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pubmed-article:2172696pubmed:abstractTextThe genes encoding the proteins of the fructose-specific phosphotransferase system (PTS) of Rhodobacter capsulatus were sequenced, and the deduced amino acyl sequences of the energy-coupling protein, Enzyme I, and the transport protein, Enzyme IIfru, were compared with published sequences. Enzyme I was found to be homologous to pyruvate:phosphate dikinase of plants, while Enzyme IIfru was found to be homologous to the insulin-responsive glucose facilitator of mammals. The evolutionary and functional implications of these findings are discussed.lld:pubmed
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pubmed-article:2172696pubmed:articleTitleOn the evolutionary origins of the bacterial phosphoenolpyruvate:sugar phosphotransferase system.lld:pubmed
pubmed-article:2172696pubmed:affiliationDepartment of Biology, University of California, San Diego, La Jolla 92093.lld:pubmed
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pubmed-article:2172696pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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