A0A7K1HF39 · A0A7K1HF39_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.

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.

Type
IDPosition(s)Description
Binding site154substrate
Binding site162(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site163substrate
Active site204Proton donor
Binding site241Mg2+ (UniProtKB | ChEBI)
Binding site288Mg2+ (UniProtKB | ChEBI)
Binding site288substrate
Binding site315Mg2+ (UniProtKB | ChEBI)
Binding site315substrate
Active site340Proton acceptor
Binding site340(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site367-370substrate
Binding site369(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site370(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site391(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site391substrate

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
      GMD66_11415

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • BIOML-A25
  • Taxonomic lineage
    Bacteria > Bacteroidota > Bacteroidia > Bacteroidales > Tannerellaceae > Parabacteroides

Accessions

  • Primary accession
    A0A7K1HF39

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
Domain3-133Enolase N-terminal
Domain138-427Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    427
  • Mass (Da)
    45,718
  • Last updated
    2021-04-07 v1
  • MD5 Checksum
    8007E6B57AE8214AEE15F6336F963FDD
MEIVKVVGREVLDSRGNPTVEVDVHLASGAFGRAAVPSGASTGENEAIELRDGDKKRYGGKGVLKAVDNVNSVIAPAILGMSALNQREVDHKLIELDGTKTKSNLGANAMLGVSLAVAKAAANYLDLPLYRYIGGTNAYVLPVPMMNIINGGSHSDAPIAFQEFMIRPVGACCFREGLRMGAEVFHALKKVLHDRGLSTAVGDEGGFAPALDGTEDALNSIMAAIKAAGYEPGKDVTIAMDCASSEFYHDGVYDYTKFEGAKGAKRTAEQQVAYLSELVAKYPIDSIEDGMDENDWAGWKLLTEALGSKCQLVGDDLFVTNVEFLKKGIEEGCANSILIKVNQIGTLSETLDAIEMAHRNGYTSVTSHRSGETEDATIADIAVATNSGQIKTGSLSRSDRMAKYNQLLRIEEELGDLAVYGYKTYKK

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
WNCR01000004
EMBL· GenBank· DDBJ
MTU29800.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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