CATH Domain 1pzqB01
|1.20.5||Single alpha-helices involved in coiled-coils or other helix-helix interfaces|
|188.8.131.520||Docking domain of the erythromycin polyketide synthase (DEBS)|
|Superfamily||Docking domain of the erythromycin polyketide synthase (DEBS)|
|Functional Family||6-deoxyerythronolide-B synthase EryA2, modules 3 and 4|
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)
6-deoxyerythronolide-B synthase EryA2, modules 3 and 4
The structure of docking domains in modular polyketide synthases.