Catalyzes the specific phosphorylation of the 3-hydroxyl group of shikimic acid using ATP as a cosubstrate. ATP + shikimate = 3-phosphoshikimate + ADP + H(+) Binds 1 Mg(2+) ion per subunit. Metabolic intermediate biosynthesis; chorismate biosynthesis; chorismate from D-erythrose 4-phosphate and phosphoenolpyruvate: step 5/7. Monomer. Consists of three domains: the CORE domain which forms the binding site for nucleotides, the LID domain which closes over the active site upon ATP or shikimate binding, and the substrate-binding domain which functions to recognize and bind shikimate. The phosphoryl transfer proceeds by an in-line associative mechanism. The random sequential binding of shikimate and nucleotide is associated with domain movements that suggest a synergic mechanism by which binding of the first substrate may enhance the affinity for the second substrate. Was identified as a high-confidence drug target. Belongs to the shikimate kinase family.