IntEnz

EC 2.7.1.191 - Protein-N^π-phosphohistidine—D-mannose phosphotransferase

IntEnz Enzyme Nomenclature
EC 2.7.1.191

Names

Reaction

• 49232 [IUBMB]
  D-mannose

  D-mannose

  Name origin: UniProt - CHECKED (C)

  CHEBI:4208

  Formula: C6H12O6
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  OUT

  +

  N^π-phospho-L-histidyl-[protein]

  N(pros)-phospho-L-histidyl-[protein]

  GENERIC:9746

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  Nπ-phospho-L-histidine residue N(pros)-phospho-L-histidine residue Name origin: UniProt - CHECKED (C) CHEBI:64837 Formula: C6H6N3O4P Charge: -2 Position: undefined ChEBI compound status: CHECKED (C)

  =

  D-mannose 6-phosphate

  D-mannose 6-phosphate

  Name origin: UniProt - CHECKED (C)

  CHEBI:58735

  Formula: C6H11O9P
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  IN

  +

  L-histidyl-[protein]

  L-histidyl-[protein]

  GENERIC:9745

  Is ROOT: no
  ROOT compound: GENERIC:9624

  Number of residues: 1

  L-histidine residue L-histidine residue Name origin: UniProt - CHECKED (C) CHEBI:29979 Formula: C6H7N3O Charge: 0 Position: undefined ChEBI compound status: CHECKED (C)

Comments:

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 (phosphoenolpyruvate—protein phosphotransferase). 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.

Links to other databases

References

1. Erni, B., Zanolari, B.
   The mannose-permease of the bacterial phosphotransferase system. Gene cloning and purification of the enzyme IIMan/IIIMan complex of Escherichia coli.
   J. Biol. Chem. 260 : 15495-15503 (1985). [PMID: 2999119]
2. Williams, N., Fox, D. K., Shea, C., Roseman, S.
   Pel, the protein that permits lambda DNA penetration of Escherichia coli, is encoded by a gene in ptsM and is required for mannose utilization by the phosphotransferase system.
   Proc. Natl. Acad. Sci. U.S.A. 83 : 8934-8938 (1986). [PMID: 2947241]
3. Erni, B., Zanolari, B., Kocher, H. P.
   The mannose permease of Escherichia coli consists of three different proteins. Amino acid sequence and function in sugar transport, sugar phosphorylation, and penetration of phage lambda DNA.
   J. Biol. Chem. 262 : 5238-5247 (1987). [PMID: 2951378]
4. Stolz, B., Huber, M., Markovi?-Housley, Z., Erni, B.
   The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit.
   J. Biol. Chem. 268 : 27094-27099 (1993). [PMID: 8262947]
5. Rhiel, E., Flukiger, K., Wehrli, C., Erni, B.
   The mannose transporter of Escherichia coli K12: oligomeric structure, and function of two conserved cysteines.
   Biol. Chem. Hoppe-Seyler 375 : 551-559 (1994). [PMID: 7811395]
6. Huber, F., Erni, B.
   Membrane topology of the mannose transporter of Escherichia coli K12.
   Eur. J. Biochem. 239 : 810-817 (1996). [PMID: 8774730]

[EC 2.7.1.191 created 1972 as EC 2.7.1.69, part transferred 2016 to EC 2.7.1.191]