Coenzyme A is synthesised from pantothenate via five enzyme-mediated steps. The first step is catalysed by pantothenate kinase (PanK). All PanKs characterised to date form homodimers. Many organisms express multiple PanKs. In some cases, these PanKs are not functionally redundant, and some appear to be non-functional. Here, we investigate the PanKs in two pathogenic apicomplexan parasites,Plasmodium falciparumandToxoplasma gondii. Each of these organisms express two PanK homologues (PanK1 and PanK2). We demonstrate thatPfPanK1 andPfPanK2 associate, forming a single, functional PanK complex that includes the multi-functional protein,Pf14-3-3I. Similarly, we demonstrate thatTgPanK1 andTgPanK2 form a single complex that possesses PanK activity. BothTgPanK1 andTgPanK2 are essential forT.gondiiproliferation, specifically due to their PanK activity. Our study constitutes the first examples of heteromeric PanK complexes in nature and provides an explanation for the presence of multiple PanKs within certain organisms.