GatD subunit of archaeal Glu-tRNA amidotransferase
GatD is involved in the alternative synthesis of Gln-tRNA(Gln) in archaea via the transamidation of incorrectly charged Glu-tRNA(Gln). GatD is active as a dimer, and it provides the amino group required for this reaction. GatD is related to bacterial L-asparaginases (amidohydrolases), which catalyze the hydrolysis of asparagine to aspartic acid and ammonia. This CD spans both the L-asparaginase_like domain and an N-terminal supplementary domain.
Structure:1ZQI: Pyrococcus abyssi GatD homodimer binds aspartic acid in one of two active sites (active site residues inferred via related family members), contacts at 4 A
Comment:Both subunits appear to contribute residues to each active site.
Jiyao W et al.(2023). "The conserved domain database in 2023.",