M0B9V9 · M0B9V9_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 site146substrate
Binding site154(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site155substrate
Active site196Proton donor
Binding site232Mg2+ (UniProtKB | ChEBI)
Binding site275Mg2+ (UniProtKB | ChEBI)
Binding site275substrate
Binding site302Mg2+ (UniProtKB | ChEBI)
Binding site302substrate
Active site327Proton acceptor
Binding site327(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site354-357substrate
Binding site356(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site357(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site378(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site378substrate

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
      C479_15722

Organism names

  • Taxonomic identifier
  • Strain
    • JCM 14624
  • Taxonomic lineage
    Archaea > Euryarchaeota > Stenosarchaea group > Halobacteria > Halobacteriales > Natrialbaceae > Halovivax

Accessions

  • Primary accession
    M0B9V9

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
Domain4-124Enolase N-terminal
Domain130-401Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    401
  • Mass (Da)
    41,965
  • Last updated
    2013-04-03 v1
  • Checksum
    595240CC207E351F
MTLITDVRLREILDSRGNPTVEADVVTESGGFGRAAAPSGASTGEYEAVERPTGEAIAAARERAVPRLVGEAYAGNQREVDAILRAADGTDTFSELGANSAVAISMAAAKAGADVLGAPLFQHLGGTFRGETFPTPLGNVVGGGEHAADATDIQEFLAAPVGAPSVQDAVFANAAVHAAVADILDERGEPAGKGDEGAWAPSITDAEAFEVVDEAVNRVENEVGFEVGIGLDVAAAELYDADAGEYVYSDRTRSTDEQIAYVADLVSEYDLVYVEDPLDEDDYEAYADLTDRVGDQTLVCGDDLFVTNVDRLREGIDRGAANSILIKPNQIGTLSDAFDAIELATEHGYEAVVSHRSGETEDTTIAHLAVATDAAFIKTGAVGGERTAKLNELIRIEDDAI

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AOIQ01000024
EMBL· GenBank· DDBJ
ELZ07068.1
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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