The genes encoding proteins in this entry are largely adjacent to genes involved in the biosynthesis of threonine (aspartate kinase, homoserine dehydrogenase and threonine synthase) in genomes which are lacking any other known homoserine kinase, and in which the presence of a homoserine kinase would indicate a complete pathway for the biosynthesis of threonine. These proteins are homologous to the archaeal form of 2,3-bisphosphoglycerate-independent phosphoglycerate mutase and form part of a superfamily of metalloenzymes including phosphopentomutases, alkaline phosphatases and sulphatases. The proposal that these proteins encode a kinase is based on analogy to phosphomutases which are intramolecular phosphotransferases. A mutase active site could evolve to bring together homoserine and a phosphate donor such as phosphoenolpyruvate, resulting in kinase activity.
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