Nonribosomal peptide synthase-like protein; part of the gene cluster that mediates the biosynthesis of cichorine, a phytotoxin active against knapweed, corn, and soybeans (PubMed:24244835). The first step in the pathway is performed by the non-reducing polyketide synthase pkbA that condenses one acetyl-CoA starter unit with 3 malonyl-CoA units (PubMed:22510154). PkbA also catalyzes one methylation step to produce 3-methylorsellinate (PubMed:22510154). The nonribosomal peptide synthase-like protein cicB, the cytochrome P450 monooxygenase cicH and the O-methyltransferase cicE are involved in the conversion of 3-methylorsellinate into nidulol (PubMed:24244835). CicB converts 3-methylorsellinate to a yet unidentified intermediate, cicH may play a ring-closing role for cichorine and cicE is plausibly responsible for the methylation of one of the phenol groups (Probable). The oxidoreductase cicC acts downstream with still unidentified enzymes to further convert nidulol into cichorine (PubMed:24244835). Phytotoxin biosynthesis. Contains three distinct domains: an adenylation (A) domain that activates the substrate amino acid which is subsequently covalently linked as a thioester (aminoacyl-S-PCP) to the 4'-phosphopantetheine prosthetic group of the second domain, the peptidyl carrier protein (PCP) domain, as well as a reductase (R) release domain. Abolishes the production of cichorine and leads to the accumulation of 3-methylorsellinic acid. Cichorine and its derivatives are promising in the course of developing novel herbicides. Belongs to the adenylate-forming reductase family.