CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.90 | Alpha-Beta Complex |
|
3.90.226 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
|
3.90.226.10 | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
Domain Context
CATH Clusters
| Superfamily | 2-enoyl-CoA Hydratase; Chain A, domain 1 |
| Functional Family | ATP-dependent Clp protease proteolytic subunit |
Enzyme Information
| 3.4.21.92 |
Endopeptidase Clp.
based on mapping to UniProt P80244
Hydrolysis of proteins to small peptides in the presence of ATP and magnesium. Alpha-casein is the usual test substrate. In the absence of ATP, only oligopeptides shorter than five residues are hydrolyzed (such as succinyl-Leu-Tyr-|-NHMec, and Leu-Tyr-Leu-|-Tyr-Trp, in which cleavage of the -Tyr-|-Leu- and -Tyr-|-Trp bonds also occurs).
-!- Belongs to peptidase family S14.
|
UniProtKB Entries (1)
| P80244 |
CLPP_BACSU
Bacillus subtilis subsp. subtilis str. 168
ATP-dependent Clp protease proteolytic subunit
|
PDB Structure
| PDB | 3TT6 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
Structural insights into the conformational diversity of ClpP from Bacillus subtilis
Mol.Cells
|