ENO1 encodes enolase 1 of Saccharomyces cerevisiae, one of two highly similar enolase isozymes (phosphopyruvate hydratase, EC 4.2.1.11). The Mg2+-dependent enzyme reversibly dehydrates 2-phospho-D-glycerate to phosphoenolpyruvate, a step shared by glycolysis and gluconeogenesis. Eno1 and Eno2 polypeptides assemble at random into three active dimers (Eno1-Eno1, Eno1-Eno2 and Eno2-Eno2). ENO1 is non-essential; it is a minor isozyme in glucose-grown cells but present at levels similar to ENO2 during growth on non-fermentable carbon sources. Enolase is predominantly cytosolic, but small pools associate with vacuoles, where enolase stimulates homotypic vacuole fusion independently of its catalytic activity, and with the mitochondrial surface.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0000015 phosphopyruvate hydratase complex | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA from enolase node PTN000224401 for the enolase (phosphopyruvate hydratase) complex; yeast enolase is a dimer and correct. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt SUBUNIT: Homodimer. PMID:6282834 isozymes are formed in the cell by random assortment of the two polypeptides into three active enolase dimers |
| GO:0000015 phosphopyruvate hydratase complex | IDA PMID:6282834 Targeted deletion of a yeast enolase structural gene. Identi... | ACCEPT | Summary: McAlister & Holland resolved three catalytically active enolase dimers (Eno1 homodimer, Eno2 homodimer and the Eno1-Eno2 heterodimer); Eno1 is a subunit of the phosphopyruvate hydratase complex. Supporting Evidence: PMID:6282834 isozymes are formed in the cell by random assortment of the two polypeptides into three active enolase dimers PMID:6282834 Three catalytically active enolases |
| GO:0000015 phosphopyruvate hydratase complex | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro enolase family (IPR000941) mapping to phosphopyruvate hydratase complex; correct for the dimeric yeast enzyme. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt SUBUNIT: Homodimer. |
| GO:0000287 magnesium ion binding | IEA GO_REF:0000002 | ACCEPT | Summary: InterPro enolase mapping to magnesium ion binding. Mg2+ is the essential catalytic and dimer-stabilising cofactor of yeast enolase; correct cofactor binding, non-core. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Name=Mg(2+); Xref=ChEBI:CHEBI:18420; |
| GO:0000324 fungal-type vacuole | IDA PMID:16565073 Enolase activates homotypic vacuole fusion and protein trans... | KEEP AS NON CORE | Summary: Decker & Wickner found that a small fraction of enolase (Eno1 and Eno2) is bound to purified vacuoles, dependent on Bor1. Experimental, but a minor pool of a cytosolic enzyme; retained as a non-core location linked to its vacuole-fusion moonlighting role. Supporting Evidence: PMID:16565073 Enolase is a cytosolic glycolytic enzyme, but a small portion of enolase is bound to vacuoles. |
| GO:0004634 phosphopyruvate hydratase activity | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA from enolase node PTN000224401; catalytic residues conserved; correct core MF. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; |
| GO:0004634 phosphopyruvate hydratase activity | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (ARBA, InterPro IPR000941, RHEA:10164, EC 4.2.1.11); correct. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; |
| GO:0004634 phosphopyruvate hydratase activity | IMP PMID:6282834 Targeted deletion of a yeast enolase structural gene. Identi... | ACCEPT | Summary: McAlister & Holland deleted ENO1; the enolase 1-containing active forms disappeared, leaving the Eno2 homodimer, attributing enolase activity to the ENO1 product. Core MF. Supporting Evidence: PMID:6282834 As expected, a single form of enolase was resolved from extracts of the mutant cell. PMID:6282834 Three catalytically active enolases |
| GO:0004634 phosphopyruvate hydratase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways GLUCFERMEN-PWY; enolase catalyses the reversible 2-phosphoglycerate/phosphoenolpyruvate interconversion in this pathway; correct MF. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; |
| GO:0004634 phosphopyruvate hydratase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways GLUCONEO-PWY-1; enolase catalyses the reversible 2-phosphoglycerate/phosphoenolpyruvate interconversion in this pathway; correct MF. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; |
