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    ENO2 phosphopyruvate hydratase ENO2 [ Saccharomyces cerevisiae S288C ]

    Gene ID: 856579, updated on 9-Dec-2024

    Summary

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    Official Symbol
    ENO2
    Official Full Name
    phosphopyruvate hydratase ENO2
    Primary source
    SGD:S000001217
    Locus tag
    YHR174W
    See related
    AllianceGenome:SGD:S000001217; FungiDB:YHR174W; VEuPathDB:YHR174W
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Saccharomyces cerevisiae S288C (strain: S288C)
    Lineage
    Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces
    Summary
    Enables melatonin binding activity and phosphopyruvate hydratase activity. Involved in glycolytic process and regulation of vacuole fusion, non-autophagic. Located in cytoplasmic side of plasma membrane; fungal-type vacuole; and mitochondrion. Part of phosphopyruvate hydratase complex. Human ortholog(s) of this gene implicated in Alzheimer's disease and prostate cancer. Orthologous to several human genes including ENO1 (enolase 1) and ENO3 (enolase 3). [provided by Alliance of Genome Resources, Dec 2024]
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    Genomic context

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    See ENO2 in Genome Data Viewer
    Location:
    chromosome: VIII
    Exon count:
    1
    Sequence:
    Chromosome: VIII; NC_001140.6 (451327..452640)

    Chromosome VIII - NC_001140.6Genomic Context describing neighboring genes Neighboring gene Spc97p Neighboring gene uncharacterized protein Neighboring gene low-affinity Cu transporter Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Genomic Sequence:
    NC_001140.6

    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae. Entelis N, et al. Genes Dev, 2006 Jun 15. PMID 16738406, Free PMC Article
    2. Characterization of differently processed forms of enolase 2 from Saccharomyces cerevisiae by two-dimensional gel electrophoresis and mass spectrometry. Larsen MR, et al. Electrophoresis, 2001 Feb. PMID 11258770
    3. Identification of a regulatory region that mediates glucose-dependent induction of the Saccharomyces cerevisiae enolase gene ENO2. Cohen R, et al. Mol Cell Biol, 1986 Jul. PMID 3537717, Free PMC Article
    4. Role of metal ions in catalysis by enolase: an ordered kinetic mechanism for a single substrate enzyme. Poyner RR, et al. Biochemistry, 2001 Jul 10. PMID 11434770
    5. Crystal structure of enolase indicates that enolase and pyruvate kinase evolved from a common ancestor. Lebioda L, et al. Nature, 1988 Jun 16. PMID 3374614

    See all (172) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. data suggest the existence of a protein complex containing Eno2p that is involved in RNA mitochondrial import
      Title: Factors beyond Enolase 2 and Mitochondrial Lysyl-tRNA Synthetase Precursor Are Required for tRNA Import into Yeast Mitochondria.
    2. Both novel and known locus-specific DNA-protein interactions were identified at the ENO2 and GAL1 promoter regions of Saccharomyces cerevisiae, and revealed subgroups of proteins present in significantly different levels at the loci in cells grown on glucose versus galactose as the carbon source
      Title: HyCCAPP as a tool to characterize promoter DNA-protein interactions in Saccharomyces cerevisiae.
    3. The results indicate an alternative molecular chaperone function of glycolytic enzyme enolase in tRNA mitochondrial targeting.
      Title: A glycolytic enzyme, enolase, is recruited as a cofactor of tRNA targeting toward mitochondria in Saccharomyces cerevisiae.
    Submit: New GeneRIF Correction

    Pathways from PubChem

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    Interactions

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    Products Interactant Other Gene Complex Source Pubs Description

    General gene information

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    Homology

    Gene Ontology Provided by SGD

    Function Evidence Code Pubs
    enables lyase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables magnesium ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables melatonin binding IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    enables metal ion binding IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phosphopyruvate hydratase activity IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    enables phosphopyruvate hydratase activity IEA
    Inferred from Electronic Annotation
    more info
    		  
    enables phosphopyruvate hydratase activity IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Process Evidence Code Pubs
    involved_in glycolytic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in glycolytic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    involved_in glycolytic process IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in regulation of vacuole fusion, non-autophagic IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    involved_in regulation of vacuole fusion, non-autophagic IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    Component Evidence Code Pubs
    located_in cytoplasm IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in cytoplasmic side of plasma membrane IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in cytosol HDA PubMed 
    located_in fungal-type vacuole IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    located_in mitochondrion HDA PubMed 
    located_in mitochondrion IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of phosphopyruvate hydratase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of phosphopyruvate hydratase complex IDA
    Inferred from Direct Assay
    more info
    		 PubMed 
    part_of phosphopyruvate hydratase complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    located_in plasma membrane HDA PubMed 

    General protein information

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    Preferred Names
    phosphopyruvate hydratase ENO2
    NP_012044.1
    • Enolase II, a phosphopyruvate hydratase; catalyzes conversion of 2-phosphoglycerate to phosphoenolpyruvate during glycolysis and the reverse reaction during gluconeogenesis; mRNA is asymmetrically distributed to daughter cells in a Sir2p-dependent manner, and asymmetry is lost during replicative aging; expression induced in response to glucose; ENO2 has a paralog, ENO1, that arose from the whole genome duplication

    NCBI Reference Sequences (RefSeq)

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    Genome Annotation

    The following sections contain reference sequences that belong to a specific genome build. Explain

    Reference assembly

    Genomic

    1. NC_001140.6 Reference assembly

      Range
      451327..452640
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_001179305.1 → NP_012044.1  TPA: phosphopyruvate hydratase ENO2 [Saccharomyces cerevisiae S288C]

      See identical proteins and their annotated locations for NP_012044.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      D3DLC2, P00925, P99013
      UniProtKB/TrEMBL
      A6ZT81, B3LST6, B5VJJ6, G2WFP7
      Conserved Domains (1) summary
      PTZ00081
      Location:1 → 430
      PTZ00081; enolase; Provisional
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    P00925.2

    Gene LinkOut

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