This model represents a a group of highly homologous enzymes related to dioxygenases which chlorinate amino acid methyl groups. BarB1 and BarB2 are proposed to trichlorinate one of the methyl groups of a leucine residue in the biosynthesis of barbamide in the cyanobacterium Lyngbya majuscula. SyrB2 is proposed to chlorinate the methyl group of threonine in the biosynthesis of syringomycin in Pseudomonas syringae. CmaB is proposed to chlorinate the beta-methyl group of alloisoleucine in the process of ring closure in the biosynthesis of coronamic acid, a component of coronatine also in Pseudomonas syringae.