| Symbol: | FTCD_N |
| Formiminotransferase domain, N-terminal subdomain | |
| Width: | 270 |
| Pfam: | PF07837 |
| Interpro: | IPR012886 |
| Scop: | 1qd1 |
| Symbol: | FTCD |
| Formiminotransferase domain | |
| Pfam: | PF02971 |
| Interpro: | IPR013802 |
| Scop: | 1qd1 |
Glutamate formimidoyltransferase is a methyltransferase enzyme which uses tetrahydrofolate as part of histidine catabolism. It catalyses two reactions:
It is classified under 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 formiminotransferase domain has an N-terminal subdomain that is made up of a six-stranded mixed beta-pleated sheet and five alpha helices, which are arranged on the external surface of the beta sheet. This, in turn, faces the beta-sheet of the C-terminal subdomain to form a double beta-sheet layer. 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.[2] In humans, deficiency of this enzyme results in a disease phenotype.[3]