InterPro domain: IPR027266

This entry represents an alpha/beta domain found in GTP-binding protein TrmE (N-terminal domain) [ 1 ] and domain 1 of glycine cleavage T-protein (also known as aminomethyltransferase) [ 2 ].

TrmE is a guanine nucleotide-binding protein conserved between bacteria and eukaryotes. It is involved in the modification of uridine bases at the first anticodon (wobble) position of tRNAs. The N-terminal portion of the protein is necessary for mediating dimer formation within the protein [ 3 ].

Glycine cleavage T-protein is part of the glycine cleavage multienzyme complex (GCV) found in bacteria and the mitochondria of eukaryotes [ 3 ]. GCV catalyses the oxidative decarboxylation of glycine. The T-protein is an aminomethyl transferase 2.1.2.10 . The N-terminal region (residues 14-35) of domain 1 plays a crucial role in H-protein interaction [ 4 ].

1. The structure of the TrmE GTP-binding protein and its implications for tRNA modification. EMBO J. 24, 23-33
2. Crystal structure of T-protein of the glycine cleavage system. Cofactor binding, insights into H-protein recognition, and molecular basis for understanding nonketotic hyperglycinemia. J. Biol. Chem. 279, 50514-23
3. The glycine decarboxylase system: a fascinating complex. Trends Plant Sci. 6, 167-76