Production of branched α-glucan, glycogen-like polymers is widely spread in the Bacteria domain. The glycogen pathway of synthesis and degradation has been fairly well characterized in the model enterobacterial species
Escherichia coli (order
Enterobacteriales, class
Gammaproteobacteria), in which the cognate genes (branching enzyme
glgB, debranching enzyme
glgX, ADP-glucose pyrophosphorylase
glgC, glycogen synthase
glgA, and glycogen phosphorylase
glgP) are clustered in a
glgBXCAP operon arrangement. However, the evolutionary origin of this particular arrangement and of its constituent genes is unknown. Here, by using 265 complete gammaproteobacterial genomes we have carried out a comparative analysis of the presence, copy number and arrangement of
glg genes in all lineages of the
Gammaproteobacteria. These analyses revealed large variations in
glg gene presence, copy number and arrangements among different gammaproteobacterial lineages. However, the
glgBXCAP arrangement was remarkably conserved in all
glg-possessing species of the orders
Enterobacteriales and
Pasteurellales (the E/P group). Subsequent phylogenetic analyses of
glg genes present in the
Gammaproteobacteria and in other main bacterial groups indicated that
glg genes have undergone a complex evolutionary history in which horizontal gene transfer may have played an important role. These analyses also revealed that the E/P
glgBXCAP genes (a) share a common evolutionary origin, (b) were vertically transmitted within the E/P group, and (c) are closely related to
glg genes of some phylogenetically distant betaproteobacterial species. The overall data allowed tracing the origin of the
E. coli glgBXCAP operon to the last common ancestor of the E/P group, and also to uncover a likely
glgBXCAP transfer event from the E/P group to particular lineages of the
Betaproteobacteria.
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