| GO:0004634 phosphopyruvate hydratase activity | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways GLYCOLYSIS; enolase catalyses the reversible 2-phosphoglycerate/phosphoenolpyruvate interconversion in this pathway; correct MF. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; |
| GO:0005737 cytoplasm | HDA PMID:11914276 Subcellular localization of the yeast proteome. | ACCEPT | Summary: Kumar et al. large-scale immunolocalization placed Eno1 in the cytoplasm; correct. Supporting Evidence: PMID:11914276 By high-throughput immunolocalization of tagged gene products, we have determined the subcellular localization of 2744 yeast proteins. |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: UniProt subcellular location (Cytoplasm) mapped to GO; correct, cytosol is more precise. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt SUBCELLULAR LOCATION: Cytoplasm |
| GO:0005739 mitochondrion | HDA PMID:24769239 Quantitative variations of the mitochondrial proteome and ph... | KEEP AS NON CORE | Summary: Detected in the proteome of isolated mitochondria (Renvoise et al.). Consistent with the reported pool of glycolytic enzymes on the mitochondrial outer surface, but highly abundant cytosolic enzymes frequently contaminate such preparations; non-core. Supporting Evidence: PMID:24769239 isolated mitochondria extracted from yeast grown on fermentative (glucose or galactose) and respiratory (lactate) media PMID:16962558 part of the cellular pool of the glycolytic enzyme, enolase, is tightly associated with the mitochondrial surface |
| GO:0005739 mitochondrion | IDA PMID:16962558 Enolase takes part in a macromolecular complex associated to... | KEEP AS NON CORE | Summary: Brandina et al. showed a fraction of enolase tightly associated with the mitochondrial surface in a large complex containing other glycolytic enzymes and imported tRNA(Lys). Experimental, but a minor pool; non-core. Supporting Evidence: PMID:16962558 part of the cellular pool of the glycolytic enzyme, enolase, is tightly associated with the mitochondrial surface PMID:16962558 we show that all glycolytic enzymes are associated with mitochondria in yeast |
| GO:0005829 cytosol | HDA PMID:26928762 One library to make them all: streamlining the creation of y... | ACCEPT | Summary: SWAT-GFP library (Yofe et al.) localised the N-terminally tagged protein to the cytosol; correct primary location. Supporting Evidence: PMID:26928762 we constructed and investigated a library of ∼1,800 strains carrying SWAT-GFP modules at the amino termini of endomembrane proteins PMID:16565073 Enolase is a cytosolic glycolytic enzyme, but a small portion of enolase is bound to vacuoles. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: is_active_in cytosol from YeastPathways GLUCFERMEN-PWY; enolase is a cytosolic glycolytic enzyme; correct. Supporting Evidence: PMID:16565073 Enolase is a cytosolic glycolytic enzyme, but a small portion of enolase is bound to vacuoles. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: is_active_in cytosol from YeastPathways GLUCONEO-PWY-1; enolase is a cytosolic glycolytic enzyme; correct. Supporting Evidence: PMID:16565073 Enolase is a cytosolic glycolytic enzyme, but a small portion of enolase is bound to vacuoles. |
| GO:0005829 cytosol | RCA GO_REF:0000123 | ACCEPT | Summary: is_active_in cytosol from YeastPathways GLYCOLYSIS; enolase is a cytosolic glycolytic enzyme; correct. Supporting Evidence: PMID:16565073 Enolase is a cytosolic glycolytic enzyme, but a small portion of enolase is bound to vacuoles. |
| GO:0005886 plasma membrane | HDA PMID:16622836 The plasma membrane proteome of Saccharomyces cerevisiae and... | KEEP AS NON CORE | Summary: Identified in a plasma-membrane proteome (HDA). Enolase lacks a membrane anchor and such fractions are prone to contamination by abundant cytosolic enzymes, but independent work reports a cell-surface/plasma-membrane-associated enolase pool. Retained as non-core. Supporting Evidence: PMID:16622836 Nearly 90 proteins were identified and clustered PMID:16544286 the enolase-GFP fusion co-localized with a plasma membrane marker |
