A0A7I8DI44 · A0A7I8DI44_9FIRM

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 site157substrate
Binding site165(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site166substrate
Active site207Proton donor
Binding site244Mg2+ (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
      bsdcttw_10430

Organism names

Accessions

  • Primary accession
    A0A7I8DI44

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
Domain6-136Enolase N-terminal
Domain141-429Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    431
  • Mass (Da)
    45,753
  • Last updated
    2021-04-07 v1
  • Checksum
    6B448AE9053B9E2A
MNYLEIEKVIGREIIDSRGNPTVEAEVILKDGTIGRGAAPSGASTGIFEALELRDEDKSRFGGKGVLKAVANINGPISEALTGLNAADIYGVDAAMIALDGTKDKSGLGANAILAVSIAAARAAATSLMIPLYKFLGGSAGNKLPVPMMNILNGGAHAANTVDVQEFMIMPAGASSFKEGLRQCTEVFHALAKILKEKGLATSVGDEGGFAPDLASDEEAIQLILQAIEKAGYVPGKDFVLAMDAASSEWKGEKPGEYILPKAGTHFTSKELIAHWKGLTEKYPIVSIEDGLDEEDWEGWQLLTKELGDKIQLVGDDLFVTNTTRLKKGIELGCGNSILIKLNQIGSVSETLEAIKMAHKAGYTAISSHRSGETEDTTIADLAVALNTCQIKTGAPSRTERVAKYNQLLRIEEDLGASAQYPGFDAFNIKR

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AP023368
EMBL· GenBank· DDBJ
BCJ98002.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

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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