Protein Domain : Acetolactate synthase, small subunit IPR004789

Type	Family
Description	Acetolactate synthases are a group of biosynthetic enzymes apparently found in plants, fungi and bacteria that are capable of de novosynthesis of the branched-chain amino acids [ ]. They can all synthesize acetolactate from pyruvate in the biosynthesis of valine, while some are also capable of synthesizing acetohydroxybutyrate from pyruvate and ketobutyrate during the biosynthesis of isoleucine. These enzymes generally require thiamin diphosphate, FAD and a divalent metal ion for catalysis, though some enzymes specific for acetolactate synthesis do not require FAD. They are composed of two subunits, a large catalytic subunit, and a smaller regulatory subunit which binds the natural modulators (valine, and in some cases leucine or isoleucine).These enzymes are the target for currently-used herbicides such as sulphonylureas and imidazolinones. Their restricted distribution also makes them potential targets for the development of novel antibacterial and antifungal compounds.This entry represents the small regulatory subunit of acetolactate synthase. It contains an ACT domain, which is a predicted regulatory ligand-binding fold often found in proteins regulated by small-molecule effectors [ ].
Short Name	Acetalactate_synth_ssu