Information on EC 2.1.1.166 - 23S rRNA (uridine2552-2'-O)-methyltransferase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.1.1.166
-
RECOMMENDED NAME
GeneOntology No.
23S rRNA (uridine2552-2'-O)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + uridine2552 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
show the reaction diagram
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O)-methyltransferase
The enzyme catalyses the 2'-O-methylation of the universally conserved U2552 in the A loop of 23S rRNA [3].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
-
absence of functional RrmJ causes the cellular accumulation of the individual ribosomal subunits at the expense of the functional 70S ribosomes
physiological function
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 + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S 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 + uridine2552 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine2552 in 23S rRNA
show the reaction diagram
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0037
S-adenosyl-L-methionine
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pH 7.5, 37C
additional information
additional information
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.001
S-adenosyl-L-methionine
Escherichia coli
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pH 7.5, 37C
additional information
additional information
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50 - 60
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50C: about 75% of maximal activity, 60C: about 95% of maximal activity
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
transcripts are abundant
Manually annotated by BRENDA team
transcripts are abundant
Manually annotated by BRENDA team
transcripts are abundant
Manually annotated by BRENDA team
transcripts are abundant
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24700
x * 24700, calculated
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
x * 24700, calculated
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structure of the FtsJ protein at 1.5 A resolution in complex with its cofactor S-adenosyl-L-methionine
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identification of a conserved tetrad K-D-K-H in the family of small nucleolar RNA-guided ribose 2'-O-methyltransferases related to fibrillarin. The corresponding functional groups of putative catalytic tetrads of Escherichia coli RrmJ and Methanococcus jannaschii Mj0697 may be superimposed in space. The invariant residues K164 in RrmJ and K179 in Mj0697 are observed in two distinct locations in the primary sequence, suggesting an interesting case of migration of the conserved side chain within the framework of the active site
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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RrmJ is a thermostable heat shock protein
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a chimera protein of RrmJ fused to a chitin-binding domain was purified by affinity chromatography on a chitin affinity column
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D124A
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the mutant D124A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
D136N
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D136N mutant strain accumulates larger amounts of 30S and 50S ribosomal subunits than wild-type strains under nonstringent salt conditions, and has a significant amount of 40S ribosomal particles under stringent salt conditions; mutation leads to slight decrease in kcat value
D20A
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mutation leads to slight decrease in kcat value
D83A
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the mutant D83A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
E199A
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the RrmJ deletion strains expressing the E199A variant protein shows only slight growth defects, indicating that the residue is not as important in the catalytic mechanism
F166A
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decrease in S-adenosyl-L-methionine binding affinity and/or the presence of a certain amount of an inactive yet stably folded RrmJ mutant species
F37A/L39A
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mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile
K164A
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the mutant D83A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
K38A
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the mutant D83A is unable to rescue the growth defect of the rrmJ deletion strain, indicating that this mutation causes the inactivation of RrmJ in vivo
Q67A/Y68A
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mutant strain shows ribosome profiles that are indistinguishable from wild-type ribosome profile
R32A/R34A
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R32A/R34A mutant strain accumulates larger amounts of 30S and 50S ribosomal subunits than wild-type strains under nonstringent salt conditions, and has a significant amount of 40S ribosomal particles under stringent salt conditions
Y201A
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the RrmJ deletion strains expressing the Y201A variant protein shows only slight growth defects, indicating that the residue is not as important in the catalytic mechanism
additional information
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