A0A1F6YI57 · A0A1F6YI57_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

Lacks conserved residue(s) required for the propagation of feature annotation.
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 site171(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Active site213Proton donor
Binding site251Mg2+ (UniProtKB | ChEBI)
Binding site294Mg2+ (UniProtKB | ChEBI)
Binding site321Mg2+ (UniProtKB | ChEBI)
Active site346Proton acceptor
Binding site346(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site375(2R)-2-phosphoglycerate (UniProtKB | ChEBI)
Binding site398(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
      A2192_02680

Organism names

Accessions

  • Primary accession
    A0A1F6YI57

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
Domain4-134Enolase N-terminal
Domain147-423Enolase C-terminal TIM barrel

Sequence similarities

Belongs to the enolase family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    423
  • Mass (Da)
    45,956
  • Last updated
    2017-02-15 v1
  • MD5 Checksum
    857254BDEE2AB0F89FDA51472D0192C2
MSKIKSIKAREILASGGTPSVEAEVELESGVAEKASVSFGVSAGKHEAAVIFDGDMDRYGGKGMLKAVENIENQIAVEILGMEVTEQREIDEKMIGLDGTEDKSRLGGNAILAVSMAVARAAAKDEGVPLYKYLGSVFGMDPSTVLRTSLPKPMMVMIEGGKHAVNTTDIQEYLCMPKGLESAKAAIERNQEIYSQLGEVLKKNGLSTNVGNEGAYAPDGIESNEKPLKYLVEAIETLGLRPGEDAVLGIDAAASEFYQNGKYNLDRDGVSMDGENLIEYWLKWIEKYPIATVEDLLFEDDWENWTKLTARLPSGVLNIGDDLTATNSKRWQKAIDTKAANSILIKLNQAGTVSETMDCCILAKVHGLPTIPSHRGGGETDDTFLVDLAVAVGSKYIKVGPTRGERVVKYNRLMEIEEEIKEN

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
MFVW01000025
EMBL· GenBank· DDBJ
OGJ06078.1
EMBL· GenBank· DDBJ
Genomic DNA

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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