A0A1E7G1W6 · A0A1E7G1W6_LACLC

Function

function

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

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

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 site243Mg2+ (UniProtKB | ChEBI)
Binding site290Mg2+ (UniProtKB | ChEBI)
Binding site290substrate
Binding site317Mg2+ (UniProtKB | ChEBI)
Binding site317substrate
Active site342Proton acceptor
Binding site342(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site369-372substrate
Binding site371(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site372(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site393(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site393substrate

GO annotations

AspectTerm
Cellular Componentcell surface
Cellular Componentextracellular region
Cellular Componentpeptidoglycan-based cell wall
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
      AJ89_10915

Organism names

Accessions

  • Primary accession
    A0A1E7G1W6

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, region.

TypeIDPosition(s)Description
Domain4-134Enolase N-terminal
Region34-56Disordered
Domain139-430Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    433
  • Mass (Da)
    46,912
  • Last updated
    2017-02-15 v1
  • Checksum
    DEA9ED13BED764FE
MSIITDIYAREVLDSRGNPTLEVEVYTEDGAFGRGMVPSGASTGEHEAVELRDGDKSRYNGLGTQKAVDNVNNIIAEAIIGYEVTDQQAIDRAMIALDGTENKGKLGANAILGVSIAAARAAADELGVPLYNYLGGFNAKVLPTPMMNIINGGSHSDAPIAFQEFMIVPVGAPTFKEALRWGAEIFHALKKILKARGLETAVGDEGGFAPKFDGTEDGVETILKAIEAAGYKAGEDGVMIGFDCASSEFYENGVYDYTKFEGEGGKKLSASEQVDYLEELVSKYPIITIEDGMDENDWDGWKILTERLGKKVQLVGDDFFVTNTKYLERGIRENASNAILIKVNQIGTLTETFEAIEMAKEAGFTAIVSHRSGETEDSTISDIAVATNAGQIKTGSLSRTDRMAKYNQLLRIEDQLAEVAQYKGLKAFYNLKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JMMZ01000033
EMBL· GenBank· DDBJ
OEU38956.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
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