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tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE
This family consists of several bacterial tRNA-(MS(2)IO(6)A)-hydroxylase (MiaE) proteins. The modified nucleoside 2-methylthio-N-6-isopentenyl adenosine (ms2i6A) is present at position 37 (3' of the anticodon) of tRNAs that read codons beginning with U except tRNA(I,V Ser) in Escherichia coli. Salmonella typhimurium 2-methylthio-cis-ribozeatin (ms2io6A) is found in tRNA, probably in the corresponding species that have ms2i6A in E. coli. The miaE gene is absent in E. coli, a finding consistent with the absence of the hydroxylated derivative of ms2i6A in this species [1-2]. [1]. 8253666. Isolation of the gene (miaE) encoding the hydroxylase involved in the synthesis of 2-methylthio-cis-ribozeatin in tRNA of Salmonella typhimurium and characterization of mutants. Persson BC, Bjork GR;. J Bacteriol 1993;175:7776-7785. [2]. 17679698. tRNA-modifying MiaE protein from Salmonella typhimurium is a nonheme diiron monooxygenase. Mathevon C, Pierrel F, Oddou JL, Garcia-Serres R, Blondin G, Latour JM, Menage S, Gambarelli S, Fontecave M, Atta M;. Proc Natl Acad Sci U S A. 2007;104:13295-13300. (from Pfam)
tRNA isopentenyl-2-thiomethyl-A-37 hydroxylase MiaE catalyzes the oxygen-dependent transformation of 2-methylthio-N-6-isopentenyl adenosine (ms[2]i[6]A) into ms[2]io[6]A, a modified nucleoside found in some tRNAs; belongs to a broad superfamily of ferritin-like diiron-carboxylate proteins
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