CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.50 | 3-Layer(bba) Sandwich |
|
3.50.20 | Pyruvoyl-Dependent Histidine Decarboxylase; Chain B |
|
3.50.20.20 | Janus/Ocnus |
Domain Context
CATH Clusters
| Superfamily | Janus/Ocnus |
| Functional Family | 14 kDa phosphohistidine phosphatase |
Enzyme Information
| 3.9.1.3 |
Phosphohistidine phosphatase.
based on mapping to UniProt Q9NRX4
A [protein]-N-phospho-L-histidine + H(2)O = a [protein]-L-histidine + phosphate.
-!- This eukaryotic enzyme dephosphorylates phosphorylated histidine residues within proteins and peptides. -!- The enzyme acts on phosphate groups attached to both the pros- and tele-nitrogen atoms, but the pros- position is somewhat preferred (by a factor of two at the most). -!- The substrate specificity depends on the amino acid sequence or structural context of the phosphohistidine in a phosphoprotein. -!- The enzyme is also active on free phosphoramidate and peptide-bound phospholysine.
|
UniProtKB Entries (1)
| Q9NRX4 |
PHP14_HUMAN
Homo sapiens
14 kDa phosphohistidine phosphatase
|
PDB Structure
| PDB | 2AI6 |
| External Links | |
| Method | SOLUTION NMR |
| Organism | Escherichia |
| Primary Citation |
Solution structure and catalytic mechanism of human protein histidine phosphatase 1.
Biochem.J.
|
