A0A0E0TFI0 · A0A0E0TFI0_GEOS2

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 site287Mg2+ (UniProtKB | ChEBI)
Binding site287substrate
Binding site314Mg2+ (UniProtKB | ChEBI)
Binding site314substrate
Active site339Proton acceptor
Binding site339(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site366-369substrate
Binding site368(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site369(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site390(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site390substrate

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
    • Ordered locus names
      GYMC52_3161

Organism names

Accessions

  • Primary accession
    A0A0E0TFI0

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
Domain139-427Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    46,604
  • Last updated
    2015-05-27 v1
  • Checksum
    F995D5AD79A180FB
MSAIIDVYAREVLDSRGNPTVEVEVYTEDGGFGRALVPSGASTGEYEAVELRDGDKNRYLGKGVLKAVENVNEIIAPEIIGLEVADQVAIDRKLIELDGTENKSKLGANAILGVSLAVARAAADELGLPLYQYLGGFNAKTLPVPMMNILNGGAHADNNVDIQEFMIMPVGAESFREALRMGAEIFHSLKAVLKAKGYNTAVGDEGGFAPNLKSNEEALQTIIEAIEKAGYKPGEQVMLAMDVASSELYNKEDGKYHLEGEGVVKTSEEMVAWYEELVSKYPIISIEDGLDENDWEGHKLLTERLGKKVQLVGDDLFVTNTKKLAEGIEKGVGNSILIKVNQIGTLTETFDAIEMAKRAGYTAVVSHRSGETEDSTIADIAVATNAGQIKTGAPSRTDRVAKYNQLLRIEDELGHTAIYQGIRSFYNLKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP002442
EMBL· GenBank· DDBJ
ADU95519.1
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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