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Annotation rule MF_00318
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General rule information [?]

Accession MF_00318
Dates 1-JUN-2001 (Created)
10-OCT-2014 (Last updated, Version 53)
Name Enolase
Scope Bacteria
Templates P0A6P9 (ENO_ECOLI); Q8GR70 (ENO_ENTHR); P37869 (ENO_BACSU); Q97QS2 (ENO_STRPN): [Recover all]

Propagated annotation [?]

Identifier, protein and gene names [?]

Protein name
RecName: Full=Enolase;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=2-phosphoglycerate dehydratase;
Gene name

Comments [?]

Function Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis.
Catalytic activity 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.
case <FTGroup:1>
Cofactor Mg(2+)
end case
case <FTTag:inhib>
Enzyme regulation The covalent binding to the substrate causes inactivation of the enzyme, and possibly serves as a signal for the export of the protein.
end case
case <OC:Gammaproteobacteria>
Subunit Component of the RNA degradosome, which is a multiprotein complex involved in RNA processing and mRNA degradation.
end case
Subcellular location Cytoplasm. Secreted. Cell surface. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the cell surface.
Similarity Belongs to the enolase family.

Keywords [?]

case <FTGroup:1>
end case

Gene Ontology [?]

case <FTGroup:1>
GO:0000287; Molecular function: magnesium ion binding.
end case
GO:0004634; Molecular function: phosphopyruvate hydratase activity.
GO:0006096; Biological process: glycolytic process.
GO:0005737; Cellular component: cytoplasm.
GO:0009986; Cellular component: cell surface.

Cross-references [?]

Pfam PF00113; Enolase_C; 1;
PF03952; Enolase_N; 1;
PIRSF PIRSF001400; Enolase; 1;
TIGRFAMs TIGR01060; Eno; 1;

Features [?]

From: ENO_ECOLI (P0A6P9)
Key     From     To       Description   Tag   Condition   FTGroup
REGION     369     372       Substrate binding     S-H-R-S  
ACT_SITE     209     209       Proton donor     [ED]  
ACT_SITE     342     342       Proton acceptor     K  
METAL     246     246       Magnesium     D   1
METAL     290     290       Magnesium     E   1
METAL     317     317       Magnesium     D   1
BINDING     159     159       Substrate     H  
BINDING     168     168       Substrate     [ED]  
BINDING     290     290       Substrate     E  
BINDING     317     317       Substrate     D  
BINDING     342     342       Substrate (covalent); in inhibited form   inhib   K  
BINDING     393     393       Substrate     K  

Additional information [?]

Size range 369-550 amino acids
Related rules None
Fusion None