Involved in the biosynthesis of mycolic acids (PubMed:19436070, PubMed:19477415). Catalyzes the activation of long-chain fatty acids as acyl-adenylates (acyl-AMP), which are then transferred to the phosphopantetheine arm of the polyketide synthase Pks13 for further chain extension (PubMed:15042094, PubMed:19436070, PubMed:19477415, PubMed:27547819, PubMed:27590338). Can use dodecanoate (C12), tetradecanoate (C14) and hexadecanoate (C16) (PubMed:19182784, PubMed:19436070, PubMed:19477415, PubMed:23364516, PubMed:26900152, PubMed:27590338). In vitro, displays a preference for long-chain over medium and short-chain fatty acid substrates (PubMed:19477415). a long-chain fatty acid + ATP + holo-[ACP] = a long-chain fatty acyl-[ACP] + AMP + diphosphate ATP + dodecanoate + holo-[ACP] = AMP + diphosphate + dodecanoyl-[ACP] ATP + holo-[ACP] + tetradecanoate = AMP + diphosphate + tetradecanoyl-[ACP] ATP + hexadecanoate + holo-[ACP] = AMP + diphosphate + hexadecanoyl-[ACP] ATP + dodecanoate + H(+) = diphosphate + dodecanoyl-AMP ATP + H(+) + tetradecanoate = diphosphate + tetradecanoyl-AMP ATP + H(+) + hexadecanoate = diphosphate + hexadecanoyl-AMP Fatty acyl-AMP ligase activity and transferase activity onto Pks13 are both inhibited by phosphorylation (PubMed:27590338). The acyl-AMP ligase activity is inhibited by the alkylphosphate ester of AMP, adenosine 50-dodecylphosphate (AMPC12) (PubMed:19477415, PubMed:26900152). Also inhibited by eicosyl-AMP (AMPC20) (PubMed:26900152). Loading of the acyl-AMP onto Pks13 is inhibited by 5'-O-[N-(11-phenoxyundecanoyl)sulfamoyl]adenosine (PhU-AMS) (PubMed:27547819). kcat is 0.150 min(-1) with dodecanoate as substrate (PubMed:19477415). kcat is 2.04 min(-1) with dodecanoate as substrate (PubMed:26900152). kcat is 0.123 min(-1) with tetradecanoate as substrate (PubMed:19477415). kcat is 0.98 min(-1) with tetradecanoate as substrate (PubMed:26900152). kcat is 0.015 min(-1) with hexadecanoate as substrate (PubMed:19477415). Lipid metabolism; mycolic acid biosynthesis. Monomer in solution. Phosphorylated on Thr-552 by PknA, PknB, PknD and PknF. Dephosphorylated by PstP. Phosphorylation regulates activity. Was identified as a drug target (PubMed:23364516, PubMed:23798446, PubMed:30316633). Inhibited by a series of 4,6-diaryl-5,7-dimethyl coumarins that directly inhibit the acyl-acyl carrier protein synthetase activity of FadD32 and kill M.tuberculosis. They effectively block bacterial replication both in vitro and in animal models of tuberculosis (PubMed:23798446). Quinoline-2-carboxamides have also potent anti-tubercular activity (PubMed:30316633). Belongs to the ATP-dependent AMP-binding enzyme family.