CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.1080 | Glutaconate Coenzyme A-transferase |
|
3.40.1080.10 | Glutaconate Coenzyme A-transferase |
Domain Context
CATH Clusters
| Superfamily | Glutaconate Coenzyme A-transferase |
| Functional Family | Acetate CoA-transferase YdiF |
Enzyme Information
| 2.8.3.8 |
Acetate CoA-transferase.
based on mapping to UniProt Q8X5X6
Acyl-CoA + acetate = a fatty acid anion + acetyl-CoA.
-!- The enzyme belongs to family I of CoA-transferases, which operate with a ping-pong kinetic mechanism. -!- The reaction takes place in two half-reactions and involves the formation of a CoA thioester intermediate with a glutamate residue. -!- Unlike EC 2.8.3.9, this enzyme exhibits maximal activity using acetate as the CoA acceptor. -!- Substrate range depends on the specific enzyme. -!- Typical substrates include butanoyl-CoA and pentanoyl-CoA.
|
UniProtKB Entries (1)
| Q8X5X6 |
YDIF_ECO57
Escherichia coli O157:H7
Acetate CoA-transferase YdiF
|
PDB Structure
| PDB | 2AHU |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystallographic trapping of the glutamyl-CoA thioester intermediate of family I CoA transferases.
J.Biol.Chem.
|
