Toxoplasma gondii, adapted to obligate intracellular parasitism, shows a remarkable capacity for nutrient sensing and metabolic rewiring during asexual reproduction in mammalian host cells. Cyclic nucleotides- and AMPK-mediated signaling are suggested to sense the parasite milieu, thereby controlling the extracellular-infective and intracellular-replicative transition. We found a lanthionine synthetase C family protein (LanCL) in T. gondii, which is potentially involved in ligand sensing and redox balance. TgLanCL is structurally similar to HsLanCL2, indicating a functional convergence in substrate/ligand binding. 3"-genomic tagging of TgLancL revealed its localization in the parasite cytosol. We are now investigating the physiological relevance and interaction partners of TgLanCL in tachyzoites.