A0A4R8GI03 · A0A4R8GI03_9FIRM

  • Protein
    Enolase
  • Gene
    eno
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    3/5

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.

Type
IDPosition(s)Description
Binding site155substrate
Binding site163(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site164substrate
Active site205Proton donor
Binding site243Mg2+ (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
    • ORF names
      C7959_14715

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MSL 6dP
  • Taxonomic lineage
    Bacteria > Bacillota > Clostridia > Halanaerobiales > Halobacteroidaceae > Orenia

Accessions

  • Primary accession
    A0A4R8GI03

Proteomes

Subcellular Location

Cytoplasm
Secreted
Cell surface
Note: Fractions of enolase are present in both the cytoplasm and on the cell surface.

Keywords

Interaction

Protein-protein interaction databases

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.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    428
  • Mass (Da)
    46,185
  • Last updated
    2019-07-31 v1
  • Checksum
    145AD0EA46EF0334
MFEIVEVLGREVLDSRGNPTVEVDVYLSGGAMGRAMVPSGASTGENEAVELRDGDKDRYRGKGVLQAVANVNETIATQVIGMDAREQVAIDRLMIELDGTSNKGDLGANAILGVSIAVAKAAAEQLGLPLYQYLGGVNAKELPVPMMNILNGGEHADSAVDVQEFMVMPVGFDTYREALRAGAEVFHALHAILAERGDVTAVGNEGGFAPRDLSGTEEAIETILEAIKKAGYTPDQDIKLALDVASSELVDEDGNYNFKREGVVRTTDEMVDFYEELVNKYPIISIEDGLGENDWEGWVKLTERLGDKVQIVGDDLFVTNTEFLAKGIEMGAANSILIKVNQIGTLTETLDAIELAKRNNMTAVVSHRSGETADDTIADLVVATNAGQIKTGSASRSDRMAKYNQLLRIEEELAETAQYNGLDNFYNL

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SOEG01000047
EMBL· GenBank· DDBJ
TDX45290.1
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.
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.
FeedbackHelp