In the first step of peptide synthesis this enzyme activates phenylalanine and racemizes it to the D-isomer. ATP + H2O + L-phenylalanine = AMP + D-phenylalanine + diphosphate + H(+) Binds 1 phosphopantetheine covalently. Antibiotic biosynthesis; tyrocidine biosynthesis. Large multienzyme complex of TycA, TycB and TycC. One-module-bearing peptide synthase with a C-terminal epimerization domain. Each module incorporates one amino acid into the peptide product and can be further subdivided into domains responsible for substrate adenylation, thiolation, condensation (not for the initiation module), and epimerization (optional), and N methylation (optional). Tyrocidine is a mixture of four cyclic decapeptides, tyrocidine A (D-Phe-Pro-Phe-D-Phe-Asn-Gln-Tyr-Val-Orn-Leu), B, C, and D, in which Phe, at positions 3, 4, and Tyr residues are gradually replaced by Trp, depending on the relative concentrations of these amino acids in the growth medium. Belongs to the ATP-dependent AMP-binding enzyme family.