Information on EC 2.1.1.185 - 23S rRNA (guanosine2251-2'-O)-methyltransferase

for references in articles please use BRENDA:EC2.1.1.185
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The expected taxonomic range for this enzyme is: Escherichia coli

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EC NUMBER
COMMENTARY hide
2.1.1.185
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RECOMMENDED NAME
GeneOntology No.
23S rRNA (guanosine2251-2'-O)-methyltransferase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanosine2251 in 23S rRNA = S-adenosyl-L-homocysteine + 2'-O-methylguanosine2251 in 23S rRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:23S rRNA (guanosine2251-2'-O)-methyltransferase
The enzyme catalyses the methylation of guanosine2251, a modification conserved in the peptidyltransferase domain of 23S rRNA.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
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a DELTArlmB mutant lacks 2'-O-methylguanosine in 23S rRNA, the mutant does not show any ribosome assembly defects and is not outgrown by a wild-type strain even after 120 cell mass doublings
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
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LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
S-adenosyl-L-methionine + guanosine2251 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine2251 in 23S rRNA
show the reaction diagram
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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 + guanosine2251 in 23S rRNA
S-adenosyl-L-homocysteine + 2'-O-methylguanosine2251 in 23S rRNA
show the reaction diagram
P63177
the enzyme is essential for formation of Gm2251 in 23S rRNA but not for ribosome maturation in Escherichia coli
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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RlmB displays a AdoMet binding site located in the divergent C-terminal half of the catalytic domain
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
29000
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2 * 29000
60000
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gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 29000
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
sparse matrix screening by hanging drop vapor diffusion, crystal structure of this 2'O-methyltransferase has been determined at 2.5 A resolution
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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a DELTArlmB mutant lacks 2'-O-methylguanosine in 23S rRNA, the mutant does not show any ribosome assembly defects and is not outgrown by a wild-type strain even after 120 cell mass doublings
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.185)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)