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Significance Biotin is an enzyme cofactor required for growth of mycobacteria, and theMycobacterium tuberculosis biotin synthetic pathway has become a validated target for antitubercular compounds. Current pathway lacks information on synthesis of the pimelate moiety that provides 7 of the 10 biotin carbon atoms. We report the first step in mycobacterial pimelate synthesis parallels the pathway first reported inEscherichia coli , in which BioC catalyzedO -methylation of a malonyl-acyl carrier protein primer allows entry into fatty acid synthesis. The mycobacterial Tam proteins functionally replace theE. coli BioC protein, although these proteins are annotated as performing a different function Moreover,tam gene function is required for biotin synthesis byMycobacterium smegmatis and its transcription is repressed by exogenous biotin.

The primary step of biotin synthesis in mycobacteria