His_Phos_1: Histidine phosphatase superfamily (branch 1)
| PAG Title | His_Phos_1: Histidine phosphatase superfamily (branch 1) |
| PAG ID | PEX000970 |
| Type | A |
| Source Link |  Pfam |
| Publication Reference | NA |
| PAG Description | The histidine phosphatase superfamily is so named because catalysis centres on a conserved His residue that is transiently phosphorylated during the catalytic cycle. Other conserved residues contribute to a phosphate pocket and interact with the phospho group of substrate before, during and after its transfer to the His residue. Structure and sequence analyses show that different families contribute different additional residues to the phosphate pocket and, more surprisingly, differ in the position, in sequence and in three dimensions, of a catalytically essential acidic residue. The superfamily may be divided into two main branches. The larger branch 1 contains a wide variety of catalytic functions, the best known being fructose 2,6-bisphosphatase (found in a bifunctional protein with 2-phosphofructokinase) and cofactor-dependent phosphoglycerate mutase. The latter is an unusual example of a mutase activity in the superfamily: the vast majority of members appear to be phosphatases. The bacterial regulatory protein phosphatase SixA is also in branch 1 and has a minimal, and possible ancestral-like structure, lacking the large domain insertions that contribute to binding of small molecules in branch 1 members. |
| Species | Homo sapiens |
| Quality Metric Scores | nCoCo Score: 0 |
| Information Content | Poor |
| Other IDs | PF00300 |
| Base PAG ID | PEX000970 |
| Human Phenotyte Annotation | |
| Curator | PAGER curation team |
| Curator Contact | PAGER-contact@googlegroups.com |
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