Cell division in bacteria is driven by a cytoskeletal ring structure, the Z ring, composed of polymers of the tubulin-like protein FtsZ. Z ring formation must be tightly regulated to ensure faithful cell division, and several mechanisms have been described that influence the positioning and timing of Z ring assembly. Another important but as yet poorly understood aspect of cell division regulation is the need to coordinate division with cell growth and nutrient availability. In this study we demonstrate for the first time that cell division is intimately linked to central carbon metabolism in the model Gram positive bacterium Bacillus subtilis. We show that a deletion of the gene encoding pyruvate kinase (pyk), which produces pyruvate in the final reaction of glycolysis, rescues the assembly defect of a temperature sensitive ftsZ mutant and has significant effects on Z ring formation in wild-type B. subtilis cells. Addition of exogenous pyruvate restores normal division in the absence of the pyruvate kinase enzyme, implicating pyruvate as a key metabolite in the coordination of bacterial growth and division. Our results support a model in which pyruvate levels are coupled to Z ring assembly via an enzyme that actually metabolizes pyruvate, the E1 alpha subunit of pyruvate dehydrogenase. We show that this protein localizes over the nucleoid in a pyruvate-dependent manner, and may stimulate more efficient Z ring formation at the cell centre under nutrient-rich conditions when cells must divide more frequently. Ultimately this helps to ensure the survival of newborn cells.