Protein Family Models

Date:

2024-08-14

Date:

2024-08-14

The C-terminal domain of Chalcone synthase is reported to be structurally similar to domains in thiolase and beta-ketoacyl synthase. The differences in activity are accounted for by differences in this N-terminal domain. [1]. 10426957. Structure of chalcone synthase and the molecular basis of plant polyketide biosynthesis. Ferrer JL, Jez JM, Bowman ME, Dixon RA, Noel JP;. Nat Struct Biol 1999;6:775-784. (from Pfam)

Date:

2024-10-16

This clade of hydroxymethylglutaryl-CoA (HMG-CoA) synthases is found in a limited spectrum of mostly gram-positive bacteria which make isopentenyl pyrophosphate (IPP) via the mevalonate pathway. This pathway is found primarily in eukaryotes and archaea, but the bacterial homologs are distinct, having aparrently diverged after being laterally transferred from an early eukaryote [1]. HMG-CoA synthase is the first step in the pathway and joins acetyl-CoA with acetoacetyl-CoA with the release of one molecule of CoA. The Borellia sequence may have resulted from a separate lateral transfer event.

Date:

2021-04-27

hydroxymethylglutaryl-CoA synthase family protein, similar to Haloferax volcanii hydroxymethylglutaryl-CoA synthase (HMG-CoA synthase) which catalyzes the condensation of acetyl-CoA with acetoacetyl-CoA, and Bacillus subtilis 3-hydroxy-3-methylglutaryl-ACP synthase PksG which catalyzes the condensation between the acetyl group attached to acyl-carrier-protein AcpK and a beta-ketothioester polyketide intermediate in a reaction analogous to that catalyzed by HMG-CoA synthase

Date:

2018-07-25