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Information on EC 2.1.1.180 - 16S rRNA (adenine1408-N1)-methyltransferase
for references in articles please use BRENDA:EC2.1.1.180
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EC Tree 2 Transferases
2.1 Transferring one-carbon groups
2.1.1 Methyltransferases
2.1.1.180 16S rRNA (adenine1408-N1)-methyltransferase
IUBMB Comments
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 .
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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adenine1408 in 16S rRNA
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N1-methyladenine1408 in 16S rRNA
Synonyms
16S rRNA (m1A1408) methyltransferase, 16S rRNA m1A1408 methyltransferase, 16S rRNA methyltransferase, 16S rRNA:m(1)A1408 methyltransferase, A1408 16S rRNA methyltransferase, DTY44_23675, KAM, KamB, kanamycin-apramycin resistance methylase, Kmr, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
16S rRNA (m1A1408) methyltransferase
16S rRNA methyltransferase
A1408 16S rRNA methyltransferase
KAM
KamB
m1A1408
NpmA
plasmid-mediated 16S rRNA methyltransferase A
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + adenine1408 in 16S rRNA = S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
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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].
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: NpmA is an adenine N-1 methyltransferase specific for the A1408 position at the A site of 16S rRNA
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: precise location of methylation site
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
sinefungin + adenine1408 in 16S rRNA
?
Substrates: -
Products: -
Products: -
?
additional information
?
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Substrates: the enzyme possesses also methylates 30S subunits with guanine1408
Products: -
Products: -
?
additional information
?
-
Substrates: NpmB1 requires a structural change of the b6/7 linker in order to bind to 16S rRNA
Products: -
Products: -
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additional information
?
-
Substrates: enzyme has low affinity for cosubstrate S-adenosylmethionine
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Substrates: 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
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
S-adenosyl-L-methionine + adenine1408 in 16S rRNA
S-adenosyl-L-homocysteine + N1-methyladenine1408 in 16S rRNA
-
Substrates: -
Products: -
Products: -
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-adenosyl-L-methionine
cofactor SAM binds to NpmB1 in a manner similar to that of the other A1408 16S rRNA methyltransferases. The cofactor-binding site consists of residues D30, G32, N38, D55, P56, A87, E88, L104, T109, and S195, binding mechanism, overview
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
not inhibitory: S-adenosylhomocysteine in up to 1000fold excess over S-adenosylmethionine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
physiological function
additional information
structure-function analysis of enzyme NpmB1. NpmB1 requires a structural change of the b6/7 linker in order to bind to 16S rRNA
evolution
NpmB1 and NpmB2 is the second group of acquired pan-aminoglycoside resistance 16S rRNA methyltransferases, besides NpmA. NpmB1 possesses 40% amino acid identity with NpmA1. Phylogenetic analysis of NpmB1 and NpmB2, its single-amino-acid variant, reveals that the encoding gene was likely acquired by Escherichia coli from a soil bacterium, as was the gene encoding NpmA1. NpmB likely originated in Acidobacteria. NpmB1 and NpmB2 consist of 217 amino acids, and only one amino acid substitution is identified in their sequences at position 21, arginine for NpmB1 and cysteine for NpmB2. Comparison of the target recognition sites and 16S rRNA-binding sites among A1408 16S rRNA methyltransferases, overview
evolution
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gene npmC has a high level of similarity (91.5%) with npmA and up to 92.7% similarity at amino acidic level. Analysis of the npmC gene background reveals that its genetic context is associated with different insertion sequences that can mobilise the gene. Similarities in the genetic context between npmC and npmA indicate that they share a common ancestor. The immediate genetic context of this methyltransferase indicates a high relationship to the Eubacteriales order. NpmC is a pan-aminoglycoside 16S rRNA methyltransferase. Bacterial reservoir of NpmC, overview
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
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
-
resistance to kanamycin plus apramycin results from conversion of residue adenine1408 to 1-methyladenine
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
physiological function
posttranslational methylation of the A site of 16S rRNA at position A1408 leads to pan-aminoglycoside resistance encompassing both 4,5- and 4,6-disubstituted 2-deoxystreptamine (DOS) aminoglycosides. NpmB1 confers resistance to all clinically relevant aminoglycosides, including 4,5-DOS agents through A1408 methylation of 16S rRNA, Tthe MICs of aminoglycosides against the NpmB1-producing strain are at least 16fold higher than that of the control strain harboring the pUC19 plasmid
