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Shikimate kinase is an enzyme which participates in the fifth step of the shikimate pathway. The functional role shikimate kinase plays in this pathway is to catalyze the ATP-dependent phosphorylation of shikimate into shikimate 3-phosphate (3-phosphoshikimate). This aids in the synthesis of chorismate, which is the precursor to aromatic amino acids and secondary metabolites. Shikimate kinase is a protein kinase, an enzyme which phosphorylates a protein leading to a functional change in the phosphorylated protein, of the transferase class. The protein fold consists of 9 helices, 5 strands, and is typically 176 amino acids in length. The subunit is that of a monomer and it is found in the cytoplasm. This enzyme consists of the CORE, LED, and substrate-binding domains. ATP is the cosubstrate while magnesium ion is the cofactor. Though the shikimate pathway is present in microorganisms and plants, shikimate kinase is found only in the bacteria taxon. This enzyme is found predominantly in the organism ''Mycobacterium tuberculosis'', but also in ''Helicobacter pylori'', ''Bacteroides thetaiotaomicron'', ''Campylobacter jejuni'', ''Aquifex aeolicus'', ''Coxiella burnetii'', ''Arabidopsis thaliana''. This enzyme is a protein target for rational drug design against tuberculosis, which holds great potential due to shikimate kinase being absent in mammals.