B2SUA6 · ENO_XANOP

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 site165(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Active site207Proton donor
Binding site244Mg2+ (UniProtKB | ChEBI)
Binding site287Mg2+ (UniProtKB | ChEBI)
Binding site314Mg2+ (UniProtKB | ChEBI)
Active site339Proton acceptor
Binding site339(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site368(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site369(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site390(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
      PXO_00171

Organism names

Accessions

  • Primary accession
    B2SUA6

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_10001159341-430Enolase

Interaction

Subunit

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

Structure

Family & Domains

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    46,015
  • Last updated
    2008-07-01 v1
  • Checksum
    DD2FA4CF68FA21A1
MTTIAKILAREILDSRGNPTLEAEVTLDDGSFGRAAVPSGASTGTKEAVELRDGDKTRYLGKGVRHAVDNVNGTIAETLKNFDAADQQGLDRRLIDLDGTENKGRLGANALLGVSLAAAHAVAASRKQPLWQYLSTITESDVALPVPMMNIINGGAHADNNVDFQEFMVLPVGCSSFSEALRAGTEIFYSLKSVLKGHGLSTAVGDEGGFAPDFRSNVEALDTILEAIGKAGYTAGEDILLGLDVASSEFYDNGKYNLVGENKRLTSEQFVDFLADWVAQYPIISIEDGLAEDDWAGWKLLTDRVGKHVQLVGDDLFVTNPKIFKQGIDSGTANAILIKVNQIGTLTETLEAIAMAHAANYASIVSHRSGETEDTTIADIAVATTATQIKTGSLCRSDRVAKYNQLLRIEQALGSDARYAGRDAFVSIKR

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP000967
EMBL· GenBank· DDBJ
ACD58296.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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