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precorrin-8X methylmutase
This is a family Precorrin-8X methylmutases also known as Precorrin isomerase, CbiC/CobH, EC:5.4.1.2. This enzyme catalyses the reaction: Precorrin-8X <=> hydrogenobyrinate. This enzyme is part of the Cobalamin (vitamin B12) biosynthetic pathway and catalyses a methyl rearrangement [1,2]. [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. [2]. 8501034. Characterization of the cobalamin (vitamin B12) biosynthetic genes of Salmonella typhimurium. Roth JR, Lawrence JG, Rubenfield M, Kieffer-Higgins S, Church GM;. J Bacteriol 1993;175:3303-3316. (from Pfam)
SAM-dependent methyltransferase
This family uses S-AdoMet in the methylation of diverse substrates. This family includes a related group of bacterial proteins of unknown function, including Swiss:P45528. This family includes the methylase Dipthine synthase. (from Pfam)
precorrin-3B C(17)-methyltransferase
This HMM represents precorrin-3B C17-methyltransferase, one of two methyltransferases commonly referred to as precorrin-3 methylase (the other is precorrin-4 C11-methyltransferase, EC 2.1.1.133). This enzyme participates in the pathway toward the biosynthesis of cobalamin and related products. Members of this family may appear as fusion proteins with other enzymes of cobalamin biosynthesis.
bifunctional precorrin-2 C(20)-methyltransferase/precorrin-3B C(17)-methyltransferase; SAM-dependent methyltransferase
bifunctional precorrin-2 C(20)-methyltransferase/precorrin-3B C(17)-methyltransferase participates in the pathway toward the biosynthesis of cobalamin (vitamin B12), catalyzing the methylation at the C-20 position of a cyclic tetrapyrrole ring of precorrin-2 to produce precorrin-3A and the methylation of precorrin-3b at C-17 to form precorrin-4| SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor
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