A5EW24 · ENO_DICNV

Function

function

Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP). It is essential for the degradation of carbohydrates via glycolysis.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds a second Mg2+ ion via substrate during catalysis.

Pathway

Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.

Features

Showing features for binding site, active site.

TypeIDPosition(s)Description
Binding site164(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Active site206Proton donor
Binding site243Mg2+ (UniProtKB | ChEBI)
Binding site286Mg2+ (UniProtKB | ChEBI)
Binding site313Mg2+ (UniProtKB | ChEBI)
Active site338Proton acceptor
Binding site338(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site367(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site368(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site389(2R)-2-phosphoglycerate (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componentcell surface
Cellular Componentextracellular region
Cellular Componentphosphopyruvate hydratase complex
Molecular Functionmagnesium ion binding
Molecular Functionphosphopyruvate hydratase activity
Biological Processglycolytic process

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Enolase
  • EC number
  • Alternative names
    • 2-phospho-D-glycerate hydro-lyase
    • 2-phosphoglycerate dehydratase

Gene names

    • Name
      eno
    • Ordered locus names
      DNO_0362

Organism names

Accessions

  • Primary accession
    A5EW24

Proteomes

Subcellular Location

Cytoplasm
Secreted
Cell surface
Note: Fractions of enolase are present in both the cytoplasm and on the cell surface.

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00003376151-430Enolase

Interaction

Subunit

Component of the RNA degradosome, a multiprotein complex involved in RNA processing and mRNA degradation.

Protein-protein interaction databases

Structure

Family & Domains

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    46,242
  • Last updated
    2007-06-12 v1
  • Checksum
    2B8107E5433F1E9C
MTITISRIHALEILDSRGNPTLQVGVTLSDGSFAQAGVPSGASTGSREALELRDGDAQRYLGKGVQKALANVKNHFAPALIGKPIYDLAALDRIMLAQDGTDFKTHLGANAILGVSLALARAKGASLKKPLYAVLCPQEEYTLPVPMMNIINGGEHADNSVDIQEFMIVPAGFDRFSEALRAGSEIFHTLKKVLKEQGLNTAVGDEGGFAPDLPSNEAAFAVIMQAIERAGYRAGEQIFLAMDAAASEFYREGRYHLASEQKAYTSAEFVDYLADLCRRYPIVSIEDGLHESDWDGWQLLTQSLGERVQLVGDDLFVTNSAILQEGIDKGVANAILIKPNQIGSLSETLQTIALADAAHYAAIISHRSGETEDTTIADIAVATTATQIKTGSLCRSDRVAKYNRLLTIEDELGTRARYAAKAAFLGKIKA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000513
EMBL· GenBank· DDBJ
ABQ13410.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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