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ENZYME

ENZYME entry: EC 3.9.1.3

PURL: https://purl.expasy.org/enzyme/EC/3.9.1.3
Accepted Name
phosphohistidine phosphatase
Alternative Name(s)
PHP
protein histidine phosphatase
Reaction catalysed
  • N(tele)-phospho-L-histidyl-[protein] + H2O = L-histidyl-[protein] + phosphate
  • N(pros)-phospho-L-histidyl-[protein] + H2O = L-histidyl-[protein] + phosphate
Comment(s)
  • 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.
Cross-references
BRENDA3.9.1.3
EC2PDB3.9.1.3
ExplorEnz3.9.1.3
KEGG Ligand Database for Enzyme Nomenclature3.9.1.3
IUBMB Enzyme Nomenclature3.9.1.3
MEDLINEFind literature relating to 3.9.1.3
MetaCyc3.9.1.3
Rhea expert-curated reactions3.9.1.3
UniProtKB/Swiss-Prot
Q32PA4, PHP14_BOVINQ9NRX4, PHP14_HUMANQ9DAK9, PHP14_MOUSE
P59083, PHP14_PIGQ5R8L6, PHP14_PONABP83468, PHP14_RABIT

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.9.1.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.9.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-