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The RidA (YjgF/YER057c/UK114) family of proteins is broadly conserved in the three domains of life yet the functional understanding of these proteins is at an early stage. Physiological studies of  ridA  mutant strains of  Salmonella enterica  provided a framework to inform  in vitro  studies and led to the description of a conserved biochemical activity for this family.  ridA  mutant strains of  S. enterica  have characteristic phenotypes including new synthesis of thiamine biosynthetic intermediate phosphoribosylamine (PRA), inability to grow on pyruvate as a sole carbon and energy source or when serine is present in the minimal growth medium, and a decreased specific activity of transaminase B (IlvE). Secondary mutations restoring growth to a  ridA  mutant in the presence of serine were in  dapA  (encoding dihydrodipicolinate synthase) and  thrA  (encoding homoserine dehydrogenase). These mutations suppressed multiple  ridA  mutant phenotypes by increasing the synthesis of threonine. The ability of threonine to suppress the metabolic defects of a  ridA  mutant is discussed in the context of recent biochemical data and  in vivo  results presented here.

Suppressor Analyses Identify Threonine as a Modulator of ridA Mutant Phenotypes in Salmonella enterica