| Type: | Conserved_site | Name: | ADP-glucose pyrophosphorylase, conserved site |
| Description: | ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) [] () catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP.ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. It is a homotetramer in bacteria while in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits.There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. | Short Name: | ADP_Glu_pyroP_CS |
