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    Eno Enolase [ Drosophila melanogaster (fruit fly) ]

    Gene ID: 33351, updated on 17-Dec-2024

    Summary

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    Official Symbol
    Enoprovided by FlyBase
    Official Full Name
    Enolaseprovided by FlyBase
    Primary source
    FLYBASE:FBgn0000579
    Locus tag
    Dmel_CG17654
    See related
    AllianceGenome:FB:FBgn0000579
    Gene type
    protein coding
    RefSeq status
    REVIEWED
    Organism
    Drosophila melanogaster
    Lineage
    Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota; Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea; Drosophilidae; Drosophila; Sophophora
    Also known as
    anon-WO0153538.76; BEST:LD15491; CG17654; CT32526; Dmel\CG17654; DmENO; eno; Eno2; ENOA; T18
    Summary
    Predicted to enable phosphopyruvate hydratase activity. Involved in glucose homeostasis. Located in cytoplasm and plasma membrane. Is expressed in adult head; adult heart; spermatozoon; and wing disc. Human ortholog(s) of this gene implicated in Alzheimer's disease and prostate cancer. Orthologous to several human genes including ENO2 (enolase 2). [provided by Alliance of Genome Resources, Dec 2024]
    Orthologs
    all
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    Genomic context

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    See Eno in Genome Data Viewer
    Location:
    22B1-22B1; 2-3 cM
    Exon count:
    5
    Annotation release Status Assembly Chr Location
    Release 6.54 current Release 6 plus ISO1 MT (GCF_000001215.4) 2L NT_033779.5 (1724768..1729636, complement)
    Release 5.57 previous assembly Release 5 (GCF_000001215.2) 2L NT_033779.4 (1724768..1729636, complement)

    Chromosome 2L - NT_033779.5Genomic Context describing neighboring genes Neighboring gene mitochondrial ribosomal protein L48 Neighboring gene fritz Neighboring gene Replication in mitochondria 2 Neighboring gene Ribosomal RNA processing 40 Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein Neighboring gene uncharacterized protein

    Genomic regions, transcripts, and products

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    Go to nucleotide: Graphics FASTA GenBank

    Bibliography

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    Related articles in PubMed

    1. The nucleotide sequence of a Drosophila melanogaster enolase gene. Bishop JG, et al. Nucleic Acids Res, 1990 Jan 11. PMID 2106662, Free PMC Article
    2. Crystal structure of enolase from Drosophila melanogaster. Sun C, et al. Acta Crystallogr F Struct Biol Commun, 2017 Apr 1. PMID 28368282, Free PMC Article
    3. Systems biology approach reveals possible evolutionarily conserved moonlighting functions for enolase. Paludo GP, et al. Comput Biol Chem, 2015 Oct. PMID 25978602
    4. Extension of Drosophila lifespan by Rhodiola rosea through a mechanism independent from dietary restriction. Schriner SE, et al. PLoS One, 2013. PMID 23704949, Free PMC Article
    5. Enhanced activity of glycolytic enzymes in Drosophila and human cell models of Parkinson's disease based on DJ-1 deficiency. Solana-Manrique C, et al. Free Radic Biol Med, 2020 Oct. PMID 32726690

    See all (123) citations in PubMed

    GeneRIFs: Gene References Into Functions

    What's a GeneRIF?
    1. Crystal structure of enolase from Drosophila melanogaster has been resolved.
      Title: Crystal structure of enolase from Drosophila melanogaster.
    2. Systems biology approach reveals possible evolutionarily conserved moonlighting functions for enolase
      Title: Systems biology approach reveals possible evolutionarily conserved moonlighting functions for enolase.
    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 FlyBase

    Function Evidence Code Pubs
    enables magnesium 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 ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    Process Evidence Code Pubs
    involved_in canonical glycolysis ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in gluconeogenesis ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    involved_in glucose homeostasis IMP
    Inferred from Mutant Phenotype
    more info
    		 PubMed 
    involved_in glycolytic process IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    involved_in glycolytic process IEA
    Inferred from Electronic Annotation
    more info
    		  
