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

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)

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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
gene rv2966c
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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
-
RsmD acts late in the assembly process and is able to modify a completely assembled 30S subunit
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
additional information
-
sinefungin is an unreactive S-adenosyl-L-methionine analogue
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
-
RsmD methyltransferase kinetics, multiple turnover reaction, overview
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
-
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
-
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
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
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)
gene rsmD, expression of N-terminally His6-tagged RsmD
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D58A
-
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
-
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
-
site-directed mutagenesis
P128A/P129A
-
site-directed mutagenesis, the mutation decreases the enthalpic contribution to SAM binding, paralleled by an increase in the entropic contribution,
P128A/P129A/F130S
-
site-directed mutagenesis, inactive mutant
additional information
-
knockout of the rsmD gene and complementation by point mutants, except for mutant P128A/P129A/F130S, overview
Show AA Sequence (3153 entries)
Please use the Sequence Search for a certain query.