Identification of a novel lipoic acid biosynthesis pathway reveals the complex evolution of lipoate assembly in prokaryotes
Fig 3
Taxonomic distribution of the lipoate synthesis systems, lipoate scavenging, and lipoate requiring proteins.
Venn diagrams show the abundance and overlap of lipoate:protein ligases (Lpl), octanoyl transferase (LipB, LipM), and lipoate synthases (LipA, LipS1/S2) in the bacteria (a) and the archaea (b). Panels c and d visualize the taxonomic distribution of these enzymes, the sulfur-oxidizing sHdr system (S) and lipoate-binding domains (LD). For each bacterial (c) and archaeal phylum (d), the percentage of genomes possessing these proteins is indicated by dots of different sizes and colors. Note that the proportion was normalized to the size of the phylum and does not show absolute counts or overall phylum size. The data underlying parts a and b are provided in S2 and S3 Tables, respectively. S4 Table supplies the data underlying parts c and d.