Information on EC 2.1.1.205 - tRNA (cytidine32/guanosine34-2'-O)-methyltransferase

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The expected taxonomic range for this enzyme is: Saccharomyces cerevisiae

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EC NUMBER
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2.1.1.205
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RECOMMENDED NAME
GeneOntology No.
tRNA (cytidine32/guanosine34-2'-O)-methyltransferase
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REACTION
REACTION DIAGRAM
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ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytidine32/guanosine34 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
tRNA methylation (yeast)
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytidine32/guanosine34-2'-O)-methyltransferase
The enzyme from Saccharomyces cerevisiae catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe, tRNATrp and, possibly, tRNALeu.
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
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LITERATURE
malfunction
a trm7DELTA strain, which is viable but grows slowly, translation is impaired. Protein synthesis is reduced to 30% in the deleted strain, compared with an isogenic wild-type strain. The formation of 2'-O-methylcytidine32 and guanosine34 is abolished in the trm7DELTA strain
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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 + cytidine32/guanosine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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 + cytidine32/guanosine34 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32/2'-O-methylguanosine34 in tRNA
show the reaction diagram
P38238
the enzyme catalyses the formation of 2'-O-methylnucleotides at positions 32 and 34 of the yeast tRNAPhe, tRNATrp and, possibly, tRNALeu
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LOCALIZATION
ORGANISM
UNIPROT
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GeneOntology No.
LITERATURE
SOURCE
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
wild-type and mutant strain D49A
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ENGINEERING
ORGANISM
UNIPROT
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LITERATURE
D49A
abolishes almost completely the formation of 2'-O-methylcytidine32, no activity is detected for guanine34
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Show AA Sequence (1183 entries)
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LINKS TO OTHER DATABASES (specific for EC-Number 2.1.1.205)
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)