physiological function
posttranslational methylation of the A site of 16S rRNA at position A1408 leads to pan-aminoglycoside resistance encompassing both 4,5- and 4,6-disubstituted 2-deoxystreptamine (DOS) aminoglycosides. NpmB1 confers resistance to all clinically relevant aminoglycosides, including 4,5-DOS agents
physiological function
-
the enzyme expressed in Escherichia coli causes methylation of A1408 and the displacement of the methylation of C1407 by RsmF
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). NPMA_ECOLX
219
0
24887
Swiss-Prot
other Location (Reliability: 1)
KAMB_STRSD
Streptoalloteichus tenebrarius (strain ATCC 17920 / DSM 40477 / JCM 4838 / CBS 697.72 / NBRC 16177 / NCIMB 11028 / NRRL B-12390 / A12253. 1 / ISP 5477)
215
0
23664
Swiss-Prot
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30000
additional information
gene sequence is used for protein structure prediction, model of ShKamB
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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electrostatic interactions made by the NpmA beta2/3 linker collectively are critical for docking of NpmA on a conserved 16S rRNA tertiary surface. Other NpmA regions (beta5/beta6 and beta6/beta7 linkers) contain several residues critical for optimal positioning of A1408 but are largely dispensable for 30S binding. In a model for NpmA action, 30S binding and adoption of a catalytically competent state are distinct: docking on 16S rRNA via the beta2/3 linker necessarily precedes functionally critical 30S substrate-driven conformational changes elsewhere in NpmA
H/D exchange mass spectrometry of apo NpmA in the presence and absence of SAM/SAH. Ligand binding results in time-dependent differences in deuterium exchange not only at the ligand-binding pocket (residues D25-D55 and A86-E112) but also in distal regions (F62-F82 and Y113-S144) of NpmA
high-resolution crystal structures of NpmA from Escherichia coli is determined at 1.69 A
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purified recombinant His-tagged enzyme, X-ray diffraction structure determination and structure analysis of NpmB1 at 1.5 A resolution, molecular replacement method using the coordinate (PDB ID 4RWZ) as the search model
apo-enzyme, to 1.8 A resolution, by molecular replacement. Kmr possesses a canonical S-adenosylmethionine binding pocket but with reduced sensitivity to mutation
high-resolution crystal structures of KamB from Streptoalloteichus tenebrarius is determined at 1.69 A
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
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
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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
-
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
-
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
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
W107F
mutant enzyme has a kanamycin MIC indistinguishable from that of wild-type Kmr
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Escherichia coli strain Rosetta2 (DE3) by nickel affinity chromatography
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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
gene encoding NpmB1, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta2 (DE3)
gene encoding NpmB2, DNA and amino acid sequence determination and analysis, sequence comparisons and phylogenetic analysis
gene npmC, recombinant expression of the enzyme in Escherichia coli strain HST08 results in a high level of resistance to 4,5-disubstituted 2-deoxystreptamine (2-DOS) and 4-monosubstituted 2-DOS aminoglycosides, as well as moderate resistance to 4,6-disusbstituted 2-DOS aminoglycosides, including the last resort aminoglycoside, plazomicin. The methyltransferase is not expressed from its native promoter or in a related species, which may account for the observed differences in resistance
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
development of a fluorescence-based binding assay for 30S-NpmA interaction
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Streptoalloteichus tenebrarius (A8G927), Escherichia coli
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
Candidatus Arthromitus sp. SFB-mouse, Catenulispora acidiphila, Catenulispora acidiphila DSM 44928, Thermomonospora curvata, Thermomonospora curvata DSM 43183, uncultured bacterium
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
Kawai, A.; Suzuki, M.; Tsukamoto, K.; Minato, Y.; Doi, Y.
Functional and structural characterization of acquired 16S rRNA methyltransferase NpmB1 conferring pan-aminoglycoside resistance
Antimicrob. Agents Chemother.
65
e0100921
2021
Escherichia coli (A0A8J0PCK0)
brenda
Matamoros, B.R.; Serna, C.; Wedel, E.; Montero, N.; Kirpekar, F.; Gonzalez-Zorn, B.
NpmC - a novel A1408 16S rRNA methyltransferase in the gut of humans and animals
Int. J. Antimicrob. Agents
65
107382
2024
uncultured bacterium
brenda
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