Information on EC 2.1.1.171 - 16S rRNA (guanine966-N2)-methyltransferase

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The enzyme appears in viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.1.1.171
-
RECOMMENDED NAME
GeneOntology No.
16S rRNA (guanine966-N2)-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine966 in 16S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine966 in 16S rRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine966-N2)-methyltransferase
The enzyme efficiently methylates guanine966 of the assembled 30S subunits in vitro. Protein-free 16S rRNA is not a substrate for RsmD [1]. The enzyme specifically methylates guanine966 at N2 in 16S rRNA.
CAS REGISTRY NUMBER
COMMENTARY hide
50812-26-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene rv2966c
P95128
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
P95128;
structural similarities with other methyltransferases are limited to the core S-adenosyl-L-methionine domain but not the target recognition domain
malfunction
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 + guanine966 in 16S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine966 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine966 in 30S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine966 in 30S rRNA
show the reaction diagram
additional information
?
-
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 + guanine966 in 16S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine966 in 16S rRNA
show the reaction diagram
S-adenosyl-L-methionine + guanine966 in 30S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine966 in 30S rRNA
show the reaction diagram
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RsmD acts late in the assembly process and is able to modify a completely assembled 30S subunit
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-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
additional information
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sinefungin is an unreactive S-adenosyl-L-methionine analogue
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
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RsmD methyltransferase kinetics, multiple turnover reaction, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
P95128;
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
P95128;
assay at
PDB
SCOP
CATH
UNIPROT
ORGANISM
A0A045IDU3
Mycobacterium tuberculosis;
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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based on a comprehensive bioinformatic analysis of m2G methyltransferases it is inferred that the prokaryotic RsmC and RsmD methyltransferases are pseudodimers. The C-terminal catalytic domain is closely related to the structurally characterized Mj0882 protein, while the N-terminal domain lacks the cofactor-binding and catalytic side-chains
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
vapor diffusion method in hanging drops, structure determined and refined to 2.05 A
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purified recombinant Rv2966c, hanging drop vapour diffusion method, mixing of 0.004 ml of 17 mg/ml Rv2966c in 10 mM potassium phosphate buffer, pH 7.4, 5 mM EDTA, 10% v/v glycerol, 0.1% v/v 2-mercaptoethanol, 50 mM NaCl, 0.1 mM S-adenosyl-L-methionine, with 0.002 ml of reservoir solution containing 100 mM Tris-HCl, pH 7.4, 3.0 M potassium acetate at 24 °C, 2-3 days, X-ray diffraction structure determination and analysis at 1.9 A resolution, molecular replacement
P95128;
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant Rv2966c with His10-Smt3 fusion at the N-terminus from Escherichia coli strain BL21 (DE3) by nickel affinity and anion exchange chromatography
P95128;
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene rsmD, complementation of rsmD-deleted Escherichia coli KL16DELTArsmD cells, expression of Rv2966c with His10-Smt3 fusion at the N-terminus from plasmid pMTase1 in Escherichia coli strain BL21 (DE3)
P95128;
gene rsmD, expression of N-terminally His6-tagged RsmD
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D58A
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site-directed mutagenesis, the mutant shows increased Km toward the 30S subunit by two orders of magnitude with only a marginal effect on kcat compared to the wild-type enzyme. The mutation decreases the enthalpic contribution to SAM binding, paralleled by an increase in the entropic contribution
D58A/P128A/P129A
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site-directed mutagenesis, the mutant shows increased Km toward the 30S subunit by two orders of magnitude with only a marginal effect on kcat compared to the wild-type enzyme
F130S
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site-directed mutagenesis
P128A/P129A
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site-directed mutagenesis, the mutation decreases the enthalpic contribution to SAM binding, paralleled by an increase in the entropic contribution,
P128A/P129A/F130S
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site-directed mutagenesis, inactive mutant
additional information
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knockout of the rsmD gene and complementation by point mutants, except for mutant P128A/P129A/F130S, overview
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