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| HAMAP annotation rule MF_00318 |
| Accession | MF_00318 |
| Dates | 1-JUN-2001 (Created) 9-JUN-2011 (Last updated, Version 49) |
| Name | Enolase |
| Scope | Bacteria Archaea |
| Triggered by |
| Identifier |
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| Protein name |
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| Gene name |
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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
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. |
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.
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
| 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; |
| From: ENO_ECOLI (P0A6P9) | ||||||||||||
| Key | From | To | Description | Tag | 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>
end case
| From: ENO_BACSU (P37869) | ||||||||||||
| MOD_RES (Optional) | 281 | 281 | Phosphotyrosine (By similarity) | Y | ||||||||
| Size range: | 398-458 amino acids |
| Related Rules: | None |
| Templates: | P0A6P9 (ENO_ECOLI); Q8GR70 (ENO_ENTHR); P37869 (ENO_BACSU); Q97QS2 (ENO_STRPN): [Recover all] |
| Fusion: | None |