Glutamate formimidoyltransferase is a methyltransferase enzyme which uses tetrahydrofolate as part of histidine catabolism.

It catalyses two reactions: It is classified under EC 2.1.2.5 and in mammals is found as part of a bifunctional enzyme that also has formimidoyltetrahydrofolate cyclodeaminase activity.

[1] The formiminotransferase (FT) domain of formiminotransferase-cyclodeaminase (FTCD) forms a homodimer, with each protomer comprising two subdomains.

The two subdomains are separated by a short linker sequence, which is not thought to be any more flexible than the remainder of the molecule.

The substrate is predicted to form a number of contacts with residues found in both the N-terminal and C-terminal subdomains.