tetrapyrrole methylase family protein similar to Omphalotus olearius omphalotin methyltransferase (OphMA) and Dendrothele bispora dbOphMA
OphMA, is the precursor protein of the fungal cyclic peptide Omphalotin A. Omphalotin A is a potent nematicide, having 9 out of 12 of its residues methylated at the backbone amide. Omphalotin A derives from the C-terminus of OphMA (also known as OphA). OphMA catalyzes the automethylation of its own C-terminus using S-adenosyl methionine (SAM); this C terminus is subsequently released and macrocyclized by the protease OphP to give Omphalotin A.
Comment:includes the SAM binding site and peptide substrate binding site
Structure:6MJG; Dendrothele bispora OphMA binds its methylated C-terminus and S-adenosyl-l-homocysteine in the active site, contacts at 4A
Comment:biosynthesis of the cyclic peptide Omphalotin A, involves a methyltransferase OphMA that catalyzes the automethylation of its own C-terminus, which is then released and cyclized by the protease OphP
Jiyao W et al.(2023). "The conserved domain database in 2023.",