2.1.1.176: 16S rRNA (cytosine967-C5)-methyltransferase
This is an abbreviated version!
For detailed information about 16S rRNA (cytosine967-C5)-methyltransferase, go to the full flat file.
Reaction
Synonyms
16S rRNA m5C967 methyltransferase, 16S rRNA methyltransferase, fma, fmu, Fmu/RsmB/RrmB, Fmu/RsmB/RrmB rRNA cytosine 5-methyltransferase, m5C methyltransferase Fmu, PH0851, RNA:m5C MTase, rsmB
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General Information
General Information on EC 2.1.1.176 - 16S rRNA (cytosine967-C5)-methyltransferase
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evolution
malfunction
metabolism
additional information
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Fmu/RsmB/RrmB homologues exist not only in bacteria but also in archaea and eukarya and constitute a large orthologous group in the RNA:m5C methyltransferase family. The sequence of the N-terminal domain is negligibly conserved between the bacterial and archaeal subfamilies
evolution
Fmu/RsmB/RrmB homologues exist not only in bacteria but also in archaea and eukarya and constitute a large orthologous group in the RNA:m5C methyltransferase family. The sequence of the N-terminal domain is negligibly conserved between the bacterial and archaeal subfamilies
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deletion of rsmB in a C-terminal S9 tail deletion strain of Escherichia coli causes significantly increased -1 frameshifting at 37°C
malfunction
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deletion of rsmB in a C-terminal S9 tail deletion strain of Escherichia coli causes significantly increased -1 frameshifting at 37°C
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two methyltransferases, RsmB and RsmF, are responsible for all four 5-methylcytidine modifications in 16S rRNA of Thermus thermophilus, overview. RsmB produces m5C967, while RsmF methylates C1400, C1404, and C1407 in a 30S subunit substrate, but only C1400 and C1404 when naked 16S rRNA is the substrate
metabolism
Thermus thermophilus HB8 / ATCC 27634 / DSM 579
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two methyltransferases, RsmB and RsmF, are responsible for all four 5-methylcytidine modifications in 16S rRNA of Thermus thermophilus, overview. RsmB produces m5C967, while RsmF methylates C1400, C1404, and C1407 in a 30S subunit substrate, but only C1400 and C1404 when naked 16S rRNA is the substrate
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next to the S-adenosyl-L-methionine-binding site is a positively charged cleft, formed between the N- and C-terminal domains, which is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate
additional information
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next to the S-adenosyl-L-methionine-binding site is a positively charged cleft, formed between the N- and C-terminal domains, which is conserved in the archaeal PH0851 homologues and seems to be suitable for binding the RNA substrate