InterPro domain: IPR036554

This domain superfamily is found in homoserine kinases ( 2.7.1.39 ), galactokinases ( 2.7.1.6 ) and mevalonate kinases ( 2.7.1.36 ). These kinases make up the GHMP kinase superfamily of ATP-dependent enzymes [ 1 , 2 ]. These enzymes are involved in the biosynthesis of isoprenes and amino acids as well as in carbohydrate metabolism. The C-terminal domain of homoserine kinase has a central alpha-beta plait fold and an insertion of four helices, which, together with the N-terminal fold, create a novel nucleotide binding fold [ 3 ].

This domain superfamily is also found in some diphosphomevalonate decarboxylases, which are structurally related members of the GHMP superfamily [ 4 ], but do not possess kinase activity.

1. Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci. 2, 31-40
2. Biochemical and structural basis for feedback inhibition of mevalonate kinase and isoprenoid metabolism. Biochemistry 47, 3715-24
3. Structure and mechanism of homoserine kinase: prototype for the GHMP kinase superfamily. Structure 8, 1247-57
4. Crystal structures of Trypanosoma brucei and Staphylococcus aureus mevalonate diphosphate decarboxylase inform on the determinants of specificity and reactivity. J. Mol. Biol. 371, 540-53