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Literature summary 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

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.1.1.192 gene rlmN, sequence comparisons and phylogenetic analysis, primer extension analysis, cloning and expression in Escherichia coli strains TOP10 and AS19 Thermus thermophilus
2.1.1.192 gene rlmN, sequence comparisons and phylogenetic analysis, primer extension analysis, cloning and expression in Escherichia coli strains TOP10 and AS19 Bacillus subtilis
2.1.1.224 gene cfr, sequence comparisons and phylogenetic analysis, primer extension analysis, cloning and expression in Escherichia coli strains TOP10 and AS19 Mammaliicoccus sciuri

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin Mammaliicoccus sciuri
-
 S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?

Organism

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

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.192 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
2.1.1.192 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
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [2Fe-2S] ferredoxin = S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-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 Mammaliicoccus sciuri
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.192 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
-
 ?
2.1.1.224 2 S-adenosyl-L-methionine + adenine2503 in 23S rRNA + 2 reduced [4Fe-4S] ferredoxin
-
 Mammaliicoccus sciuri S-adenosyl-L-homocysteine + L-methionine + 5'-deoxyadenosine + 8-methyladenine2503 in 23S rRNA + 2 oxidized [4Fe-4S] ferredoxin
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.1.1.192 Cfr
-
 Mammaliicoccus sciuri
2.1.1.192 RlmN
-
 Escherichia coli
2.1.1.192 RlmN methyltransferase
-
 Thermus thermophilus
2.1.1.192 RlmN methyltransferase
-
 Bacillus subtilis
2.1.1.224 Cfr methyltransferase
-
 Mammaliicoccus sciuri

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.192 S-adenosyl-L-methionine
-
 Thermus thermophilus
2.1.1.192 S-adenosyl-L-methionine
-
 Bacillus subtilis
2.1.1.224 S-adenosyl-L-methionine
-
 Mammaliicoccus sciuri

General Information

EC Number General Information Comment Organism
2.1.1.192 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
2.1.1.192 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
2.1.1.192 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
2.1.1.192 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
2.1.1.224 evolution the cfr gene can be horizontally transferred to its hosts, as it is always found either on plasmids or together with insertion sequences. The cfr gene with only minor sequence differences are found worldwide in various bacteria isolated from humans and animals. 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 that 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 Mammaliicoccus sciuri
2.1.1.224 physiological function the Cfr methyltransferase primarily methylates C-8 in A2503 of 23S rRNA in the peptidyl transferase region of bacterial ribosomes. Enzyme Cfr confers resistance to antibiotics binding to the peptidyl transferase center on the ribosome, defining a PhLOPSa phenotype that reflects resistance to phenicol, lincosamide, oxazolidinone, pleuromutilin, and streptogramin A antibiotic classes. Cfr also provides resistance to some large macrolide antibiotics. The cfr gene is thus a health threat when spreading in pathogenic bacteria because many clinically important antibiotics become useless for treatment Mammaliicoccus sciuri