The gene from encoding the formate-dependent glycinamide ribonucleotide transformylase T was cloned by functional complementation of an double mutant. The nucleotide sequence revealed an open reading frame of 384 amino acids. The amino acid sequence showed similarity to the enzyme phosphoribosylaminoimidazole carboxylase encoded by the gene but not to the -formyltetrahydrofolate-dependent glycinamide ribonucleotide transformylase N enzyme encoded by the gene. The glycinamide ribonucleotide transformylase T level was repressed in cells grown in rich medium compared to minimal-medium-grown cells. However, when the culture entered the stationary-growth phase the enzyme level increased in rich medium and decreased in minimal medium. By comparing the deduced amino acid sequence of the gene product with translated nucleotide sequences in various databanks, evidence for the existence of putative genes in the Gram-negative bacteria and was obtained.


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