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2.1.1.182: 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase

This is an abbreviated version!
For detailed information about 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase, go to the full flat file.

Reaction

4 S-adenosyl-L-methionine +

adenine1518/adenine1519 in 16S rRNA
= 4 S-adenosyl-L-homocysteine +
N6-dimethyladenine1518/N6-dimethyladenine1519 in 16S rRNA

Synonyms

16S rRNA adenine dimethyltransferase, EC 2.1.1.48, KsgA, ksgA methyltransferase, RsmA, S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase

ECTree

     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.182 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase

Engineering

Engineering on EC 2.1.1.182 - 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase

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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
C168A
-
site-directed mutagenesis, the mutation does not affect KsgA activity
E43A
-
mutation located in the S-adenosylmethionine-binding motifs severely reduces methyltransferase activity, the mutation retains the ability to suppress the growth defect of the Era(E200K) strain at a low temperature
G47A
-
mutation located in the S-adenosylmethionine-binding motifs severely reduces methyltransferase activity, the mutation retains the ability to suppress the growth defect of the Era(E200K) strain at a low temperature
L114P
-
site-directed mutagenesis of the active site residue, the KsgA mutant shows diminished overall activity, and impaired ability to methylate the N6-methyladenosine intermediate to produce N6,N6-dimethyladenosine. Reduced activity is not due to disruption of 30S substrate binding
N113A
-
site-directed mutagenesis of the active site residue, the KsgA mutant shows diminishes activity to a level comparable to L114P without affecting the methylation of N6-methyladenosine. Reduced activity is not due to disruption of 30S substrate binding
R248A
-
mutation at the C-terminal does not affect the methyltransferase activity and fails to suppress the growth defect of the Era(E200K) strain