{PDOC00152} {PS00168; TRP_SYNTHASE_BETA} {BEGIN} ********************************************************************** * Tryptophan synthase beta chain pyridoxal-phosphate attachment site * ********************************************************************** Tryptophan synthase (EC 4.2.1.20) catalyzes the last step in the biosynthesis of tryptophan: the conversion of indoleglycerol phosphate and serine, to tryptophan and glyceraldehyde 3-phosphate [1,2]. It has two functional domains: one for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate and the other for the synthesis of tryptophan from indole and serine. In bacteria and plants [3], each domain is found on a separate subunit (alpha and beta chains), while in fungi the two domains are fused together on a single multifunctional protein. The beta chain of the enzyme requires pyridoxal-phosphate as a cofactor. The pyridoxal-phosphate group is attached to a lysine residue. The region around this lysine residue also contains two histidine residues which are part of the pyridoxal-phosphate binding site. The signature pattern for the tryptophan synthase beta chain is derived from that conserved region. -Consensus pattern: [LIVMYAHQ]-x-[HPYNVF]-x-G-[STA]-H-K-x-N-x(2)-[LIVM]-x- [QEH] [K is the pyridoxal-P attachment site] -Sequences known to belong to this class detected by the pattern: ALL. -Other sequence(s) detected in Swiss-Prot: NONE. -Last update: December 2004 / Pattern and text revised. [ 1] Crawford I.P. "Evolution of a biosynthetic pathway: the tryptophan paradigm." Annu. Rev. Microbiol. 43:567-600(1989). PubMed=2679363; DOI=10.1146/annurev.mi.43.100189.003031 [ 2] Hyde C.C., Miles E.W. "The tryptophan synthase multienzyme complex: exploring structure-function relationships with X-ray crystallography and mutagenesis." Biotechnology (N.Y.) 8:27-32(1990). PubMed=1366510 [ 3] Berlyn M.B., Last R.L., Fink G.R. "A gene encoding the tryptophan synthase beta subunit of Arabidopsis thaliana." Proc. Natl. Acad. Sci. U.S.A. 86:4604-4608(1989). PubMed=2734310 -------------------------------------------------------------------------------- PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see https://prosite.expasy.org/prosite_license.html -------------------------------------------------------------------------------- {END}