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Synonyms
16S rRNA (m1A1408) methyltransferase, 16S rRNA m1A1408 methyltransferase, 16S rRNA:m(1)A1408 methyltransferase, A1408 16S rRNA methyltransferase, KAM, KamB, kanamycin-apramycin resistance methylase, Kmr, m1A1408, Npm,
more
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S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
S-adenosyl-L-methionine + adenosine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenosine1408 in 16S rRNA
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
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sinefungin + adenine1408 in 16S rRNA
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additional information
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S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
NpmA is an adenine N-1 methyltransferase specific for the A1408 position at the A site of 16S rRNA
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S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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-
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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precise location of methylation site
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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-
?
sinefungin + adenine1408 in 16S rRNA
?
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?
sinefungin + adenine1408 in 16S rRNA
?
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?
additional information
?
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the enzyme possesses also methylates 30S subunits with guanine1408
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additional information
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enzyme has low affinity for cosubstrate S-adenosylmethionine
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
S-adenosyl-L-methionine + adenosine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenosine1408 in 16S rRNA
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
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
-
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
-
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
-
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
-
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
-
-
-
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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physiological function
microorganisms that produce aminoglycosides have developed a special mechanism of high level resistance by posttranscriptional methylation of 16S rRNA in the aminoglycoside binding site. N1-methylation of A1408 confers resistance to kanamycin, tobramycin, sisomycin and apramycin, but not to gentamycin. The M1A1408 methylation is carried out by methyltransferases from the Kam family
physiological function
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resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine
physiological function
the introduction of a recombinant plasmid carrying npmA confers on Escherichia coli consistent resistance to both 4,6-disubstituted 2-deoxystreptamines, such as amikacin and gentamicin, and 4,5-disubstituted 2-deoxystreptamines, including neomycin and ribostamycin. 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 A1408
physiological function
expression in Escherichia coli provides high-level resistance to kanamycin and apramycin but not to gentamicin
physiological function
NpmA confers resistance to aminoglycosides. Structure of the bacterial ribosomal decoding A site with an A1408m1A antibiotic-resistance mutation both in the presence and absence of aminoglycosides shows that G418 and paromomycin both possessing a 6'-OH group specifically bind to the mutant A site and disturb its function as a molecular switch in the decoding process. Binding of gentamicin with a 6'-NH3+ group to the mutant A site cannot be observed. Adenine 1408 may change ist conformation during the N1-methylation reaction by NpmA
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D21A
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
E94A
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
K115A
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
R43A/R73A
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
R66A
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
S201A
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the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
S202A
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W113A
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W113F
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the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W203A
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the mutant shows increased binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
W203F
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the mutant shows reduced binding affinity with S-adenosyl-L-methionine compared to the wild type enzyme
E146A
functionally compromised mutant
E184C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S and dissociates upon addition of SAM
E188C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM
K131C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutation blocks 30S-NpmA interaction
S89C
introduction of a residue displaying high modification efficiency with other Cys-reactive reagents for fluorescence assays. Mutant binds to 30S but fails to dissociate upon addition of SAM
E146A
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functionally compromised mutant
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F144A
mutation does not affect enzyme activity
R204A
mutation does not affect enzyme activity
R205A
mutation does not affect enzyme activity
W107A/F144A
loss of activity
W107F
mutant enzyme has a kanamycin MIC indistinguishable from that of wild-type Kmr
W107F/F144A
loss of activity
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Wachino, J.; Shibayama, K.; Kurokawa, H.; Kimura, K.; Yamane, K.; Suzuki, S.; Shibata, N.; Ike, Y.; Arakawa, Y.
Novel plasmid-mediated 16S rRNA m1A1408 methyltransferase, NpmA, found in a clinically isolated Escherichia coli strain resistant to structurally diverse aminoglycosides
Antimicrob. Agents Chemother.
51
4401-4409
2007
Escherichia coli (A8C927), Escherichia coli
brenda
Koscinski, L.; Feder, M.; Bujnicki, J.M.
