora crassa.

Guydosh NR, et al. (2017 Sep 25). Regulated Ire1-dependent mRNA decay requires no-go mRNA degradation to maintain endoplasmic reticulum homeostasis in <i>S. pombe</i>.

Mitochondrial localization predictions
Predotar TargetP MitoProt
Raw data
Phobius transmembrane predictions
0 genes with posterior transmembrane prediction > 50%


FOG00296
EOG8JM664
ERR1
sce:ERR1

Genes: 1

Protein description
Uncharacterized enolase ohnolog


Parent
ohnolog:FOG00295


SGD Description
Protein of unknown function; has similarity to enolases


References

Pryde FE, et al. (1995 Apr 15). Sequence analysis of the right end of chromosome XV in Saccharomyces cerevisiae: an insight into the structural and functional significance of sub-telomeric repeat sequences.

Mitochondrial localization predictions
Predotar TargetP MitoProt
Raw data
Phobius transmembrane predictions
0 genes with posterior transmembrane prediction > 50%


FOG00297
EOG8JM664

sce:absent

Genes: 1

Protein description
Uncharacterized enolase paralog


Parent
paralog:FOG00295

Mitochondrial localization predictions
Predotar TargetP MitoProt
Raw data
Phobius transmembrane predictions
0 genes with posterior transmembrane prediction > 50%