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Literature summary for 2.1.1.174 extracted from

  • Sergiev, P.V.; Bogdanov, A.A.; Dontsova, O.A.
    Ribosomal RNA guanine-(N2)-methyltransferases and their targets (2007), Nucleic Acids Res., 35, 2295-2301.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
S-adenosyl-L-methionine + guanine1835 in 23S rRNA Escherichia coli
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S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
-
?

Organism

Organism UniProt Comment Textmining
Escherichia coli Q0T0I4
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + guanine1835 in 23S rRNA
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Escherichia coli S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
-
?
S-adenosyl-L-methionine + guanine1835 in 23S rRNA RlmG possessing an additional RNA-binding domain act on naked ribosomal RNA or early assembly intermediates in the cell Escherichia coli S-adenosyl-L-homocysteine + N2-methylguanine1835 in 23S rRNA
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?

Synonyms

Synonyms Comment Organism
ribosomal RNA large subunit methyltransferase G
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Escherichia coli
RlmG
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Escherichia coli
ygjO
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Escherichia coli

General Information

General Information Comment Organism
malfunction lack of G1835 methylation in rlmG(ygjO) knockout strain does not lead to significant growth retardation at the optimal growth conditions. However, in the poor medium and at elevated temperature, the rlmG(ygjO) knockout strain has significantly decreased fitness Escherichia coli