A0A8I1G2E0 · A0A8I1G2E0_9GAMM

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 site159substrate
Binding site167(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site168substrate
Active site209Proton donor
Binding site246Mg2+ (UniProtKB | ChEBI)
Binding site289Mg2+ (UniProtKB | ChEBI)
Binding site289substrate
Binding site316Mg2+ (UniProtKB | ChEBI)
Binding site316substrate
Active site341Proton acceptor
Binding site341(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site368-371substrate
Binding site370(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site371(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site392(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site392substrate

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
      JHC11_01415

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KJE-2
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Gammaproteobacteria > Alteromonadales > Idiomarinaceae > Idiomarina

Accessions

  • Primary accession
    A0A8I1G2E0

Proteomes

Subcellular Location

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

Keywords

Interaction

Subunit

Component of the RNA degradosome, a multiprotein complex involved in RNA processing and mRNA degradation.

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain4-134Enolase N-terminal
Domain143-429Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    430
  • Mass (Da)
    45,816
  • Last updated
    2022-01-19 v1
  • Checksum
    BCF9B833F61DC983
MSNIVKVIGREIMDSRGNPTVEADVYLESGHMGRAAAPSGASTGSREALELRDGDKSRYLGKGVETAVANINGAIAEALSGIDATNQDAVDNIMLKLDGTDNKEKLGANAILAVSLAVAKAAALSKGIELYEHIANLNNTSGKYSMPLPMMNILNGGEHADNNVDIQEFMIQPVGAESFKEGLRMGAEVFYALKKVLQKRGLSTAVGDEGGFAPNLASNEEALQVIVEAVENAGYKMGSDITLALDCAASEFYRDGKYELSGEGKSFTAEEFADYLAELCDRYPIISIEDGLDESDWDGWKVLTEKLGSKVQLVGDDLFVTNTRILKEGIDKSIANSILIKFNQIGSLTETLAAIAMAREAGYSAVISHRSGETEDATIADLAVGTAAGQIKTGSLCRSDRVAKYNQLLRIEGDLNGQAPYRGRQEVNAG

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
JAEMOP010000002
EMBL· GenBank· DDBJ
MBJ7314663.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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