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methyltransferase domain-containing protein
This family appears to be a methyltransferase domain. (from Pfam)
methyltransferase
Members of this family are SAM dependent methyltransferases. (from Pfam)
class I SAM-dependent methyltransferase
This family consist of Cyclopropane-fatty-acyl-phospholipid synthase or CFA synthase EC:2.1.1.79 this enzyme catalyse the reaction: S-adenosyl-L-methionine + phospholipid olefinic fatty acid <=> S-adenosyl-L-homocysteine + phospholipid cyclopropane fatty acid. [1]. 8917504. A common mechanism for the biosynthesis of methoxy and cyclopropyl mycolic acids in Mycobacterium tuberculosis. Yuan Y, Barry CE 3rd;. Proc Natl Acad Sci U S A 1996;93:12828-12833. [2]. 7592990. The biosynthesis of cyclopropanated mycolic acids in Mycobacterium tuberculosis. Identification and functional analysis of CMAS-2. George KM, Yuan Y, Sherman DR, Barry CE 3d;. J Biol Chem 1995;270:27292-27298. [3]. 10882107. A novel mycolic acid cyclopropane synthetase is required for cording, persistence, and virulence of Mycobacterium tuberculosis. Glickman MS, Cox JS, Jacobs WR Jr;. Mol Cell. 2000;5:717-727. (from Pfam)
cyclopropane mycolic acid synthase family methyltransferase
Members of this family include tailoring enzymes that make site-specific modifications to mycolic acid precursor molecules. These include Mycobacterium tuberculosis enzymes MmaA1-MmaA4, CmaA1-CmaA2, and PcaA. The family also includes UmaA, reported to be the lone member of this family not involved in mycolic acid biosynthesis. No members of this family are found in species that lack mycolic acids. This model excludes two more distantly related paralogs, Rv0447c (UfaA1 ) and Rv3720, that are also encoded in the Mycobacterium tuberculosis H37Rv genome.
cyclopropane mycolic acid synthase CmaA1
class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor; similar to Mycobacterium tuberculosis mycolic acid cyclopropane synthases (such as PcaA, CmaA, and MmaA) that are responsible for site-specific modifications of mycolic acids
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