Controls both the activation and catalytic activity of PanD in a coenzyme A (CoA)-dependent fashion. Binding of CoA or a derivative to PanZ leads to interaction with PanD, which promotes the processing and activation of pro-PanD, and subsequent substrate-mediated inhibition of the active form of PanD (PubMed:23170229, PubMed:25910242). Inhibition of PanD activity is probably the primary metabolic role of PanZ, allowing negative feedback regulation of pantothenate biosynthesis by CoA (PubMed:25910242). Activation of PanD processing occurs even at low CoA concentrations. In contrast, full inhibition of PanD catalytic activity only occurs at sufficiently high CoA concentrations. Interacts with PanD in the presence of CoA (PubMed:23170229, PubMed:22940551, PubMed:25910242). Forms a heterooctameric complex composed of four PanD subunits and four PanZ subunits (PubMed:22940551, PubMed:25910242). Monomer in solution (PubMed:22940551). Deletion mutants are deficient in the biosynthetic pathway for pantothenate. Belongs to the PanZ/PanM family. Lacks the conserved catalytic glutamate found in many enzymatically active members of the Gcn5-like N-acetyltransferase (GNAT) family.