Article snapshot taken from Wikipedia with creative commons attribution-sharealike license.
Give it a read and then ask your questions in the chat.
We can research this topic together.
Protein family
Glutamine amidotransferase class-I
crystal structure of putative glutamine amido transferase (tm1158) from thermotoga maritima at 1.70 a resolution
In molecular biology, glutamine amidotransferases (GATase) are enzymes which catalyse the removal of the ammonia group from a glutamine molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This activity is found in a range of biosynthetic enzymes, including glutamine amidotransferase, anthranilate synthase component II, p-aminobenzoate, and glutamine-dependent carbamoyl-transferase (CPSase). Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. On the basis of sequence similarities two classes of GATase domains have been identified: class-I (also known as trpG-type) and class-II (also known as purF-type). Class-I GATase domains are defined by a conservedcatalytic triad consisting of cysteine, histidine and glutamate. Class-I GATase domains have been found in the following enzymes: the second component of anthranilate synthase and 4-amino-4-deoxychorismate (ADC) synthase; CTP synthase; GMP synthase; glutamine-dependent carbamoyl-phosphate synthase; phosphoribosylformylglycinamidine synthase II; and the histidine amidotransferase hisH.
Nyunoya H, Lusty CJ (August 1984). "Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain". The Journal of Biological Chemistry. 259 (15): 9790–8. PMID6086650.
crystal structure of putative glutamine amido transferase (tm1158) from thermotoga maritima at 1.70 a resolution