CATH Classification

Domain Context

CATH Clusters

Superfamily HPr-like
Functional Family Phosphotransferase system, phosphocarrier protein HPr

Enzyme Information

2.7.11.-
Protein-serine/threonine kinases.
based on mapping to UniProt P0AA04
2.7.3.9
Phosphoenolpyruvate--protein phosphotransferase.
based on mapping to UniProt P0AA04
Phosphoenolpyruvate + protein L-histidine = pyruvate + protein N(pi)- phospho-L-histidine.
-!- Acts only on histidine residues in specific phosphocarrier proteins of low molecular mass (9.5 kDa) involved in bacterial sugar transport. -!- A similar reaction where the protein is the enzyme EC 2.7.9.2 is part of the mechanism of that enzyme.
2.7.1.191
Protein-N(pi)-phosphohistidine--D-mannose phosphotransferase.
based on mapping to UniProt P0AA04
[Protein]-N(pi)-phospho-L-histidine + D-mannose(Side 1) = [protein]-L- histidine + D-mannose 6-phosphate(Side 2).
-!- This enzyme is a component (known as enzyme II) of a phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). -!- The system, which is found only in prokaryotes, simultaneously transports its substrate from the periplasm or extracellular space into the cytoplasm and phosphorylates it. -!- The phosphate donor, which is shared among the different systems, is a phospho-carrier protein of low molecular mass that has been phosphorylated by EC 2.7.3.9. -!- Enzyme II, on the other hand, is specific for a particular substrate, although in some cases alternative substrates can be transported with lower efficiency. -!- The reaction involves a successive transfer of the phosphate group to several amino acids within the enzyme before the final transfer to the substrate. -!- Formerly EC 2.7.1.69.
2.7.1.69
Transferred entry: 2.7.1.191, 2.7.1.192, 2.7.1.193, 2.7.1.194, 2.7.1.195, 2.7.1.196, 2.7.1.197, 2.7.1.198, 2.7.1.199, 2.7.1.200, 2.7.1.201, 2.7.1.202, 2.7.1.203, 2.7.1.204, 2.7.1.205, 2.7.1.206, 2.7.1.207 and 2.7.1.208.
based on mapping to UniProt P0AA04

UniProtKB Entries (1)

P0AA04
PTHP_ECOLI
Escherichia coli K-12
Phosphocarrier protein HPr

PDB Structure

PDB 1CM2
External Links
Method X-RAY DIFFRACTION
Organism Escherichia
Primary Citation
The aspartyl replacement of the active site histidine in histidine-containing protein, HPr, of the Escherichia coli Phosphoenolpyruvate:Sugar phosphotransferase system can accept and donate a phosphoryl group. Spontaneous dephosphorylation of acyl-phosphate autocatalyzes an internal cyclization
Napper, S., Delbaere, L.T., Waygood, E.B.
J.Biol.Chem.