Identification of a missing sequence and functionally important residues of 16S rRNA:m(1)A1408 methyltransferase KamB that causes bacterial resistance to aminoglycoside antibiotics
Cell Cycle
6
1268-1271
2007
Streptoalloteichus hindustanus (Q2MEY3)
brenda
Holmes, D.J.; Drocourt, D.; Tiraby, G.; Cundliffe, E.
Cloning of an aminoglycoside-resistance-encoding gene, kamC, from Saccharopolyspora hirsuta: comparison with kamB from Streptomyces tenebrarius
Gene
102
19-26
2007
Streptoalloteichus tenebrarius (P25920)
brenda
Beauclerk, A.A.; Cundliffe, E.
Sites of action of two ribosomal RNA methylases responsible for resistance to aminoglycosides
J. Mol. Biol.
193
661-671
1987
Streptomyces tenjimariensis
brenda
Macmaster, R.; Zelinskaya, N.; Savic, M.; Rankin, C.R.; Conn, G.L.
Structural insights into the function of aminoglycoside-resistance A1408 16S rRNA methyltransferases from antibiotic-producing and human pathogenic bacteria
Nucleic Acids Res.
38
7791-7799
2010
Escherichia coli, Streptoalloteichus tenebrarius (A8G927)
brenda
Zelinskaya, N.; Witek, M.A.; Conn, G.L.
The pathogen-derived aminoglycoside resistance 16S rRNA methyltransferase NpmA possesses dual m1A1408/m1G1408 specificity
Antimicrob. Agents Chemother.
59
7862-7865
2015
Escherichia coli (A8C927)
brenda
Witek, M.A.; Conn, G.L.
Expansion of the aminoglycoside-resistance 16S rRNA (m1A1408) methyltransferase family: expression and functional characterization of four hypothetical enzymes of diverse bacterial origin
Biochim. Biophys. Acta
1844
1648-1655
2014
uncultured bacterium, Thermomonospora curvata, Catenulispora acidiphila, Candidatus Arthromitus sp. SFB-mouse, Catenulispora acidiphila DSM 44928, Thermomonospora curvata DSM 43183
brenda
Witek, M.A.; Conn, G.L.
Functional dichotomy in the 16S rRNA (m1A1408) methyltransferase family and control of catalytic activity via a novel tryptophan mediated loop reorganization
Nucleic Acids Res.
44
342-353
2016
Catenulispora acidiphila
brenda
Dunkle, J.A.; Vinal, K.; Desai, P.M.; Zelinskaya, N.; Savic, M.; West, D.M.; Conn, G.L.; Dunham, C.M.
Molecular recognition and modification of the 30S ribosome by the aminoglycoside-resistance methyltransferase NpmA
Proc. Natl. Acad. Sci. USA
111
6275-6280
2014
Escherichia coli (A8C927), Escherichia coli ARS3 (A8C927)
brenda
Savic, M.; Sunita, S.; Zelinskaya, N.; Desai, P.M.; Macmaster, R.; Vinal, K.; Conn, G.L.
30S Subunit-dependent activation of the Sorangium cellulosum So ce56 aminoglycoside resistance-conferring 16S rRNA methyltransferase Kmr
Antimicrob. Agents Chemother.
59
2807-2816
2015
Sorangium cellulosum (B2L3G9)
brenda
Vinal, K.; Conn, G.
Substrate recognition and modification by a pathogen-associated aminoglycoside resistance 16S rRNA methyltransferase
Antimicrob. Agents Chemother.
61
e00077
2017
Escherichia coli (A8C927)
brenda
Kanazawa, H.; Baba, F.; Koganei, M.; Kondo, J.
A structural basis for the antibiotic resistance conferred by an N1-methylation of A1408 in 16S rRNA
Nucleic Acids Res.
45
12529-12535
2017
Escherichia coli (A8C927)
brenda
Husain, N.; Tulsian, N.K.; Chien, W.L.; Suresh, S.; Anand, G.S.; Sivaraman, J.
Ligand-mediated changes in conformational dynamics of NpmA implications for ribosomal interactions
Sci. Rep.
6
37061
2016
Escherichia coli (A8C927)
brenda