Essential maintenance is planned to begin on Tue Jan 28 2025. The website may be temporarily unavailable. Please use our fallback: https://wwwdev.ebi.ac.uk/uniprot/front-end/fallback/ during this time.

Q703Y8 · Q703Y8_THETE

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.

Type
IDPosition(s)Description
Binding site147substrate
Binding site156(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site157substrate
Active site200Proton donor
Binding site236Mg2+ (UniProtKB | ChEBI)
Binding site279Mg2+ (UniProtKB | ChEBI)
Binding site279substrate
Binding site305Mg2+ (UniProtKB | ChEBI)
Binding site305substrate
Active site330Proton acceptor
Binding site330(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site357-360substrate
Binding site359(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site360(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site381(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site381substrate

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

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Archaea > Thermoproteota > Thermoprotei > Thermoproteales > Thermoproteaceae > Thermoproteus

Accessions

  • Primary accession
    Q703Y8

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
Domain5-126Enolase N-terminal
Domain131-410Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    412
  • Mass (Da)
    44,055
  • Last updated
    2004-07-05 v1
  • MD5 Checksum
    AB2ED189B0AD0A8501B9A0EA5D94E30B
MDTTIEELLARRILTGRGDQTIEVEVYTADGFGKAAAPAGASKGKHEVAFLPEGGIDAALSAFERLVSPELAGVDAAEQYAVDGKLEEVDGTGRFERIGGAVAIAVSMAAARAAANTLGIPLFRHLGGAPARTLPLPLGNAIGGGKHSRGLGPDLQEFLVIPLNPPDIATAVLANLEVHKRALKYIVKADPHFTGGKNDEGAWTPRISAETALKILKESAAEVSKEIGVEIGLGVDAAASSLWNGSKYVYQNEGKERGPREQLEYMARLLDEFGLVYLEDPFHEDDFQSFAELTSRFKDRLIVGDDLYVTNAARIERGGREGATTAALIKPDQTGTLTRAHEAVKTARRYGMRIVVSHRSGDTEYDTLAHIAVAFGAEVIKTGIVGGERTAKLNELIRIGDYLGKWGRISSL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AJ621325
EMBL· GenBank· DDBJ
CAF18506.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
Help