Conserved Site

Tryptophan synthase, beta chain, conserved site (IPR006653)

Short name: Trp_synth_b_CS


Tryptophan synthase catalyzes the last step in the biosynthesis of tryptophan [PMID: 2679363, PMID: 1366510]: L-serine + 1-(indol-3-yl)glycerol 3-phosphate = L-tryptophan + glyceraldehyde 3-phosphate + H2O It has two functional domains, each found in bacteria and plants on a separate subunit: alpha chain (IPR002028) is for the aldol cleavage of indoleglycerol phosphate to indole and glyceraldehyde 3-phosphate and beta chain is for the synthesis of tryptophan from indole and serine. In fungi the two domains are fused together on a single multifunctional protein [PMID: 2734310].

The beta chain of the enzyme, represented here, 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.

GO terms

Biological Process

GO:0006568 tryptophan metabolic process

Molecular Function

GO:0004834 tryptophan synthase activity

Cellular Component

No terms assigned in this category.

Contributing signatures

Signatures from InterPro member databases are used to construct an entry.
PROSITE patterns