A0A0V0PTR3 · A0A0V0PTR3_9RHOB

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 site155substrate
Binding site163(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site164substrate
Active site205Proton donor
Binding site242Mg2+ (UniProtKB | ChEBI)
Binding site285Mg2+ (UniProtKB | ChEBI)
Binding site285substrate
Binding site312Mg2+ (UniProtKB | ChEBI)
Binding site312substrate
Active site337Proton acceptor
Binding site337(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site364-367substrate
Binding site366(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site367(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site388(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site388substrate

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
      AQY21_26125

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • MKU1
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Rhodobacterales > Paracoccaceae > Paracoccus

Accessions

  • Primary accession
    A0A0V0PTR3

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
Domain139-425Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    425
  • Mass (Da)
    44,907
  • Last updated
    2016-03-16 v1
  • Checksum
    121FA2A953851D04
MTAIIDIFAREILDSRGNPTVEVDVTLEDGTMGRAAVPSGASTGAHEAVEKRDGDKARYLGKGVLEAVAAVNGEIAENLIGEDATEQVAIDRMMIELDGTPNKGRLGANAILGVSLAVAKAAAEACSQPLYRYVGGAGARVLPVPMMNIINGGEHADNPIDIQEFMIMPVAAENIREAVRMGSEVFHTLKKELSSAGLATGVGDEGGFAPNLSSTRDALDFILKAIEKAGYQPGDDIMLALDCASTEYFKGGKYEMAGEGKSLSPAENVAYLEALCNDYPILSIEDGCAEDDWDGWKLLTDTLGGRVQLVGDDLFVTNPARLAEGIAKGCGNSLLVKVNQIGTLTETLDAVRMADRARYTSVMSHRSGETEDATIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEMLGAAAEYAGKSILRG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LLWQ01000221
EMBL· GenBank· DDBJ
KRW93322.1
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.
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