Ferrochelatase, N-terminal domain: Ferrochelatase (protoheme ferrolyase or HemH) is the terminal enzyme of the heme biosynthetic pathway. It catalyzes the insertion of ferrous iron into the protoporphyrin IX ring yielding protoheme. This enzyme is ubiquitous in nature and widely distributed in bacteria and eukaryotes. Recently, some archaeal members have been identified. The oligomeric state of these enzymes varies depending on the presence of a dimerization motif at the C-terminus.
Structure:1C9E_A; Bacillus subtilis ferrochelatase with bound inhibitor, N-MeMP; contacts at 3.5A
Comment:Structure has Cu2+ inserted into the porphyrin moiety.
Comment:The active site is located in a cleft between the N- and C-terminal domains. The active site is partially but not completely symmetrical, containing some residues from equivalent positions in both domains. An insert at the N-terminus of ferrochelatase makes additional contributions to the active site.
Jiyao W et al.(2023). "The conserved domain database in 2023.",