    Component Evidence Code Pubs
    located_in cytoplasm HDA PubMed 
    is_active_in cytosol ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    part_of phosphopyruvate hydratase complex IBA
    Inferred from Biological aspect of Ancestor
    more info
    		  
    part_of phosphopyruvate hydratase complex IEA
    Inferred from Electronic Annotation
    more info
    		  
    part_of phosphopyruvate hydratase complex ISS
    Inferred from Sequence or Structural Similarity
    more info
    		  
    located_in plasma membrane HDA PubMed 

    General protein information

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    Preferred Names
    enolase
    Names
    CG17654-PA
    CG17654-PB
    CG17654-PC
    CG17654-PD
    CG17654-PE
    CG17654-PF
    Eno-PA
    Eno-PB
    Eno-PC
    Eno-PD
    Eno-PE
    Eno-PF
    phosphopyruvate hydratase
    NP_001162853.1
    NP_477421.1
    NP_722721.1
    NP_722722.1
    NP_722723.1
    NP_722724.1

    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. NT_033779.5 Reference assembly

      Range
      1724768..1729636 complement
      Download
      GenBank, FASTA, Sequence Viewer (Graphics)

    mRNA and Protein(s)

    1. NM_164434.3 → NP_722724.1  enolase, isoform E [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_722724.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A4UZY9, A5XD39, A5XD43, B9EQS7, C0PV73, P15007, Q8IPX8, Q8MT10, Q9VQ38
      Related
      FBpp0077572
      Conserved Domains (2) summary
      PLN00191
      Location:69 → 499
      PLN00191; enolase
      cd03313
      Location:72 → 484
      enolase; Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.

    2. NM_164431.3 → NP_722721.1  enolase, isoform B [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_722721.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A4UZY9, A5XD39, A5XD43, B9EQS7, C0PV73, P15007, Q8IPX8, Q8MT10, Q9VQ38
      Related
      FBpp0077571
      Conserved Domains (2) summary
      PLN00191
      Location:69 → 499
      PLN00191; enolase
      cd03313
      Location:72 → 484
      enolase; Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.

    3. NM_164433.3 → NP_722723.1  enolase, isoform D [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_722723.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A4UZY9, A5XD39, A5XD43, B9EQS7, C0PV73, P15007, Q8IPX8, Q8MT10, Q9VQ38
      Related
      FBpp0077574
      Conserved Domains (2) summary
      PLN00191
      Location:69 → 499
      PLN00191; enolase
      cd03313
      Location:72 → 484
      enolase; Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.

    4. NM_164432.3 → NP_722722.1  enolase, isoform C [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_722722.1

      Status: REVIEWED

      UniProtKB/Swiss-Prot
      A4UZY9, A5XD39, A5XD43, B9EQS7, C0PV73, P15007, Q8IPX8, Q8MT10, Q9VQ38
      Related
      FBpp0077573
      Conserved Domains (2) summary
      PLN00191
      Location:69 → 499
      PLN00191; enolase
      cd03313
      Location:72 → 484
      enolase; Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.

    5. NM_058073.5 → NP_477421.1  enolase, isoform A [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_477421.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      E1JHR5
      Related
      FBpp0077575
      Conserved Domains (2) summary
      PLN00191
      Location:2 → 432
      PLN00191; enolase
      cd03313
      Location:5 → 417
      enolase; Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.

    6. NM_001169382.2 → NP_001162853.1  enolase, isoform F [Drosophila melanogaster]

      See identical proteins and their annotated locations for NP_001162853.1

      Status: REVIEWED

      UniProtKB/TrEMBL
      E1JHR5
      Conserved Domains (2) summary
      PLN00191
      Location:2 → 432
      PLN00191; enolase
      cd03313
      Location:5 → 417
      enolase; Enolase: Enolases are homodimeric enzymes that catalyse the reversible dehydration of 2-phospho-D-glycerate to phosphoenolpyruvate as part of the glycolytic and gluconeogenesis pathways. The reaction is facilitated by the presence of metal ions.
    Nucleotide Protein
    Heading Accession and Version
    Protein Accession Links
    GenPept Link UniProtKB Link
    E1JHR5 E1JHR5
    P15007.2 P15007

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