A0A4R0P7V1 · A0A4R0P7V1_9HYPH

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.

TypeIDPosition(s)Description
Binding site154substrate
Binding site162(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site163substrate
Active site204Proton donor
Binding site241Mg2+ (UniProtKB | ChEBI)
Binding site284Mg2+ (UniProtKB | ChEBI)
Binding site284substrate
Binding site311Mg2+ (UniProtKB | ChEBI)
Binding site311substrate
Active site336Proton acceptor
Binding site336(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site363-366substrate
Binding site365(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site366(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site387(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site387substrate

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
      E0D97_14075

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • KCTC 52183
  • Taxonomic lineage
    Bacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Ahrensiaceae > Oricola

Accessions

  • Primary accession
    A0A4R0P7V1

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
Domain4-133Enolase N-terminal
Domain138-424Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    424
  • Mass (Da)
    44,769
  • Last updated
    2019-07-31 v1
  • Checksum
    4CB307D0915DDBA1
MSAIVDIIGRQIFDSRGNPTVEVDVVLDDGTMGRAAVPSGASTGAHEAVELRDGGDRYKGKGVSKAVDAVNGAIFDAIGGMDATQQSKIDATMIELDGTPNKASLGANAILGVSLAVAKAAALYCGMPLYRYVGGTNAHILPVPMMNIINGGAHADNPIDIQEFMIMPVGAESLTDAVRMGSEIFHTLKSALNKAGHNTGVGDEGGFAPNLRSTNEALDFIMSAVSSAGFTPGEDVRLALDCAASEYYRKGRYELSGEGKSLSSEENAAYLEELVNNYPIISIEDGMHEDDWDGWKILTEKIGSKCQLVGDDLFVTNTARLRDGIKMGVGNSILVKVNQIGSLTETLDAVETAHKAGYTAVMSHRSGETEDATIADLAVATNCGQIKTGSLARSDRLAKYNQLIRIEEELGRLAHYAGPGILRA

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
SJST01000006
EMBL· GenBank· DDBJ
TCD13130.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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