CATH Classification

Domain Context

CATH Clusters

Superfamily Docking domain of the erythromycin polyketide synthase (DEBS)
Functional Family 6-deoxyerythronolide-B synthase EryA2, modules 3 and 4

Enzyme Information
6-deoxyerythronolide-B synthase.
based on mapping to UniProt Q03132
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)

Saccharopolyspora erythraea
6-deoxyerythronolide-B synthase EryA2, modules 3 and 4

PDB Structure

External Links
Organism Escherichia
Primary Citation
The structure of docking domains in modular polyketide synthases.
Broadhurst, R.W., Nietlispach, D., Wheatcroft, M.P., Leadlay, P.F., Weissman, K.J.