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Eno Enolase [ Drosophila melanogaster (fruit fly) ]

Gene ID: 33351, updated on 4-Jan-2025

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, Jan 2025]
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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