F0V270 · F0V270_MYCS3

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

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

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

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 site179(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Active site221Proton donor
Binding site261Mg2+ (UniProtKB | ChEBI)
Binding site315Mg2+ (UniProtKB | ChEBI)
Binding site342Mg2+ (UniProtKB | ChEBI)
Active site367Proton acceptor
Binding site367(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site396(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site397(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site418(2R)-2-phosphoglycerate (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

Gene names

    • Name
      eno
    • ORF names
      MSUIS_06580

Organism names

Accessions

  • Primary accession
    F0V270

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, region, compositional bias.

TypeIDPosition(s)Description
Domain5-144Enolase N-terminal
Domain155-450Enolase C-terminal TIM barrel
Region502-540Disordered
Compositional bias514-540Basic and acidic residues

Sequence similarities

Belongs to the enolase family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    540
  • Mass (Da)
    58,736
  • Last updated
    2011-05-03 v1
  • Checksum
    243E731FF9CD2355
MAFSIENLFAYELIDSRGNPTVACIAKVAKGKFLSKKSFTAKVLVPSGASTGAKEALELRDGDSSRFGGKGVKKAVHYINYVLGPSLIENDVNPADQAELDRFLMDLDGTENKSRYGANTILAVSLSVAKAVAKAKGLPFYQYVAELSGNPKVRKYVLPLPMVNVINGGAHSDNSLDFQEFMFVPVGASSMHEAVRISAECFHALAKYLKSKGLSTAKGDEGGFAPNFNSNEEALNAMLIAIANAGYKAGVIHGHVAIALDCAASELYDSNTKLYKFKKMIKAGCLSEEAGTKGTVQMIDYYVDLVEKYPIISIEDPLAEDDYEGFALLQKRIGKKVQIVGDDLYCTNPELTQMGIEKGLSNSVLIKVNQIGTLSETLNTMSLAKKAGWSCIISHRSGETEDTTIADIAVGTAAGQIKTGSFSRSERIAKYNRLLEIEIDLTSVNSTFYGLYSLFSLDFNNTELFKAKSYMVNERTGEVKCEVLKAELDQSFNKTSQIFDGVSAGVNPSEESEIKSMEAQKIEDDQEGEDKKKKSRFSKS

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias514-540Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
FQ790233
EMBL· GenBank· DDBJ
CBZ40751.1
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.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp