Microperfuranone synthase is the only protein required for the biosynthesis of the secondary metabolite microperfuranone from phenylpyruvic acid (PPA) (PubMed:22627757). Several steps for the microperfuranione biosynthesis have been proposed (PubMed:22627757). These steps include the activation of PPA, by the micA adenylation (A) domain to AMP-phenylpyruvic acid followed by loading of the PPA unit to the thiolation and peptide carrier (T) domain and eventually transferring to the thioesterase (TE) domain (PubMed:22627757). After loading another PPA unit onto the T domain, aldol condensation establishes the carbon-carbon bond between the alpha- and beta-carbon of the two PPA units (PubMed:22627757). Sulfur-assisted furan ring formation, TE domain mediated hydrolysis, decarboxylation, and keto-enol tautomerization would generate microperfuranone attached to the T domain (PubMed:22627757). Finally, microperfuranone is released by the TE domain (PubMed:22627757). Secondary metabolite biosynthesis. Belongs to the ATP-dependent AMP-binding enzyme family.