Information on EC 2.1.1.172 - 16S rRNA (guanine1207-N2)-methyltransferase

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The expected taxonomic range for this enzyme is: Escherichia coli

EC NUMBER
COMMENTARY hide
2.1.1.172
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RECOMMENDED NAME
GeneOntology No.
16S rRNA (guanine1207-N2)-methyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine1207 in 16S rRNA = S-adenosyl-L-homocysteine + N2-methylguanine1207 in 16S rRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:16S rRNA (guanine1207-N2)-methyltransferase
The enzyme reacts well with 30S subunits reconstituted from 16S RNA transcripts and 30S proteins but is almost inactive with the corresponding free RNA [1]. The enzyme specifically methylates guanine1207 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
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 + guanine1207 in 16S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1207 in 16S rRNA
show the reaction diagram
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 + guanine1207 in 16S rRNA
S-adenosyl-L-homocysteine + N2-methylguanine1207 in 16S rRNA
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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close to unit stoichiometry of methylation can be achieved at 0.9 mM Mg2+
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
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2 mM, markedly reduces the level of methylation
Mg2+
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6 mM, markedly reduces the level of methylation
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
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gel filtration
37600
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1 * 37600, calculated from sequence
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
monomer
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1 * 37600, calculated from sequence
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, crystal structure of RsmC refined to 2.1 A resolution, reveals two homologous domains tandemly duplicated within a single polypeptide. Characterization of the function of the individual domains and identification of key residues involved in binding of rRNA and S-adenosyl-L-methionine, and in catalysis. It is discovered that one of the domains is important for the folding of the other. RsmC can be regarded as a model system for functional streamlining of domains accompanied by the development of dependencies concerning folding and stability
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purification and refolding of C-RsmC from inclusion bodies
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
the rsmC gene, cloned into pCA24N vector with a noncleavable N-terminal His6 tag
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Show AA Sequence (2707 entries)
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