Contributes to jasmonic acid biosynthesis by initiating the beta-oxidative chain shortening of its precursors (PubMed:18267944). CoA ligase that can use preferentially p-coumarate, ferulate and caffeate as substrates and can use, with a lower efficiency, t-cinnamate and 4-hydroxybenzoate as substrates (PubMed:24838974). Involved in the biosynthesis of ubiquinone from phenylalanine by activating the propyl side chain of 4-coumarate, and possibly trans-cinnamate and 4-hydroxybenzoate, for subsequent beta-oxidative shortening and the formation of the benzenoid moiety of ubiquinone (PubMed:24838974). ATP + CoA + tetradecanoate = AMP + diphosphate + tetradecanoyl-CoA ATP + CoA + hexanoate = AMP + diphosphate + hexanoyl-CoA ATP + CoA + heptanoate = AMP + diphosphate + heptanoyl-CoA (E)-caffeate + ATP + CoA = (E)-caffeoyl-CoA + AMP + diphosphate (E)-ferulate + ATP + CoA = (E)-feruloyl-CoA + AMP + diphosphate (E)-4-coumarate + ATP + CoA = (E)-4-coumaroyl-CoA + AMP + diphosphate 4-hydroxybenzoate + ATP + CoA = 4-hydroxybenzoyl-CoA + AMP + diphosphate kcat is 0.43 sec(-1) with tetradecanoic acid as substrate (PubMed:18267944). kcat is 0.7 sec(-1) with trans-cinnamate as substrate (PubMed:24838974). kcat is 2.1 sec(-1) with p-coumarate as substrate (PubMed:24838974). kcat is 3.6 sec(-1) with ferulate as substrate (PubMed:24838974). kcat is 2.4 sec(-1) with caffeate as substrate (PubMed:24838974). kcat is 0.01 sec(-1) with 4-hydroxybenzoate as substrate (PubMed:24838974). Expressed at very low level in leaves. Both substrate-binding domains (SBD1 and SBD2) are involved in the substrate recognition, and are sufficient to confer the substrate specificity. Cannot use 4-coumarate for ubiquinone biosynthesis. Belongs to the ATP-dependent AMP-binding enzyme family.