Information on EC 2.1.1.179 - 16S rRNA (guanine1405-N7)-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.179
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RECOMMENDED NAME
GeneOntology No.
16S rRNA (guanine1405-N7)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1405 in 16S rRNA = S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine1405-N7)-methyltransferase
The enzyme from the antibiotic-producing bacterium Micromonospora zionensis specifically methylates guanine1405 at N7 in 16S rRNA, thereby rendering the ribosome resistant to 4,6-disubstituted deoxystreptamine aminoglycosides, which include gentamicins and kanamycins [2].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
RmtD2; gene rmtD2
UniProt
Manually annotated by BRENDA team
i.e. strain BB1074, gene rmtC
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Manually annotated by BRENDA team
strain Ccl3
UniProt
Manually annotated by BRENDA team
strain Ccl3
UniProt
Manually annotated by BRENDA team
; gene rmtF encoded on a non-self-transferable plasmid pIP849
UniProt
Manually annotated by BRENDA team
gene rmtF encoded on a non-self-transferable plasmid pIP849
UniProt
Manually annotated by BRENDA team
Smr1; gene smr1
UniProt
Manually annotated by BRENDA team
FmrO; gene fmrO
UniProt
Manually annotated by BRENDA team
GrmB; gene grmB
UniProt
Manually annotated by BRENDA team
plasmid pAT780
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Manually annotated by BRENDA team
plasmid pIP1206
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Manually annotated by BRENDA team
RmtB; gene rmtB
UniProt
Manually annotated by BRENDA team
NbrB; gene nbrB
UniProt
Manually annotated by BRENDA team
Kmr; gene kmr
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
physiological function
additional information
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 + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
show the reaction diagram
additional information
?
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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 + cytosine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 5-methylcytosine1405 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + 7-methylguanine1405 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine1405 in 16S rRNA
S-adenosyl-L-homocysteine + N7-methylguanine1405 in 16S rRNA
show the reaction diagram
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
16S rRNA methyltransferase ArmA
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29500
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x * 29500, RmtD2, SDS-PAGE; x * 29500, RmtD, SDS-PAGE
30669
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x * 30669, calculated from sequence
31500
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x * 31500, RmtG, SDS-PAGE
32400
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x * 32400, SDS-PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
RmtB containing S-adenosyl-L-homocysteine in the active site
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purified Sgm is complexed with 5 mM of the cofactors S-adenosylmethionine/S-adenosylhomocysteine. Crystallization trials are carried out at room temperature by hanging-drop vapor-diffusion method, structure of Sgm in complex with cofactors S-adenosylmethionine and S-adenosylhomocysteine is determined at 2.0 A and 2.1 A resolution, respectively
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45 - 50
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Sgm is fully stable up to 45 to 50°C, after which point the spectra become progressively more like those of an unstructured random coil. No further change is observed beyond 65°C, where all secondary structure appears to be lost
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Ni2+ affinity column chromatography and Superdex 75 gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned in Streptomyces lividans. The sgm gene is expressed in Micromonospora melanosporea, where its own promoter is active, and also in Escherichia coli under the control of the lacZ promoter
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cloning of the sgm gene into pET-25b (+) vector with the addition of N-terminal non-cleavable His6 tag, as well as alanine mutagenesis of residues D156, D182 and R108. The constructs are co-transformed along with pGroESL into the strain BL21 (DE3) of Escherichia coli for protein expression
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expressed in Escherichia coli BL21(DE3) cells
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expression in Escherichia coli
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expression in Escherichia coli, Bacillus subtilis or Staphylococcus aureus
gene fmrO, phylogenetic analysis, sequence comparisons
gene grmA, phylogenetic analysis, sequence comparisons
gene grmB, phylogenetic analysis, sequence comparisons
gene kmr, phylogenetic analysis, sequence comparisons
gene nbrB, phylogenetic analysis, sequence comparisons
gene rmtA, phylogenetic analysis, sequence comparisons; phylogenetic analysis, sequence comparisons
gene rmtB, phylogenetic analysis, sequence comparisons
gene rmtC, expression of wild-type enzyme in Escherichi coli Top10 cells
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gene rmtC, phylogenetic analysis, sequence comparisons
gene rmtD2, phylogenetic analysis, sequence comparisons
gene rmtF encoded on a non-self-transferable plasmid pIP849, cotranscribed with the upstream aac(6')-Ib gene, DNA and amino acid sequence determination, analysis, and comparisons, overview. Genetic structure and phylogenetic tree
gene sgm, phylogenetic analysis, sequence comparisons
gene smr1, phylogenetic analysis, sequence comparisons
introduction of a recombinant version of the Sgm methyltransferase gene from Micromonospora zionensis into an Escherichia coli strain that has a full complement of housekeeping methyltransferases. Analyses of the 16S rRNA shows that the m5C1407-specific housekeeping methyltransferase RsmF (YebU) is outcompeted by Sgm as the resistance methyltransferase gains access to its own m7G1405 target on the 30S ribosomal subunit. A single amino acid change in Sgm, which lowers the level of conferred resistance, reduces the ability of Sgm to interfere with RsmF methylation on the 30S subunit
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sgm is cloned into a yeast expression vector to test whether the prokaryotic methylases can modify the 18S rRNA A-site and thus confer resistance to the aminoglycoside antibiotic G-418. Sgm does not provide resistant phenotypes to yeast cells. Despite all similarities in the antibiotic binding site, methylation by Sgm does not occur in yeast, suggesting that the recognition site for these methylases could be different in 30S and 40S subunits
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E182A
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tobramycin MIC is identical with that of wild-type RmtB
H50A
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tobramycin MIC is drastically reduced compared to wild-type enzyme
H81A
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tobramycin MIC is identical with that of wild-type RmtB. No change in methylation activity compared to wild-type enzyme
K14A
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tobramycin MIC is identical with that of wild-type RmtB. 36% of the methylation activity compared to wild-type enzyme
K174A
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tobramycin MIC is drastically reduced compared to wild-type enzyme. 0.7% of the methylation activity compared to wild-type enzyme
R17A
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tobramycin MIC is identical with that of wild-type RmtB
R181A
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tobramycin MIC is drastically reduced compared to wild-type enzyme
R48A
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tobramycin MIC is identical with that of wild-type RmtB
S83A
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tobramycin MIC is identical with that of wild-type RmtB. 18% of the methylation activity compared to wild-type enzyme
Y56F
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tobramycin MIC is identical with that of wild-type RmtB
D158A
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mutant with drastically increased sensitivity to kanamycin
K54A
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mutant with drastically increased sensitivity to kanamycin
R108A
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mutant with drastically increased sensitivity to kanamycin
R187S
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mutant with drastically increased sensitivity to kanamycin
R187S/G212S
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mutant with strongly reduced activity
R433A
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mutant with drastically increased sensitivity to kanamycin
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
drug development