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Literature summary for 2.1.1.190 extracted from

  • Auxilien, S.; Rasmussen, A.; Rose, S.; Brochier-Armanet, C.; Husson, C.; Fourmy, D.; Grosjean, H.; Douthwaite, S.
    Specificity shifts in the rRNA and tRNA nucleotide targets of archaeal and bacterial m5U methyltransferases (2011), RNA, 17, 45-53.
    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 + uracil1939 in 23S rRNA Escherichia coli
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S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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?

Organism

Organism UniProt Comment Textmining
Escherichia coli
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gene rlmD
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
S-adenosyl-L-methionine + uracil1939 in 23S rRNA
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Escherichia coli S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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?
S-adenosyl-L-methionine + uracil1939 in 23S rRNA rRNA substrate structure, overview Escherichia coli S-adenosyl-L-homocysteine + 5-methyluracil1939 in 23S rRNA
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?

Synonyms

Synonyms Comment Organism
m5U methyltransferase
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Escherichia coli
RlmD
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Escherichia coli
RNA m5U methyltransferase
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Escherichia coli
RumA formerly Escherichia coli

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
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Escherichia coli

General Information

General Information Comment Organism
physiological function RlmD is the archetypical enzyme that is specific for m5U1939 in 23S rRNA Escherichia coli