P42448 · ENO_CAMJE

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 site162(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Active site204Proton donor
Binding site239Mg2+ (UniProtKB | ChEBI)
Binding site280Mg2+ (UniProtKB | ChEBI)
Binding site307Mg2+ (UniProtKB | ChEBI)
Active site332Proton acceptor
Binding site332(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site361(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site362(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site383(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
    • Phosphopyruvate hydratase

Gene names

    • Name
      eno
    • Ordered locus names
      Cj1672c

Organism names

Accessions

  • Primary accession
    P42448
  • Secondary accessions
    • Q0P7V7
    • Q9PM05

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_00001338611-414Enolase

Proteomic databases

Interaction

Protein-protein interaction databases

Family & Domains

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    414
  • Mass (Da)
    44,939
  • Last updated
    2000-12-01 v2
  • Checksum
    25C132C6B631FF3D
MLVIEDVRAYEVLDSRGNPTVKAEVTLSDGSVGAAIVPSGASTGSKEALELRDNDERFGGKGVLKAVANVNETIADEILGLDAFNQTQLDDTLRELDGTNNYSNLGANATLGVSMATARAAAAALGMPLYRYLGGANASILPVPMCNIINGGAHANNNVDFQEFMIMPFGFTSFKEALRSVCEIYAILKKELANSGHSTALGDEGGFAPNLANNTEPIDLLMTCIKKAGYENRVKIALDVASTEFFKDGKYHMEGKAFSSEALIERYVELCAKYPICSIEDGLAENDFEGWIKLTEKLGNKIQLVGDDLFVTNEDILREGIIKKMANAVLIKPNQIGTITQTMRTVRLAQRNNYKCVMSHRSGESEDAFIADFAVALNTGQIKTGALARGERTAKYNRLLEIEFESDEYLGEKL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AL111168
EMBL· GenBank· DDBJ
CAL35768.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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