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 |
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 | - |
? |
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 | - |
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 | |
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 | |
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 |
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 | - |
? |
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 |
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 |
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 |