A0A150IUQ6 · A0A150IUQ6_9EURY

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 site161substrate
Binding site169(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site170substrate
Active site213Proton donor
Binding site248Mg2+ (UniProtKB | ChEBI)
Binding site291Mg2+ (UniProtKB | ChEBI)
Binding site291substrate
Binding site318Mg2+ (UniProtKB | ChEBI)
Binding site318substrate
Active site343Proton acceptor
Binding site343(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site370-373substrate
Binding site372(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site373(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site394(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site394substrate

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
      AMQ74_01582

Organism names

  • Taxonomic identifier
  • Strain
    • U1lsi0528_Bin089
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Candidatus Methanofastidiosia > Candidatus Methanofastidiosales > Candidatus Methanofastidiosaceae > Candidatus Methanofastidiosum

Accessions

  • Primary accession
    A0A150IUQ6

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
Domain12-140Enolase N-terminal
Domain145-431Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    432
  • Mass (Da)
    47,170
  • Last updated
    2016-06-08 v1
  • Checksum
    878E6DE70816B676
MLNAKDFEMFEIIDIKSREVLDSRGNPTIETEIITGGGYGSAIVPSGASTGKHEALELRDKNDRYGGKGVLNAVRNVNEKITPLLIGMDIRKQREIDRVMIEEDGTENKSNLGANAILSVSLAAARCAADTINVPLYQYLGGLNTYVLPVPMMNVINGGEHAGNELDFQEFMIMPVGAKSFSEALRICAEVYHQMKKVISKKYGKSSTNVGDEGGYAPPMKEISEPLEVIMSTLEELSYKDIVKIALDTASSTFYDEKTGTYNAMGKKMSPGELIDLFADVSSKYPIISIEDPMAEDDFEGFVEITKKLGKKIQIVGDDLFVTNKNRLSNGIKKGACNSLLLKVNQIGSLTEAIDTASLAYRSGYSVVVSHRSGETEDTMIADLAVGISSGQIKTGAPSRSERCAKYNRLLRIEEYLGESAVYAGKNFRIPF

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LNGD01000136
EMBL· GenBank· DDBJ
KYC48682.1
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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