Catalyzes the formation of acetolactate from pyruvate, the first step in valine and isoleucine biosynthesis. Requires FAD, thiamine pyrophosphate and Mg. Inhibited by the sulphonylurea herbicide, chlorsulphuron, and the imidazolinone herbicide, imazapyr. The obtained crystal structure of acetohydroxyacid synthase AHAS, EC 2.2.1.6)in complex with herbicides of the sulphonylurea and imidazolinone family reveals the molecular basis for substrate/inhibitor binding.
Computational Description
chlorsulfuron/imidazolinone resistant 1 (CSR1); FUNCTIONS IN: acetolactate synthase activity, pyruvate decarboxylase activity; INVOLVED IN: branched chain family amino acid biosynthetic process; LOCATED IN: chloroplast; EXPRESSED IN: 24 plant structures; EXPRESSED DURING: 15 growth stages; CONTAINS InterPro DOMAIN/s: TPP-binding enzyme, conserved site (InterPro:IPR000399), Thiamine pyrophosphate enzyme, central domain (InterPro:IPR012000), Acetolactate synthase, large subunit, biosynthetic (InterPro:IPR012846), Thiamine pyrophosphate enzyme, N-terminal TPP-binding domain (InterPro:IPR012001), Thiamine pyrophosphate enzyme, C-terminal TPP-binding (InterPro:IPR011766); BEST Arabidopsis thaliana protein match is: Thiamine pyrophosphate dependent pyruvate decarboxylase family protein (TAIR:AT5G17380.1); Has 30963 Blast hits to 30605 proteins in 2694 species: Archae - 488; Bacteria - 17421; Metazoa - 266; Fungi - 871; Plants - 599; Viruses - 25; Other Eukaryotes - 11293 (source: NCBI BLink).
