ExplorEnz: EC 2.7.1.191

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2.7.1.191

Accepted name:

protein-N^π-phosphohistidine—D-mannose phosphotransferase

Reaction:

[protein]-N^π-phospho-L-histidine + D-mannose_{[side 1]} = [protein]-L-histidine + D-mannose 6-phosphate_{[side 2]}

Other name(s):

manXYZ (gene names); mannose PTS permease; EII^Man; Enzyme II^Man

Systematic name:

protein-N^π-phospho-L-histidine:D-mannose N^π-phosphotransferase

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:

BRENDA, EXPASY, KEGG, MetaCyc, PDB

References:

1.	Erni, B. and 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 (1985) 15495–15503. [PMID: 2999119]
2.	Williams, N., Fox, D.K., Shea, C. and 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. USA 83 (1986) 8934–8938. [DOI] [PMID: 2947241]
3.	Erni, B., Zanolari, B. and 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 (1987) 5238–5247. [PMID: 2951378]
4.	Stolz, B., Huber, M., Markovic-Housley, Z. and Erni, B. The mannose transporter of Escherichia coli. Structure and function of the IIABMan subunit. J. Biol. Chem. 268 (1993) 27094–27099. [PMID: 8262947]
5.	Rhiel, E., Flukiger, K., Wehrli, C. and Erni, B. The mannose transporter of Escherichia coli K12: oligomeric structure, and function of two conserved cysteines. Biol. Chem. Hoppe Seyler 375 (1994) 551–559. [PMID: 7811395]
6.	Huber, F. and Erni, B. Membrane topology of the mannose transporter of Escherichia coli K12. Eur. J. Biochem. 239 (1996) 810–817. [DOI] [PMID: 8774730]

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