EC Number | Cloned (Comment) | Organism |
---|---|---|
2.1.1.173 | gene rlmKL, DNA and amino acid sequence determination and analysis, gene rlmL/ycbY has been renamed rlmKL | Escherichia coli |
2.1.1.264 | gene rlmK, expression in Escherichia coli DELTArlmKL mutant | Neisseria meningitidis |
2.1.1.264 | gene rlmL, renamed rlmKL, encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445 | Escherichia coli |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
2.1.1.173 | additional information | generation of several base-flipping mutant enzymes lacking m2G2445 formation activity, overview | Escherichia coli |
2.1.1.264 | D195A | site-directed mutagenesis, the mutation does not affect the methylation activity | Escherichia coli |
2.1.1.264 | D568A | site-directed mutagenesis, the D568A mutation in the C-terminal domain does not rescue m7G2069 formation, but m2G2445 is efficiently formed in this mutant | Escherichia coli |
2.1.1.264 | D597A | site-directed mutagenesis, the mutation does not affect the methylation activity | Escherichia coli |
2.1.1.264 | N309A | site-directed mutagenesis, the N309A mutation in the NTD impairs m2G2445 formation, but rescues m7G2069 formation | Escherichia coli |
2.1.1.264 | N397A | site-directed mutaagenesis, the N397A mutant exhibits no m2G2445 formation but rescues m7G2069 formation | Escherichia coli |
2.1.1.264 | R530A | site-directed mutagenesis, the mutation does not affect the methylation activity | Escherichia coli |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.173 | Mg2+ | required | Escherichia coli |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.173 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | Escherichia coli | - |
S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? | |
2.1.1.173 | S-adenosyl-L-methionine + guanine2445 in 23S rRNA | Escherichia coli | - |
S-adenosyl-L-homocysteine + N2-methylguanine2445 in 23S rRNA | - |
? | |
2.1.1.264 | additional information | Escherichia coli | the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173 | ? | - |
? | |
2.1.1.264 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | Escherichia coli | RlmK activity in helix 74 of Escherichia coli 23S rRNA | S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? | |
2.1.1.264 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | Neisseria meningitidis | RlmK activity in helix 74 of Escherichia coli 23S rRNA | S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? | |
2.1.1.264 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | Neisseria meningitidis MC58 | RlmK activity in helix 74 of Escherichia coli 23S rRNA | S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
2.1.1.173 | Escherichia coli | - |
gene rlmL/ycbY has been renamed rlmKL | - |
2.1.1.264 | Escherichia coli | - |
gene rlmL, renamed rlmKL | - |
2.1.1.264 | Neisseria meningitidis | Q9JYY8 | gene rlmK | - |
2.1.1.264 | Neisseria meningitidis MC58 | Q9JYY8 | gene rlmK | - |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
2.1.1.173 | additional information | helix 80 and the 12 nt ss region are critical sites necessary for m2G2445 and m7G2069 formation. Transcript 7, which lacks helix 80 and the 12 nt single-strand region, is not methylated at either position | Escherichia coli | ? | - |
? | |
2.1.1.173 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | - |
Escherichia coli | S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? | |
2.1.1.173 | S-adenosyl-L-methionine + guanine2445 in 23S rRNA | - |
Escherichia coli | S-adenosyl-L-homocysteine + N2-methylguanine2445 in 23S rRNA | - |
? | |
2.1.1.173 | S-adenosyl-L-methionine + guanine2445 in 23S rRNA | duplex formation of H74 is not required for the m2G2445 formation. The 29-mer single-stranded transcript 6, which consists of residues C2422 to A2450, can form m2G2445 efficiently | Escherichia coli | S-adenosyl-L-homocysteine + N2-methylguanine2445 in 23S rRNA | - |
? | |
2.1.1.264 | additional information | the enzyme also catalyzes the N2-methylation of guanine2445 in 23S rRNA, RlmL activity, reaction of EC 2.1.1.173 | Escherichia coli | ? | - |
? | |
2.1.1.264 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | RlmK activity in helix 74 of Escherichia coli 23S rRNA | Escherichia coli | S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? | |
2.1.1.264 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | RlmK activity in helix 74 of Escherichia coli 23S rRNA | Neisseria meningitidis | S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? | |
2.1.1.264 | S-adenosyl-L-methionine + guanine2069 in 23S rRNA | RlmK activity in helix 74 of Escherichia coli 23S rRNA | Neisseria meningitidis MC58 | S-adenosyl-L-homocysteine + N7-methylguanine2069 in 23S rRNA | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
2.1.1.173 | More | RlmKL is a fused methyltransferase consisting of an N-terminal RlmL domain and a C-terminal RlmK domain | Escherichia coli |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
2.1.1.173 | m2G2445 methyltransferase | - |
Escherichia coli |
2.1.1.173 | RlmKL | - |
Escherichia coli |
2.1.1.173 | RlmL | - |
Escherichia coli |
2.1.1.264 | rlmK | - |
Escherichia coli |
2.1.1.264 | rlmK | - |
Neisseria meningitidis |
2.1.1.264 | RlmKL | - |
Escherichia coli |
EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|---|
2.1.1.173 | 37 | - |
assay at | Escherichia coli |
2.1.1.264 | 37 | - |
assay at | Escherichia coli |
EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|---|
2.1.1.173 | 7.5 | - |
assay at | Escherichia coli |
2.1.1.264 | 7.5 | - |
assay at | Escherichia coli |
EC Number | Cofactor | Comment | Organism | Structure |
---|---|---|---|---|
2.1.1.173 | S-adenosyl-L-methionine | - |
Escherichia coli | |
2.1.1.264 | S-adenosyl-L-methionine | - |
Escherichia coli |
EC Number | General Information | Comment | Organism |
---|---|---|---|
2.1.1.173 | malfunction | deletion of rlmL/ycbY results in a slight growth reduction phenotype | Escherichia coli |
2.1.1.173 | additional information | RlmKL is involved in the efficient assembly of 50S subunit in a mutant strain lacking an RNA helicase deaD | Escherichia coli |
2.1.1.173 | physiological function | cooperative methylation of helix 74 by RlmKL plays a key role in the efficient assembly of the 50S subunit, RlmKL enzyme is an example of a methyltransferase catalyzing two mechanistically different types of RNA modification. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. Methyltransferase RlmL, encoded by rlmL/ycbY, catalyzes S-adenosyl-L-methionine-dependent m2G2445 formation | Escherichia coli |
2.1.1.264 | malfunction | Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain | Escherichia coli |
2.1.1.264 | malfunction | Neisseria meningitidis rlmL and rlmK homologues rescue m2G2445 and m7G2069 formation, respectively, in the Escherichia coli DELTArlmKL strain, overview | Neisseria meningitidis |
2.1.1.264 | physiological function | rlmKL encodes a fused methyltransferase responsible for forming both m7G2069 and m2G2445, the N-terminal RlmL activity for m2G2445 formation is significantly enhanced by the C-terminal RlmK. RlmKL has an unwinding activity of Helix 74, facilitating cooperative methylations of m7G2069 and m2G2445 during biogenesis of 50S subunit. For unwinding single-stranded RNA is a good substrate for RlmKL, substrate speccificity, overview. RlmKL is involved in the efficient assembly of 50S subunit in a mutant strain lacking an RNA helicase deaD | Escherichia coli |