Involved in the biosynthesis of prenylated phenolics natural products which contribute to the bitter taste of beer and display broad biological activities (Probable). Catalyzes the ligation of CoA on propanoate to produce propanoyl-CoA (PubMed:23300257). Can also use 2-methylpropanoate (isobutyric acid), acetate, butanoate, isovalerate, pentanoate, hexanoate, 2-methylbutanoate, 2-methylpentanoate, 3-methylpentanoate and 4-methylpentanoate as substrates with a lower efficiency (PubMed:23300257). Triggers the formation of very short chain acyl-CoAs from the corresponding fatty acids, including acetic acid, propanoic acid, butyric acid and its isomer (PubMed:23300257). acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate ATP + CoA + propanoate = AMP + diphosphate + propanoyl-CoA ATP + butanoate + CoA = AMP + butanoyl-CoA + diphosphate ATP + CoA + isovalerate = 3-methylbutanoyl-CoA + AMP + diphosphate ATP + CoA + pentanoate = AMP + diphosphate + pentanoyl-CoA ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA 2-methylpropanoate + ATP + CoA = 2-methylpropanoyl-CoA + AMP + diphosphate 2-methylbutanoate + ATP + CoA = 2-methylbutanoyl-CoA + AMP + diphosphate 2-methylpentanoate + ATP + CoA = 2-methylpentanoyl-CoA + AMP + diphosphate 3-methylpentanoate + ATP + CoA = 3-methylpentanoyl-CoA + AMP + diphosphate 4-methylpentanoate + ATP + CoA = 4-methylpentanoyl-CoA + AMP + diphosphate Secondary metabolite biosynthesis. Mostly expressed in glandular trichomes (lupulin glands) after flowering and in old leaves, and, to a lower extent, in stems, young leaves, cones and flowers. Accumulates progressively in glandular trichomes (lupulin glands) after flowering. Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity. Belongs to the ATP-dependent AMP-binding enzyme family.