| GO:0006094 gluconeogenesis | RCA GO_REF:0000123 | ACCEPT | Summary: RCA from YeastPathways GLUCONEO-PWY-1. The enolase reaction is freely reversible and is used in the gluconeogenic direction on non-fermentable carbon sources, where Eno1 and Eno2 are present at similar levels (ENO1 is the isozyme relatively enriched under these conditions); correct. Supporting Evidence: PMID:6282834 Log phase cells grown on glucose contain 20-fold more enolase 2 polypeptide than enolase 1 polypeptide, whereas cells grown on ethanol or glycerol plus lactate contain similar amounts of the two polypeptides. file:yeast/ENO1/ENO1-uniprot.txt Reaction=(2R)-2-phosphoglycerate = phosphoenolpyruvate + H2O; |
| GO:0006096 glycolysis | IBA GO_REF:0000033 | ACCEPT | Summary: PAINT IBA for glycolysis; correct. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Carbohydrate degradation; glycolysis; pyruvate from D- |
| GO:0006096 glycolysis | IEA GO_REF:0000120 | ACCEPT | Summary: Combined IEA (InterPro, UniPathway UPA00109); correct. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Carbohydrate degradation; glycolysis; pyruvate from D- |
| GO:0006096 glycolysis | IMP PMID:6282834 Targeted deletion of a yeast enolase structural gene. Identi... | ACCEPT | Summary: Curator IMP from the eno1 deletion study (full text not cached). ENO1 is non-essential because ENO2 compensates, so the glycolytic role is shared; Eno1 contributes enolase activity to glycolysis. Accepted, deferring to curator. Supporting Evidence: PMID:6282834 As expected, a single form of enolase was resolved from extracts of the mutant cell. PMID:6282834 Log phase cells grown on glucose contain 20-fold more enolase 2 polypeptide than enolase 1 polypeptide, whereas cells grown on ethanol or glycerol plus lactate contain similar amounts of the two polypeptides. |
| GO:0019658 bifid shunt | RCA GO_REF:0000123 | REMOVE | Summary: 'bifid shunt' propagated by the YeastPathways superpathway GLUCFERMEN-PWY. The bifid shunt is the Bifidobacterium phosphoketolase pathway and does not operate in S. cerevisiae; enolase acts in canonical glycolysis. RCA mapping artefact. Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Carbohydrate degradation; glycolysis; pyruvate from D- |
| GO:0032889 regulation of vacuole fusion, non-autophagic | IDA PMID:16565073 Enolase activates homotypic vacuole fusion and protein trans... | KEEP AS NON CORE | Summary: Decker & Wickner purified a cytosolic vacuole-fusion-stimulating activity as enolase; recombinant Eno1 or Eno2, and a catalytically inactive mutant, stimulate homotypic vacuole fusion in vitro. A genuine but non-glycolytic moonlighting role; non-core. Supporting Evidence: PMID:16565073 Recombinant Eno1p or Eno2p stimulates in vitro vacuole fusion, as does a catalytically inactive mutant enolase |
| GO:0032889 regulation of vacuole fusion, non-autophagic | IMP PMID:16565073 Enolase activates homotypic vacuole fusion and protein trans... | KEEP AS NON CORE | Summary: Decker & Wickner: eno1 deletion or ENO2 depletion causes vacuole fragmentation in vivo, and enolase-deficient vacuoles fail to fuse in vitro. Moonlighting role; non-core. Supporting Evidence: PMID:16565073 Either deletion of the non-essential ENO1 gene or diminished expression of the essential ENO2 gene causes vacuole fragmentation in vivo |
| GO:0061620 obsolete glycolytic process through glucose-6-phosphate | RCA GO_REF:0000123 | MODIFY | Summary: RCA from YeastPathways GLYCOLYSIS to the obsolete 'glycolytic process through glucose-6-phosphate'; replace with glycolysis. Proposed replacements: glycolytic process Supporting Evidence: file:yeast/ENO1/ENO1-uniprot.txt Carbohydrate degradation; glycolysis; pyruvate from D- |
| GO:1904408 melatonin binding | IDA PMID:31708896 Glycolytic Proteins Interact With Intracellular Melatonin in... | MARK AS OVER ANNOTATED | Summary: Morcillo-Parra et al. affinity-captured proteins from yeast extracts on anti-melatonin IgG beads and identified Eno1 and Eno2 among the most abundant glycolytic enzymes. No direct binding constants, specificity controls against abundance, or functional consequence were reported, so 'melatonin binding' is weakly supported and of unclear physiological significance. Not removed because it is an experimental report. Supporting Evidence: PMID:31708896 proteins bound to melatonin were immunopurified by melatonin-IgG-Dynabeads PMID:31708896 Surprisingly, most of the proteins identified participate in the glycolytic pathway |
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Download this section (compressed HTML)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
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