2.1.1.107	D227A	full activity	485091	
2.1.1.107	D248A	no transmethylase activity	485091	
2.1.1.107	D303A	full activity	485091	
2.1.1.107	D47N	binds about a quarter the quantity of S-adenosyl-L-methionine compared with wild-type, reaction product is only poxidised precorrin-1	662638	
2.1.1.107	E114Q	increase in the root mean square deviations of the uroporphyrinogen III substrate in respect to the wild-type	758359	
2.1.1.107	E114Q	the mutant shows strongly reduced activity compared to the wild type enzyme	719948	
2.1.1.107	F106A	considerably less soluble than wild-type, no binding of S-adenosyl-L-methionine, no enzymic activity	662638	
2.1.1.107	G12A	site-directed mutagenesis of cobA abolishes the tellurite resistance of the mesophilic, heterologous host Escherichia coli and the SUMT activity in vitro. Cells overexpressing SUMT G12A show 7fold less tolerance to K2TeO3 as compared to that exhibit by cells expressing the wild-type methyltransferase	-, 706702	
2.1.1.107	G189K	increase in activity compared to wild-type. The side chain of K189 makes electrostatic interactions with the propionate side chain of ring B with an average distance of 4.0 A. The backbone of K189 makes hydrogen bonds with the propionate side chain of ring B of uroporphyrinogen III	758359	
2.1.1.107	G189K	the mutant shows increased activity and reduced S-adenosyl-L-methionine-binding ability compared to the wild type enzyme	719948