A0A2N3B6Y2 · A0A2N3B6Y2_9PROT

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 site156substrate
Binding site164(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site165substrate
Active site206Proton donor
Binding site243Mg2+ (UniProtKB | ChEBI)
Binding site286Mg2+ (UniProtKB | ChEBI)
Binding site286substrate
Binding site313Mg2+ (UniProtKB | ChEBI)
Binding site313substrate
Active site338Proton acceptor
Binding site338(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site365-368substrate
Binding site367(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site368(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site389(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site389substrate

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
      CVT87_00485

Organism names

Accessions

  • Primary accession
    A0A2N3B6Y2

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
Domain4-135Enolase N-terminal
Domain140-426Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    428
  • Mass (Da)
    45,157
  • Last updated
    2018-04-25 v1
  • MD5 Checksum
    EF257AACFBD1F2467B53A8479721772D
MTAIIDLHGREILDSRGNPTVEVDVLLEDGSFGRAAVPSGASTGAHEAVELRDGDAARYLGKGVLKAIEAVNSEIRDLLIDNFDAEDQRDVDLALIALDGTHNKARLGANAILGTSLAVAKAAANARGLPLYSYLGGVSAHLLPVPMMNIINGGEHADNPIDIQEFMIMPVGADSIAEAVRWGSEVFHTLKKGLSQKGLATSVGDEGGFAPDLASTRAALDFIMESITKAGFTPGEDMVLALDCAATEFFKNGRYEISGEGLSMSGEEMADYLAKLCDDYPIRSIEDGMSEDDFAGWAALTAKIGDKVQLVGDDLFVTNPARLSDGIANGLANSLLVKVNQIGTLTETLAAVDMAHRARYTCVMSHRSGETEDATIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEELGDSAAFAGKGCFGGRC

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
PHDZ01000013
EMBL· GenBank· DDBJ
PKP67215.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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