| Primary Identifier | IPR017959 | Type | Family |
| Short Name | Asn/Gln-tRNA_amidoTrfase_suB/E |
| description | Glutamyl-tRNA(Gln) amidotransferase (Gat; ) provides a means of producing correctly charged Gln-tRNA(Gln) through the transamidation of mis-acylated Glu-tRNA(Gln) in organisms which lack glutaminyl-tRNA synthetase [, ]. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The enzyme is composed of three subunits: A (an amidase), B and C. It also exists in eukaryotes as a protein targeted to the mitochondria.The heterotrimer GatABC is involved in converting Glu to Gln and/or Asp to Asn, when the amino acid is attached to the appropriate tRNA. In Lactobacillus, GatABC is responsible for producing tRNA(Gln). In Archaea, GatABC is responsible for producing tRNA(Asn), while GatDE is responsible for producing tRNA(Gln). In lineages that include Thermus, Chlamydia, or Acidithiobacillus, the GatABC complex catalyses both tRNA(Gln) and tRNA(Asn).Glutamyl-tRNA(Gln) amidotransferase, subunit E (GatE) is found only in the Archaea. It is part of a heterodimer, with GatD (), that acts as an amidotransferase on misacylated Glu-tRNA(Gln) to produce Gln-tRNA(Gln) []. The reaction takes place in the presence of glutamine and ATP through an activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is specific for glutamate and does not act on aspartate. This function is carried out in bacteria by the GatABC system, which acts both on Asp-tRNA(Asn) and Glu-tRNA(Gln). GatABC orthologues also exist in some archaea, where it coexist with GatDE (GatE being paralogous to GatB); while other archaea only posses GatED and use an asparaginyl-tRNA synthetase to produce Asn-tRNA by direct acylation of the tRNA []. The crystal structure of GatED showed tRNA(Gln) recognition by indirect readout based on shape complementarity []. This entry represents aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B and glutamyl-tRNA(Gln) amidotransferase subunit E. |
