A0A449B6A1 · A0A449B6A1_9BACT

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 site159substrate
Binding site167(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site168substrate
Active site209Proton donor
Binding site250Mg2+ (UniProtKB | ChEBI)
Binding site310Mg2+ (UniProtKB | ChEBI)
Binding site310substrate
Binding site337Mg2+ (UniProtKB | ChEBI)
Binding site337substrate
Active site362Proton acceptor
Binding site362(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site389-392substrate
Binding site391(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site392(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site413(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site413substrate

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
      NCTC10179_00310

Organism names

  • Taxonomic identifier
  • Strain
    • NCTC10179
  • Taxonomic lineage
    Bacteria > Mycoplasmatota > Mycoplasmoidales > Metamycoplasmataceae > Mycoplasmopsis

Accessions

  • Primary accession
    A0A449B6A1

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
Domain4-138Enolase N-terminal
Domain143-450Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    455
  • Mass (Da)
    49,433
  • Last updated
    2019-05-08 v1
  • Checksum
    1B7D03D68CF34730
MSAIKKIHAREVLDSRGNPTVQVEVWTEYEGYGSAMVPSGASTGSREALELRDKGSKYEGNWFGGKGVMLAVDHVNQDLAPELLGMEVTDQRAIDLKMIALDGTANKEKMGANAILGVSLAVARAAANELQLPLYKYLGGFNGHQLPVPMLNVINGGEHASNTIDFQEFMIMPVGAKTFRESMQMANFVFHNLAKLLKKAGHGVQVGDEGGFAPNFKSHEEALDFLVEAIKAAGYVPARSGEKAVAIAMDCASSELYSDGVYTFGKLKAAIEAKKPGFEELQGVKLSYTTDEMIEYLGKLVDKYPIISIEDGLAEADWEGFAKFTKQYGDRLQIVGDDLTVTNTSILKRAIEEKSMNSILIKINQIGSLTETFEAIQMAQKANMTAVVSHRSGETEDSTIADIAVAMNAGQIKTGSMSRTDRIAKYNRLLAIEEELGSSAKFEGAKAFYNIKLNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LR215039
EMBL· GenBank· DDBJ
VEU76140.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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