InterPro domain: IPR044992
General Information
- Identifier IPR044992
- Description Glutamine amidotransferase domain containing protein ChyE-like
- Number of genes 387
- Gene duplication stats Loading...
Abstract
This entry represents a subgroup of class 1 glutamine amidotransferase (GATase1). GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved.
Proteins in this subgroup are mostly from archaea, bacteria, plants and fungi. This entry includes ChyE from Penicillium rubens, YLR126C from budding yeast, GGP1-5 from plants. ChyE converts 2-(2-aminopropanamido)benzoic acid and 2-(2-aminopropanamido)benzamidine into 2-(2-(2-carboxyacetamido)propanamido)benzoic acid and 3-((1-((2-carbamoylphenyl)amino)-1-oxopropan-2-yl)amino)-3-oxopropanoic acid, respectively [ 1 ]. In Arabidopsis, GGP1 hydrolyzes the gamma-glutamyl peptide bond of several glutathione (GSH) conjugates to produce Cys-Gly conjugates related to glucosinolates. The gamma-Glu-Cys-Gly-GSH conjugates are the sulfur-donating molecule in glucosinolate biosynthesis [ 2 , 3 ]. The function of YLR126C is still not clear.
1. Pathway for the Biosynthesis of the Pigment Chrysogine by Penicillium chrysogenum. Appl Environ Microbiol 84, 2456-69
2. Glucosinolate engineering identifies a gamma-glutamyl peptidase. Nat Chem Biol 5
3. Cytosolic γ-glutamyl peptidases process glutathione conjugates in the biosynthesis of glucosinolates and camalexin in Arabidopsis. Plant Cell 23, 575-7