| Type: | Family | Name: | Histidine phosphatase superfamily |
| Description: | The histidine phosphatase superfamily is a large and functionally diverse group of proteins. They share a conserved catalytic core centred on a histidine which becomes phosphorylated during the course of the reaction. The superfamily is mainly composed of phosphatases, but the best-studied member is dPGM (cofactor-dependent phosphoglycerate mutase). The superfamily contains two branches sharing very limited sequence similarity: histidine phosphatase clade-1 and clade-2 [].The larger clade-1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctionalprotein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutaseactivity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is alsoin clade-1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of smallmolecules in clade-1 members.The smaller clade-2 contains predominantly eukaryotic proteins. The catalytic functions of these proteins nclude phytase, glucose-1-phosphataseand multiple inositol polyphosphate phosphatase. The in vivo roles of the mammalian acid phosphatases in clade-2 are not fully understood,although activity against lysophosphatidic acid and tyrosine-phosphorylated proteins has been demonstrated. | Short Name: | His_PPase_superfam |
