Information on EC 2.1.1.180 - 16S rRNA (adenine1408-N1)-methyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.180
-
RECOMMENDED NAME
GeneOntology No.
16S rRNA (adenine1408-N1)-methyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + adenine1408 in 16S rRNA = S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase
The enzyme provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N1-methylation at position adenine1408 [4].
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + adenosine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenosine1408 in 16S rRNA
show the reaction diagram
the enzyme provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N-1 methylation at position A1408
-
-
?
sinefungin + adenine1408 in 16S rRNA
?
show the reaction diagram
additional information
?
-
-
the enzyme possesses also methylates 30S subunits with guanine1408
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + adenosine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenosine1408 in 16S rRNA
show the reaction diagram
A8C927
the enzyme provides a panaminoglycoside-resistant nature through interference with the binding of aminoglycosides toward the A site of 16S rRNA through N-1 methylation at position A1408
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
gene sequence is used for protein structure prediction, model of ShKamB
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 0.03 M Bis-Tris (pH 5.5) and 25.5% (w/v) polyethylene glycol 3350
-
high-resolution crystal structures of NpmA from Escherichia coli is determined at 1.69 A
-
in complex with the 30S ribosome subunit and sinefungin
-
high-resolution crystal structures of KamB from Streptoalloteichus tenebrarius is determined at 1.69 A
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
His-tagged NpmA
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
expression in Escherichia coli under the control of the lpp promoter
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D21A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
E94A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
K115A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
R43A/R73A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
R66A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
S201A
-
the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
S202A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W113A
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W113F
-
the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W203A
-
the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W203F
-
the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
D30A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function SAM-binding: mutant highly affected
D55A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function SAM-binding: mutant highly affected
E88A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
K174A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: no difference to wild-type
K37A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant highly affected
K58A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
K63A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
K67A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
K71A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
K74A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
N138A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
R179A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
R195A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
R196A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant highly affected
R201A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant highly affected
R203A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
R60A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
R8A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant moderately affected
S107A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function RNA/30S binding: mutant slightly affected
T191A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function SAM-binding: mutant highly affected
W105A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
W105F
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
W193A
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected
W193F
mutant protein is tested for its ability to support bacterial growth in the presence of kanamycin. Proposed function A1408 Positioning/catalysis: mutant highly affected