A0A1Q7JZ12 · A0A1Q7JZ12_9ARCH

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 site146substrate
Binding site155(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site156substrate
Active site199Proton donor
Binding site235Mg2+ (UniProtKB | ChEBI)
Binding site280Mg2+ (UniProtKB | ChEBI)
Binding site280substrate
Binding site306Mg2+ (UniProtKB | ChEBI)
Binding site306substrate
Active site331Proton acceptor
Binding site331(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site358-361substrate
Binding site360(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site361(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site382(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site382substrate

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
      AUJ08_07805

Organism names

Accessions

  • Primary accession
    A0A1Q7JZ12

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
Domain4-125Enolase N-terminal
Domain130-414Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    415
  • Mass (Da)
    44,917
  • Last updated
    2017-04-12 v1
  • Checksum
    38BAF3E23474F1AF
MPSITSVRGRIIFNSRGSKSIEIDVVTDNRFMGRACAPSGASVGKFEAQSFPDNKVEKALAAFNGNSKKFVGLQAESLQEVFDALRSIDKTDNYATIGGSVAYALSIAAVDSAAKALNIPLFKLLKASKPFSFPFPLGNILGGGAHAGPGTPDIQEILACPVGAKSIVEALEMNFKLHAETRKVIESIDRRFTYGRGDEGAWAPNVNNDRALEIVEKAVKNCGYTLGKDMAIGIDFASSSFWDEKNNVYDYARQGIKRDAGEQIEFANRLIRDYRLIYTEDPVHEGDFQSMATLTKKNPGIFVTGDDMLVTNACKVKEAVKYGACSGAILKVNQAGSLYDAMKFAEECDKNDIKIITSHRSGESIDSHISHIAIATGSKMIKTGVLGGERVAKLNELVRLTEYDLIEGMAELSSA

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MNFY01000295
EMBL· GenBank· DDBJ
OLC81152.1
EMBL· GenBank· DDBJ
Genomic DNA

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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