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Information on EC 2.1.1.172 - 16S rRNA (guanine1207-N2)-methyltransferase and Organism(s) Escherichia coli and UniProt Accession P39406

for references in articles please use BRENDA:EC2.1.1.172
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IUBMB Comments
The enzyme reacts well with 30S subunits reconstituted from 16S RNA transcripts and 30S proteins but is almost inactive with the corresponding free RNA . The enzyme specifically methylates guanine1207 at N2 in 16S rRNA.
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This record set is specific for:
Escherichia coli
UNIPROT: P39406
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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
+
guanine1207 in 16S rRNA
=
S-adenosyl-L-homocysteine
+
N2-methylguanine1207 in 16S rRNA
+
guanine1207 in 16S rRNA
=
+
N2-methylguanine1207 in 16S rRNA
Synonyms
16s rrna:m2g966 mtase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
16 S RNA m2G1207 methyltransferase
-
16S rRNA:(guanine-N2) methyltransferase
-
16S rRNA:m2G1207 MTase
-
16S rRNA:m2G966 MTase
-
ribosomal RNA small subunit methyltransferase C
-
RNA:(guanine-N2) methyltransferase RsmC
-
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
-
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 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 + 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+
close to unit stoichiometry of methylation can be achieved at 0.9 mM Mg2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
2 mM, markedly reduces the level of methylation
Mg2+
6 mM, markedly reduces the level of methylation
KNHDWGV
-
7-mer peptide that binds to the second strand of 16S h34 RNA. Binding of the peptide alters RNA structure and inhibits the binding of the ribosomal RNA small subunit methyltransferase C. The addition of the peptide also increases the lag phase of bacterial growth
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
gel filtration
37600
1 * 37600, calculated from sequence
SUBUNIT
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
monomer
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification and refolding of C-RsmC from inclusion bodies
recombinant protein
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
the rsmC gene, cloned into pCA24N vector with a noncleavable N-terminal His6 tag
expression in Escherichia coli
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bujnicki, J.M.
Phylogenomic analysis of 16S rRNA:(guanine-N2) methyltransferases suggests new family members and reveals highly conserved motifs and a domain structure similar to other nucleic acid amino-methyltransferases
FASEB J.
14
2365-2368
2000
Escherichia coli (P39406), Escherichia coli
Manually annotated by BRENDA team
Tscherne, J.S.; Nurse, K.; Popienick, P.; Ofengand, J.
Purification, cloning, and characterization of the 16S RNA m2G1207 methyltransferase from Escherichia coli
J. Biol. Chem.
274
924-929
1999
Escherichia coli (P39406), Escherichia coli
Manually annotated by BRENDA team
Sergiev, P.V.; Bogdanov, A.A.; Dontsova, O.A.
Ribosomal RNA guanine-(N2)-methyltransferases and their targets
Nucleic Acids Res.
35
2295-2301
2007
Escherichia coli (P39406)
Manually annotated by BRENDA team
Bujnicki, J.M.
Rychlewski. L.: RNA:(guanine-N2) methyltransferases RsmC/RsmD and their homologs revisited--bioinformatic analysis and prediction of the active site based on the uncharacterized Mj0882 protein structure
BMC Bioinformatics
3
10
2002
Escherichia coli (P39406)
Manually annotated by BRENDA team
Sunita, S.; Purta, E.; Durawa, M.; Tkaczuk, K.L.; Swaathi, J.; Bujnicki, J.M.; Sivaraman, J.
Functional specialization of domains tandemly duplicated within 16S rRNA methyltransferase RsmC
Nucleic Acids Res.
35
4264-4274
2007
Escherichia coli (P39406)
Manually annotated by BRENDA team
Gc, K.; To, D.; Jayalath, K.; Abeysirigunawardena, S.
Discovery of a novel small molecular peptide that disrupts helix 34 of bacterial ribosomal RNA
RSC Adv.
9
40268-40276
2019
Escherichia coli
-
Manually annotated by BRENDA team