CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.40 | 3-Layer(aba) Sandwich |
|
3.40.50 | Rossmann fold |
|
3.40.50.1820 | alpha/beta hydrolase |
Domain Context
CATH Clusters
| Superfamily | alpha/beta hydrolase |
| Functional Family |
Enzyme Information
| 2.3.1.94 |
6-deoxyerythronolide-B synthase.
based on mapping to UniProt Q03133
Propanoyl-CoA + 6 (2S)-methylmalonyl-CoA + 6 NADPH = 6-deoxyerythronolide B + 7 CoA + 6 CO(2) + H(2)O + 6 NADP(+).
-!- The product, 6-deoxyerythronolide B, contains a 14-membered lactone ring and is an intermediate in the biosynthesis of erythromycin antibiotics. -!- Biosynthesis of 6-deoxyerythronolide B requires 28 active sites that are precisely arranged along three large polypeptides, denoted DEBS1, -2 and -3. -!- The polyketide product is synthesized by the processive action of a loading didomain, six extension modules and a terminal thioesterase domain. -!- Each extension module contains a minimum of a ketosynthase (KS), an acyltransferase (AT) and an acyl-carrier protein (ACP). -!- The KS domain both accepts the growing polyketide chain from the previous module and catalyzes the subsequent decarboxylative condensation between this substrate and an ACP-bound methylmalonyl extender unit, introduce by the AT domain. -!- This combined effort gives rise to a new polyketide intermediate that has been extended by two carbon atoms.
|
UniProtKB Entries (1)
| Q03133 |
ERYA3_SACER
Saccharopolyspora erythraea
6-deoxyerythronolide-B synthase EryA3, modules 5 and 6
|
PDB Structure
| PDB | 1KEZ |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Crystal structure of the macrocycle-forming thioesterase domain of the erythromycin polyketide synthase: versatility from a unique substrate channel.
Proc.Natl.Acad.Sci.USA
|
