Category:Complex:EIIAga

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Description (originally from EcoCyc[1][2]) EIIAga

Comments (originally from EcoCyc[1][2]) AgaBCDVWX, the putative N-acetylgalactosamine PTS permease, belongs to the functional superfamily of the phosphoenolpyruvate (PEP)-dependent, sugar transporting phosphotransferase system (PTS). The PTS transports and simultaneously phosphorylates its sugar substrates in a process called group translocation. AgaBCDVWX may take up exogenous N-acetylgalactosamine, releasing the phosphate ester into the cell cytoplasm in preparation for metabolism [3][4] . The overall PTS-mediated phosphoryl transfer reaction, requiring the two general energy coupling proteins of the PTS, Enzyme I and HPr, as well as the four domains of the Enzyme II complex is proposed to be:

PEP --> Enzyme I(his~~P) --> HPr(his~~P) --> IIA(his~~P) --> IIB(his~~P) -(IICD)-> N-acetylgalactosamine-6-P.

The aga operon (agaZVWASYBCDI) also encodes putative enzymes that may be a kinase (AgaZ), a deacetylase (AgaA), a synthase (AgaS), an aldolase (AgaY) and an isomerase (AgaI), all sugar metabolic enzymes. The agaR gene, encoding a putative transcriptional regulatory protein, precedes and is divergently transcribed from the aga operon. Nothing is known concerning expression of the aga operon. It may be cryptic in wild type E. coli K12.


References

  1. 1.0 1.1 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  2. 2.0 2.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
  3. Postma, PW et al. (1993) Phosphoenolpyruvate:carbohydrate phosphotransferase systems of bacteria. Microbiol. Rev. 57 543-94 PubMed
  4. Reizer, J et al. (1996) Novel phosphotransferase genes revealed by bacterial genome sequencing: a gene cluster encoding a putative N-acetylgalactosamine metabolic pathway in Escherichia coli. Microbiology (Reading, Engl.) 142 ( Pt 2) 231-50 PubMed

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