CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.47 | Peroxisomal Thiolase; Chain A, domain 1 |
|
3.40.47.10 | Thiolase/Chalcone synthase |
Domain Context
CATH Clusters
| Superfamily | 3.40.47.10 |
| Functional Family |
Enzyme Information
| 2.3.1.9 |
Acetyl-CoA C-acetyltransferase.
based on mapping to UniProt P07097
2 acetyl-CoA = CoA + acetoacetyl-CoA.
-!- The enzyme, found in both eukaryotes and prokaryotes, catalyzes the Claisen condensation of an acetyl-CoA and an acyl-CoA (often another acetyl-CoA), leading to the formation of an acyl-CoA that is longer by two carbon atoms. -!- The reaction starts with the acylation of a nucleophilic cysteine at the active site, usually by acetyl-CoA but potentially by a different acyl-CoA, with concomitant release of CoA. -!- In the second step the acyl group is transferred to an acetyl-CoA molecule. -!- Cf. EC 2.3.1.16.
|
UniProtKB Entries (1)
| P07097 |
THIL_ZOORA
Zoogloea ramigera
Acetyl-CoA acetyltransferase
|
PDB Structure
| PDB | 2VU0 |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | |
| Primary Citation |
The sulfur atoms of the substrate CoA and the catalytic cysteine are required for a productive mode of substrate binding in bacterial biosynthetic thiolase, a thioester-dependent enzyme.
FEBS J.
|