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cobalt-precorrin-5B (C(1))-methyltransferase
CbiD is essential for cobalamin biosynthesis in both S. typhimurium and B. megaterium, no functional role has been ascribed to the protein. The CbiD protein has a putative S-AdoMet binding site. It is possible that CbiD might have the same role as CobF in undertaking the C-1 methylation and deacylation reactions required during the ring contraction process [1]. [1]. 9742225. Cobalamin (vitamin B12) biosynthesis: identification and characterization of a Bacillus megaterium cobI operon. Raux E, Lanois A, Warren MJ, Rambach A, Thermes C;. Biochem J 1998;335:159-166. (from Pfam)
cobalt-precorrin-5B (C(1))-methyltransferase CbiD
The methyltransferase CbiD belongs to an anaerobic pathway for cobalamin biosynthesis, one in which cobalt is added early.
cobalt-precorrin-5B (C(1))-methyltransferase catalyzes the methylation of C-1 in cobalt-precorrin-5B to form cobalt-precorrin-6A
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