A0A3S7JA46 · A0A3S7JA46_9PROT

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

Protein has several cofactor binding sites:
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds a second Mg2+ ion via substrate during catalysis.
Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Mg2+ is required for catalysis and for stabilizing the dimer.

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 site155substrate
Binding site163(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site164substrate
Active site205Proton donor
Binding site242Mg2+ (UniProtKB | ChEBI)
Binding site286Mg2+ (UniProtKB | ChEBI)
Binding site286substrate
Binding site313Mg2+ (UniProtKB | ChEBI)
Binding site313substrate
Active site338Proton acceptor
Binding site338(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site365-368substrate
Binding site367(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site368(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site389(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site389substrate

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
    • ORF names
      CKSOR_00430

Organism names

Accessions

  • Primary accession
    A0A3S7JA46

Proteomes

Subcellular Location

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

Keywords

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-134Enolase N-terminal
Domain139-426Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    429
  • Mass (Da)
    46,862
  • Last updated
    2019-05-08 v1
  • Checksum
    F0F979E9078E0109
MNTIVDIIGREILDSRGQPTVECDVILESGIIGRASVPSGASTGSREALELRDEDSNRYLGKGVLKAVENINNEISESLIGLDSQNQKLIDNILIDLDGTENKERLGANAILATSMAVLKAAAQQSNLPLYRYLGGIGPISMPVPMMNIINGGAHANNNLDIQEFMIIPVGAKSFREALRWGSEIFQILKKIIHNKGLSTAVGDEGGFAPNISNHDEAIKLIIKAIIDAGYEPGNQIFLGLDCACSELYHDGKYVLKSEGNLSLNSKDFVNILSNWCDQYPIITIEDGMSENDWDGWALLTEKLGSKIQLVGDDLFVTNSKILKEGINKKIANSILIKINQIGTITETFEAIDMAKRNGYSSIISHRSAETEDTTIADIAVGTNVMQIKTGSLSRSDRMAKYNQLLRIEEELTTSSIYAGYNAFSKFKI

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP025628
EMBL· GenBank· DDBJ
AWD32543.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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