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Information on EC 2.1.1.180 - 16S rRNA (adenine1408-N1)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession A8C927

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EC Tree
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 .
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This record set is specific for:
Escherichia coli
UNIPROT: A8C927
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Word Map
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  • 2.1.1.180
  • trna
  • microcephaly
  • disability
  • intellectual
  • spout
  • purine
  • aminoglycoside
  • stature
  • guanosine
  • exome
  • eukaryal
  • circumference
  • monogenic
  • post-transcriptionally
  • puberty
  • guanosine-specific
  • islet
  • cdkal1
  • methylthiotransferase
  • adenosine-specific
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Archaea
Reaction Schemes
hide
S-adenosyl-L-methionine
+
adenine1408 in 16S rRNA
=
S-adenosyl-L-homocysteine
+
N1-methyladenine1408 in 16S rRNA
+
adenine1408 in 16S rRNA
=
+
N1-methyladenine1408 in 16S rRNA
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
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16S rRNA m1A1408 methyltransferase
-
plasmid-mediated 16S rRNA methyltransferase A
-
A1408 16S rRNA methyltransferase
-
-
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].
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 SUBSTRATE
NATURAL 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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
NPMA_ECOLX
219
0
24887
Swiss-Prot
-
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
in complex with the 30S ribosome subunit and sinefungin
high-resolution crystal structures of NpmA from Escherichia coli is determined at 1.69 A
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
His-tagged NpmA
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
analysis
development of a fluorescence-based binding assay for 30S-NpmA interaction
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
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team
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)
Manually annotated by BRENDA team