The shikimate pathway links metabolism of carbohydrates to biosynthesis of aromatic compounds. In a sequence of seven steps, phosphoenolpyruvate and erythrose 4-phosphate are converted to chorismate, a precursor of the aromatic amino acids and many secondary aromatic metabolites. The shikimate pathway is essential for most bacteria and plants but absent in humans, making it an attractive target for the development of novel antibiotics. 3-deoxy-7-phosphoheptulonate DAHP synthase catalyzes the conversion of phosphoenolpyruvate and D-erythrose 4-phosphate to DAHP, the first step in the shikimate pathway. Chorismate mutase catalyzes the conversion of chorismate, the shikimate pathway’s endproduct, to prephenate. Prephenate is a precursor for the aromatic amino acids phenylalanine and tyrosine. While structures of individual DAHP and chorismate mutase domains have been previously solved, this structure is the first to characterize this natural bifunctional protein which is found in a subset of bacteria. This structure reveals that the DAHP synthase domains are assembled into their typical physiological tetrameric state. The N-terminal chorismate mutase domains emerge from either side of the tetramer and after a lengthy linker region form a pair of dimers which sandwich the tetrameric core. The linker region between the DAHP and chorismate mutase domains acts differently within the two molecules within the asymmetric unit - a result which may be due to crystal packing.