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Literature summary for 2.1.1.192 extracted from

  • Atkinson, G.C.; Hansen, L.H.; Tenson, T.; Rasmussen, A.; Kirpekar, F.; Vester, B.
    Distinction between the Cfr methyltransferase conferring antibiotic resistance and the housekeeping RlmN methyltransferase (2013), Antimicrob. Agents Chemother., 57, 4019-4026.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.1.1.192

Cloned(Commentary)

Cloned (Comment) Organism
gene rlmN, sequence comparisons and phylogenetic analysis, primer extension analysis, cloning and expression in Escherichia coli strains TOP10 and AS19 Thermus thermophilus
gene rlmN, sequence comparisons and phylogenetic analysis, primer extension analysis, cloning and expression in Escherichia coli strains TOP10 and AS19 Bacillus subtilis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin Thermus thermophilus
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin Bacillus subtilis
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin Bacillus subtilis 168
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin Thermus thermophilus HB8 / ATCC 27634 / DSM 579
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
S-adenosyl-L-methionine + adenine2503 in 23S rRNA Escherichia coli the enzyme primarily methylates C-8 in A2503 of 23S rRNA S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
-
 ?
S-adenosyl-L-methionine + adenine2503 in 23S rRNA Mammaliicoccus sciuri the enzyme primarily methylates C-8 in A2503 of 23S rRNA S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
-
 ?

Organism

Organism UniProt Comment Textmining
Bacillus subtilis O34617 subsp. subtilis, gene rlmN
-
Bacillus subtilis 168 O34617 subsp. subtilis, gene rlmN
-
Escherichia coli
-
-
-
Mammaliicoccus sciuri Q9FBG4
-
-
Thermus thermophilus Q5SGZ3 gene rlmN
-
Thermus thermophilus HB8 / ATCC 27634 / DSM 579 Q5SGZ3 gene rlmN
-

Reaction

Reaction Comment Organism Reaction ID
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin the enzyme uses a mechanism involving radical S-adenosyl methionine to methylate RNA via an intermediate with a methylated cysteine in the enzyme and a transient cross-linking to the RNA Thermus thermophilus
a
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [2Fe-2S] ferredoxin the enzyme uses a mechanism involving radical S-adenosyl methionine to methylate RNA via an intermediate with a methylated cysteine in the enzyme and a transient cross-linking to the RNA Bacillus subtilis
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
-
 Thermus thermophilus S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
-
 Bacillus subtilis S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
-
 Bacillus subtilis 168 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
-
 Thermus thermophilus HB8 / ATCC 27634 / DSM 579 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?
S-adenosyl-L-methionine + adenine2503 in 23S rRNA the enzyme primarily methylates C-8 in A2503 of 23S rRNA Escherichia coli S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
-
 ?
S-adenosyl-L-methionine + adenine2503 in 23S rRNA the enzyme primarily methylates C-8 in A2503 of 23S rRNA Mammaliicoccus sciuri S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 2-methyladenine2503 in 23S rRNA
-
 ?

Synonyms

Synonyms Comment Organism
Cfr
-
 Mammaliicoccus sciuri
RlmN
-
 Escherichia coli
RlmN methyltransferase
-
 Thermus thermophilus
RlmN methyltransferase
-
 Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
S-adenosyl-L-methionine
-
 Thermus thermophilus
S-adenosyl-L-methionine
-
 Bacillus subtilis

General Information

General Information Comment Organism
evolution comparative sequence analysis identifies differentially conserved residues that indicate functional sequence divergence between the two classes of Cfr and RlmN-like sequences. The enzymes are homologous and use the same mechanism involving radical S-adenosyl methionine to methylate RNA via an intermediate involving a methylated cysteine in the enzyme and a transient cross-linking to the RNA, but they differ in which carbon atom in the adenine they methylate. The differentiation between the two classes is supported by experimental evidence from antibiotic resistance, primer extensions, and mass spectrometry. The Cfr- and RlmN-specific conserved sites provide a very good indication of whether a gene is Cfr-like or RlmN-like. Most bacteria have an rlmN-like gene and all those that have a cfr-like gene also have an rlmN-like gene, evolutionary aspects of the bacterial distribution of Cfr and RlmN-like enzymes, overview Thermus thermophilus
evolution comparative sequence analysis identifies differentially conserved residues that indicate functional sequence divergence between the two classes of Cfr and RlmN-like sequences. The enzymes are homologous and use the same mechanism involving radical S-adenosyl methionine to methylate RNA via an intermediate involving a methylated cysteine in the enzyme and a transient cross-linking to the RNA, but they differ in which carbon atom in the adenine they methylate. The differentiation between the two classes is supported by experimental evidence from antibiotic resistance, primer extensions, and mass spectrometry. The Cfr- and RlmN-specific conserved sites provide a very good indication of whether a gene is Cfr-like or RlmN-like. Most bacteria have an rlmN-like gene and all those that have a cfr-like gene also have an rlmN-like gene, evolutionary aspects of the bacterial distribution of Cfr and RlmN-like enzymes, overview Bacillus subtilis
physiological function the RlmN methyltransferase primarily methylates C-2 in A2503 of 23S rRNA in the peptidyl transferase region of bacterial ribosomes. Enzyme RlmN does not confer resistance to antibiotics Thermus thermophilus
physiological function the RlmN methyltransferase primarily methylates C-2 in A2503 of 23S rRNA in the peptidyl transferase region of bacterial ribosomes. Enzyme RlmN does not confer resistance to antibiotics Bacillus subtilis