| Type: | Domain | Name: | Class I glutamine amidotransferase-like |
| Description: | This entry represents the class I glutamine amidotransferase-like domain.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). In class I glutamine amidotransferases, 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.This entry also include the DJ-1/PfpI protein that contains a catalytic triad or dyad different from the class I GAT triad. | Short Name: | Class_I_gatase-like |
