Formyl transferase, C-terminal-like <p>Methionyl-tRNA formyltransferase (FMT) (<db_xref db="EC" dbkey="2.1.2.9"/>) transfers a formyl group onto the amino terminus of the acyl moiety of the methionyl aminoacyl-tRNA. The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by promoting its recognition by IF2 and by impairing its binding to EFTU-GTP. This family also includes formyltetrahydrofolate dehydrogenases, which produce formate from formyl-tetrahydrofolate. These enzymes contain an N-terminal domain in common with other formyl transferase enzymes (<db_xref db="INTERPRO" dbkey="IPR002376"/>). The C-terminal domain has an open beta-barrel fold [<cite idref="PUB00014118"/>].</p><p>The C-terminal domain of FMT structurally resembles methylpurine-DNA glycosylases (MPG). Human 3-methyladenine DNA glycosylase (AAG) catalyses the first step of base excision repair by cleaving damaged bases from DNA, excising a chemically diverse selection of substrate bases damaged by alkylation or deamination [<cite idref="PUB00014119"/>].</p>