HAMAP annotation rule: MF_00318
Send feedback new


Accession MF_00318
Dates 1-JUN-2001 (Created)
9-JUN-2011 (Last updated, Version 49)
Data class Protein
Names Enolase



Identifier ENO
Protein name
RecName: Full=Enolase;
EC=4.2.1.11;
AltName: Full=2-phospho-D-glycerate hydro-lyase;
AltName: Full=2-phosphoglycerate dehydratase;
Gene name eno

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis. It is also a component of the RNA degradosome, a multi-enzyme complex involved in RNA processing and messenger RNA degradation. Its interaction with RNase E is important for the turnover of mRNA, in particular on transcripts encoding enzymes of energy-generating metabolic routes. Its presence in the degradosome is required for the response to excess phosphosugar. May play a regulatory role in the degradation of specific RNAs, such as ptsG mRNA, therefore linking cellular metabolic status with post-translational gene regulation (By similarity).
end case


case not <OC:Escherichia> and not <OC:Shigella> and not <OC:Salmonella>
FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate into phosphoenolpyruvate. It is essential for the degradation of carbohydrates via glycolysis (By similarity).
end case

CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + H(2)O.

case <FTGroup:1>
COFACTOR: Magnesium. Required for catalysis and for stabilizing the dimer (By similarity).
end case


case <FT:11>
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 (By similarity).
end case

PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-glyceraldehyde 3-phosphate: step 4/5.

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
SUBUNIT: Homodimer. Interacts with the C-terminal region of the endoribonuclease RNase E in the RNA degradosome (By similarity).
end case


case <OC:Streptococcus>
SUBUNIT: Homooctamer (By similarity).
end case


case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Secreted. Cell surface. Note=Fractions of enolase are present in both the cytoplasm and on the cell surface. As part of the bacterial cytoskeleton in the cytoplasm, is organized as extended coiled structures that wind around the cell, from one cell pole to the other. The export of enolase possibly depends on the covalent binding to the substrate; once secreted, it remains attached to the bacterial cell surface (By similarity).

else
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 (By similarity).
end case

SIMILARITY: Belongs to the enolase family.
Pfam PF00113; Enolase_C; 1;
PF03952; Enolase_N; 1;
PIRSF PIRSF001400; Enolase; 1;
PRINTS PR00148; ENOLASE; 1;
TIGRFAMs TIGR01060; Eno; 1;
PROSITE PS00164; ENOLASE; 1;

case <FT:13>
end case


case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
end case


case <FTGroup:1>
end case


case <FT:14>
end case

GO:0000287; Molecular function: magnesium ion binding.
GO:0004634; Molecular function: phosphopyruvate hydratase activity.
GO:0006096; Biological process: glycolysis.

case <OC:Escherichia> or <OC:Shigella> or <OC:Salmonella>
GO:0005856; Cellular component: cytoskeleton.
end case

GO:0005737; Cellular component: cytoplasm.
GO:0009986; Cellular component: cell surface.
From: ENO_ECOLI (P0A6P9)
Key     From     To       Description   Condition   FTGroup
REGION     369     372       Substrate binding (By similarity)   S-H-R-S  
ACT_SITE     209     209       Proton donor (By similarity)   E  
ACT_SITE     342     342       Proton acceptor (By similarity)   K  
 
METAL     246     246       Magnesium (By similarity)   D   1
METAL     290     290       Magnesium (By similarity)   E   1
METAL     317     317       Magnesium (By similarity)   D   1
 
BINDING     159     159       Substrate (By similarity)   H  
BINDING     168     168       Substrate (By similarity)   E  
BINDING     290     290       Substrate (By similarity)   E  
BINDING     317     317       Substrate (By similarity)   D  
BINDING     342     342       Substrate (covalent); in inhibited form (By similarity)   K  
BINDING     393     393       Substrate (By similarity)   K  
case <OC:Escherichia> or <OC:Shigella>
Key     From     To       Description   Condition   FTGroup
MOD_RES     257     257       N6-acetyllysine (By similarity)   K  
end case

From: ENO_BACSU (P37869)
Key     From     To       Description   Condition   FTGroup
MOD_RES (Optional)     281     281       Phosphotyrosine (By similarity)   Y  



Size range: 398-458 amino acids
Related UniRules: None
Template: P0A6P9 (ENO_ECOLI); Q8GR70 (ENO_ENTHR); P37869 (ENO_BACSU); Q97QS2 (ENO_STRPN): [Recover all]
Scope: Bacteria
Archaea
Fusion: Nter: None; Cter: None
Duplicate: in CHLTE, DESHY, LACGA, LACJO, LACLA, LACLS, LACPL, METCA, PSESM, STRCO
Plasmid encoded: in STRTR

View rule in raw text format (no links)