Class I glutamine amidotransferase-like
IPR029062
Definition
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 PMID:4355768. 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 [[cite:PMID:3298209], [cite:PMID:6086650]]: 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 [[cite:PMID:8548458], [cite:PMID:9575335]]. 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. This superfamily represents the class I glutamine amidotransferase-like domain.
12 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
Loading the interactive Seroatlas explorer...