InterPro : IPR017926

Name  Glutamine amidotransferase Short Name  GATASE
Type  Domain Description  Glutamine amidotransferase (GATase) enzymes catalyse the removal of the ammonia group from glutamine and then transfer this group to a substrate to form a new carbon-nitrogen group []. The GATase domain exists either as a separate polypeptidic subunit or as part of a larger polypeptide fused in different ways to a synthase domain. Two classes of GATase domains have been identified [, ]: class-I (also known as trpG-type or triad) and class-II (also known as purF-type or Ntn). Class-I (or type 1) GATase domains have been found in the following enzymes:The second component of anthranilate synthase (AS) []. AS catalyzes the biosynthesis of anthranilate from chorismate and glutamine. AS is generally a dimeric enzyme: the first component can synthesize anthranilate using ammonia rather than glutamine, whereas component II provides the GATase activity []. In some bacteria and in fungi the GATase component of AS is part of a multifunctional protein that also catalyzes other steps of the biosynthesis of tryptophan.The second component of 4-amino-4-deoxychorismate (ADC) synthase, a dimeric prokaryotic enzyme that functions in the pathway that catalyzes the biosynthesis of para-aminobenzoate (PABA) from chorismate and glutamine. The second component (gene pabA) provides the GATase activity [].CTP synthase. CTP synthase catalyzes the final reaction in the biosynthesis of pyrimidine, the ATP-dependent formation of CTP from UTP and glutamine. CTP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the C-terminal section [].GMP synthase (glutamine-hydrolyzing). GMP synthase catalyzes the ATP-dependent formation of GMP from xanthosine 5'-phosphate and glutamine. GMP synthase is a single chain enzyme that contains two distinct domains; the GATase domain is in the N-terminal section [, ].Glutamine-dependent carbamoyl-phosphate synthase (GD-CPSase); an enzyme involved in both arginine and pyrimidine biosynthesis and which catalyzes the ATP-dependent formation of carbamoyl phosphate from glutamine and carbon dioxide. In bacteria GD-CPSase is composed of two subunits: the large chain (gene carB) provides the CPSase activity, while the small chain (gene carA) provides the GATase activity. In yeast the enzyme involved in arginine biosynthesis is also composed of two subunits: CPA1 (GATase), and CPA2 (CPSase). In most eukaryotes, the first three steps of pyrimidine biosynthesis are catalyzed by a large multifunctional enzyme (called URA2 in yeast, rudimentary in Drosophila, and CAD in mammals). The GATase domain is located at the N-terminal extremity of this polyprotein [].Phosphoribosylformylglycinamidine synthase, an enzyme that catalyzes the fourth step in the de novo biosynthesis of purines. In some species of bacteria and rchaea, FGAM synthase II is composed of two subunits: a small chain (gene purQ) which provides the GATase activity and a large chain (gene purL) which provides the aminator activity. In eukaryotes and Gram-negative bacteria a single polypeptide (large type of purL) contains a FGAM synthethase domain and the GATase as the C-terminal domain [].Imidazole glycerol phosphate synthase subunit hisH, an enzyme that catalyzes the fifth step in the biosynthesis of histidine.A triad of conserved Cys-His-Glu forms the active site, wherein the catalytic cysteine is essential for the amidotransferase activity [, ]. Different structures show that the active site Cys of type 1 GATase is located at the tip of a nucleophile elbow.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



1 Child Features

Id Name Short Name Type
IPR006221 Anthranilate synthase/para-aminobenzoate synthase like domain TrpG/PapA_dom Domain

0 Contains

4 Found In

Id Name Short Name Type
IPR004468 CTP synthase CTP_synthase Family
IPR010073 Phosphoribosylformylglycinamidine synthase PRibForGlyAmidine_synth Family
IPR010141 Phosphoribosylformylglycinamidine synthase, FGAM FGAM_synthase Family
IPR010075 Phosphoribosylformylglycinamidine synthase I PRibForGlyAmidine_synth_I Family

1 Parent Features

Id Name Short Name Type
IPR029062 Class I glutamine amidotransferase-like Class_I_gatase-like Domain

10 Publications

First Author Title Year Journal Volume Pages
Buchanan JM The amidotransferases. 1973 Adv Enzymol Relat Areas Mol Biol 39 91-183
Weng ML Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain. 1987 J Bacteriol 169 3023-8
Nyunoya H Sequence of the small subunit of yeast carbamyl phosphate synthetase and identification of its catalytic domain. 1984 J Biol Chem 259 9790-8
Tesmer JJ The crystal structure of GMP synthetase reveals a novel catalytic triad and is a structural paradigm for two enzyme families. 1996 Nat Struct Biol 3 74-86
Crawford IP Evolution of a biosynthetic pathway: the tryptophan paradigm. 1989 Annu Rev Microbiol 43 567-600
Davidson JN The evolutionary history of the first three enzymes in pyrimidine biosynthesis. 1993 Bioessays 15 157-64
Knöchel T The crystal structure of anthranilate synthase from Sulfolobus solfataricus: functional implications. 1999 Proc Natl Acad Sci U S A 96 9479-84
Anand R Domain organization of Salmonella typhimurium formylglycinamide ribonucleotide amidotransferase revealed by X-ray crystallography. 2004 Biochemistry 43 10328-42
Zalkin H Identification of a trpG-related glutamine amide transfer domain in Escherichia coli GMP synthetase. 1985 J Biol Chem 260 3350-4
Massière F The mechanism of glutamine-dependent amidotransferases. 1998 Cell Mol Life Sci 54 205-22

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)