O69174 · ENO_STAAU

Function

function

Catalyzes the reversible conversion of 2-phosphoglycerate (2-PG) into phosphoenolpyruvate (PEP) (PubMed:26627653).
It is essential for the degradation of carbohydrates via glycolysis
'Moonlights' as a laminin receptor. Binds laminin when expressed on the bacterial cell surface; this probably induces destruction of the extracellular matrix, favoring invasion and dissemination.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds a second Mg2+ ion via substrate during catalysis.

Kinetics

KM SUBSTRATE pH TEMPERATURE[C] NOTES EVIDENCE
0.37 mM2-phosphoglycerate by octamer
kcat is 83 sec-1 for octamer.

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 site41phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site165(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Active site207Proton donor
Binding site244Mg2+ (UniProtKB | ChEBI)
Binding site291Mg2+ (UniProtKB | ChEBI)
Binding site318Mg2+ (UniProtKB | ChEBI)
Active site343Proton acceptor
Binding site343(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site343phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site372(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site372phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site373(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site373phosphoenolpyruvate (UniProtKB | ChEBI)
Binding site394(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site394phosphoenolpyruvate (UniProtKB | ChEBI)

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
    • Laminin-binding protein

Gene names

    • Name
      eno

Organism names

  • Taxonomic identifier
  • Strains
    • ISP3
    • ATCC 10832 / Wood 46
  • Taxonomic lineage
    Bacteria > Bacillota > Bacilli > Bacillales > Staphylococcaceae > Staphylococcus

Accessions

  • Primary accession
    O69174

Subcellular Location

Cytoplasm
Secreted
Cell surface
Note: Fractions of enolase are present in both the cytoplasm and on the cell surface (PubMed:15158195).
Once secreted, it remains attached to the cell surface (PubMed:15158195).

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis135No longer forms homooctamers.
Mutagenesis138No longer forms homooctamers.
Mutagenesis139Significantly impairs homooctamer formation, no enzymatic activity.
Mutagenesis140Significantly impairs homooctamer formation.
Mutagenesis355Significantly impairs homooctamer formation, no enzymatic activity.
Mutagenesis389Slightly decrease in homooctamer formation, octomeric form has about 50% activity, dimeric form has none.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001339701-434Enolase

Interaction

Subunit

Homodimer and homooctamer; the homodimer is inactive (PubMed:26627653).

Family & Domains

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    434
  • Mass (Da)
    47,117
  • Last updated
    1998-08-01 v1
  • Checksum
    C4A19BA3675429B3
MPIITDVYAREVLDSRGNPTVEVEVLTESGAFGRALVPSGASTGEHEAVELRDGDKSRYLGKGVTKAVENVNEIIAPEIIEGEFSVLDQVSIDKMMIALDGTPNKGKLGANAILGVSIAVARAAADLLGQPLYKYLGGFNGKQLPVPMMNIVNGGSHSDAPIAFQEFMILPVGATTFKESLRWGTEIFHNLKSILSQRGLETAVGDEGGFAPKFEGTEDAVETIIQAIEAAGYKPGEEVFLGFDCASSEFYENGVYDYSKFEGEHGAKRTAAEQVDYLEQLVDKYPIITIEDGMDENDWDGWKQLTERIGDRVQLVGDDLFVTNTEILAKGIENGIGNSILIKVNQIGTLTETFDAIEMAQKAGYTAVVSHRSGETEDTTIADIAVATNAGQIKTGSLSRTDRIAKYNQLLRIEDELFETAKYDGIKSFYNLDK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF065394
EMBL· GenBank· DDBJ
AAC17130.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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