AC   MF_00318;
DC   Protein; auto
TR   HAMAP; MF_00318; -; 1; level=0
XX
Names: Enolase
XX
ID   ENO
DE   RecName: Full=Enolase;
DE            EC=4.2.1.11;
DE   AltName: Full=2-phospho-D-glycerate hydro-lyase;
DE   AltName: Full=2-phosphoglycerate dehydratase;
GN   Name=eno;
XX
CC   -!- FUNCTION: Catalyzes the reversible conversion of 2-phosphoglycerate (2-
CC       PG) into phosphoenolpyruvate (PEP). It is essential for the degradation
CC       of carbohydrates via glycolysis.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R)-2-phosphoglycerate = H2O + phosphoenolpyruvate;
CC         Xref=Rhea:RHEA:10164, ChEBI:CHEBI:15377, ChEBI:CHEBI:58289,
CC         ChEBI:CHEBI:58702; EC=4.2.1.11;
case <FTGroup:1>
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC       Note=Binds a second Mg(2+) ion via substrate during catalysis.;
end case
CC   -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D-
CC       glyceraldehyde 3-phosphate: step 4/5.
case <OC:Gammaproteobacteria>
CC   -!- SUBUNIT: Component of the RNA degradosome, a multiprotein complex
CC       involved in RNA processing and mRNA degradation.
end case
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Secreted. Cell surface. Note=Fractions
CC       of enolase are present in both the cytoplasm and on the cell surface.
CC       Once secreted, it may remain attached to the cell surface.
CC   -!- SIMILARITY: Belongs to the enolase family.
XX
DR   Pfam; PF00113; Enolase_C; 1; trigger=no
DR   Pfam; PF03952; Enolase_N; 1; trigger=no
DR   PIRSF; PIRSF001400; Enolase; 1; trigger=no
DR   PRINTS; PR00148; ENOLASE; 1; trigger=no
DR   NCBIfam; TIGR01060; eno; 1; trigger=no
DR   PROSITE; PS00164; ENOLASE; 1; trigger=no
XX
KW   Secreted
KW   Cytoplasm
KW   Lyase
KW   Glycolysis
case <FTGroup:1>
KW   Magnesium
KW   Metal-binding
end case
XX
case <FTGroup:1>
GO   GO:0000287; F:magnesium ion binding
end case
GO   GO:0004634; F:phosphopyruvate hydratase activity
GO   GO:0006096; P:glycolytic process
GO   GO:0005737; C:cytoplasm
GO   GO:0009986; C:cell surface
XX
FT   From: ENO_ECOLI (P0A6P9)
FT   ACT_SITE        209
FT                   /note="Proton donor"
FT   Condition: [ED]
FT   ACT_SITE        342
FT                   /note="Proton acceptor"
FT   Condition: K
FT   BINDING         246
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         290
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: E
FT   BINDING         317
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT   Group: 1; Condition: D
FT   BINDING         167
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT   Condition: Q
FT   BINDING         342
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT   Condition: K
FT   BINDING         371
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT   Condition: R
FT   BINDING         372
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT                   /ligand="(2R)-2-phosphoglycerate"
FT   Condition: S
FT   BINDING         393
FT                   /ligand="(2R)-2-phosphoglycerate"
FT                   /ligand_id="ChEBI:CHEBI:58289"
FT   Condition: K
XX
Size: 369-550;
Related: None;
Template: P0A6P9; Q8GR70; P37869; Q97QS2; P9WNL1;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: None
 Cter: None
Duplicate: None
Plasmid: in STRTR
Comments: None
XX
# Revision 1.64 2024/01/30
//