InterPro domain: IPR000623

Shikimate kinase ( 2.7.1.71 ) catalyses the fifth step in the biosynthesis of aromatic amino acids from chorismate (the so-called shikimate pathway) [ 1 ]. The enzyme catalyses the following reaction:

ATP + shikimate = ADP + shikimate-3-phosphate

The protein is found in bacteria (gene aroK or aroL), plants and fungi (whereit is part of a multifunctional enzyme that catalyses five consecutive steps in this pathway). In 1994, the 3D structure of shikimate kinase was predicted to be very close to that of adenylate kinase, suggesting a functional similarity as well as an evolutionary relationship [ 2 ]. This prediction has since been confirmed experimentally. The protein is reported to possess an alpha/beta fold, consisting of a central sheet of five parallel beta-strands flanked by alpha-helices. Such a topology is very similar to that of adenylate kinase [ 3 ].

The N terminus of threonine synthase-like 1 from metazoan shares protein sequence similarity with shikimate kinase and is included in this entry. However, their functions may be different.

1. The gene (aroK) encoding shikimate kinase I from Escherichia coli. DNA Seq. 5, 195-7
2. Protein structural similarities predicted by a sequence-structure compatibility method. Protein Sci. 3, 2055-63
3. The three-dimensional structure of shikimate kinase. J. Mol. Biol. 278, 983-97