Involved in chloramphenicol biosynthesis (PubMed:11577160). Activates 4-amino-L-phenylalanine by adenylation and loads it onto its peptidyl carrier domain, via a thioester linkage to the phosphopanthetheine moiety (PubMed:17520135). Can also adenylate tyrosine and phenylalanine at low rates, but not L-p-nitrophenylalanine or threo-phenylserine (PubMed:17520135). 4-amino-L-phenylalanine + ATP + holo-[peptidyl-carrier protein] = 4-amino-L-phenylalanyl-[peptidyl-carrier protein] + AMP + diphosphate Binds 1 phosphopantetheine covalently. kcat is 7.3 min(-1) for adenylation of 4-amino-L-phenylalanine. kcat is 1.97 min(-1) for adenylation of L-tyrosine. kcat is 0.90 min(-1) for adenylation of L-phenylalanine. Antibiotic biosynthesis. Contains an N-terminal adenylation domain, an internal peptidyl carrier domain and a C-terminal domain that is homologous to nicotinamide-dependent dehydrogenases. Disruption mutant does not produce chloramphenicol. Mutant does not accumulate 4-amino-L-phenylalanine. Belongs to the ATP-dependent AMP-binding enzyme family.