<jats:title>Abstract</jats:title><jats:p>Fatty acyl‐AMP ligases (FAALs) activate fatty acids as acyladenylates, and subsequently catalyze their transfer onto the acyl carrier proteins (ACPs) of polyketide synthases (PKSs) or nonribosomal peptide synthetases to produce lipidic metabolites. <jats:italic>Myxococcus xanthus</jats:italic> contains a polyketide biosynthesis gene cluster in which putative FAAL (FtpD) and ACP (FtpC) genes are located close to a type III PKS (FtpA) gene. Here we describe the characterization of these three proteins in vitro. FtpD adenylated stearic acid and produced stearoyl‐FtpC. The stearoyl moiety was then transferred to FtpA. When extender substrates (malonyl‐CoA and methylmalonyl‐CoA) were added to the reaction, the alkylresorcinol 5‐heptadecyl‐4‐methyl‐benzene‐1,3‐diol was synthesized. Further in vitro analysis indicated that FtpA produces an alkylresorcylic acid as the direct product, and that this decarboxylates to alkylresorcinol nonenzymatically. This is the first report of a FAAL supplying a long‐chain fatty acyl‐ACP starter substrate to a type III PKS.