Information on EC 2.1.1.200 - tRNA (cytidine32/uridine32-2'-O)-methyltransferase

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

EC NUMBER
COMMENTARY hide
2.1.1.200
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RECOMMENDED NAME
GeneOntology No.
tRNA (cytidine32/uridine32-2'-O)-methyltransferase
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytidine32 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
show the reaction diagram
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S-adenosyl-L-methionine + uridine32 in tRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
show the reaction diagram
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (cytidine32/uridine32-2'-O)-methyltransferase
In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of 2'-O-methylcytidine32 in tRNA. No methylation of cytosine34 in tRNALeu(CAA). In vitro the enzyme 2-O-methylates cytidine32 of tRNASer1 and uridine32 of tRNAGln2.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
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 + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet1(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet1(CAU)
show the reaction diagram
S-adenosyl-L-methionine + nucleoside32 in EctRNAfMet2(CAU)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAfMet2(CAU)
show the reaction diagram
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln1(UUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln1(UUG)
show the reaction diagram
S-adenosyl-L-methionine + nucleoside32 in EctRNAGln2(CUG)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNAGln2(CUG)
show the reaction diagram
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?
S-adenosyl-L-methionine + nucleoside32 in EctRNASer1(UGA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNASer1(UGA)
show the reaction diagram
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?
S-adenosyl-L-methionine + nucleoside32 in EctRNATrp1(CCA)
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in EctRNATrp1(CCA)
show the reaction diagram
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-
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?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
show the reaction diagram
additional information
?
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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 + cytidine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylcytidine32 in tRNA
show the reaction diagram
P0AE01
presence of 2'-O-methylated cytidine at position 32 in tRNAfMet1(CAU), tRNAfMet2(CAU), tRNASer1(UGA), and tRNATrp1(CCA). In Escherichia coli YfhQ is the only methyltransferase responsible for the formation of Cm32 in tRNA
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?
S-adenosyl-L-methionine + nucleoside32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methylnucleoside32 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + uridine32 in tRNA
S-adenosyl-L-homocysteine + 2'-O-methyluridine32 in tRNA
show the reaction diagram
P0AE01
presence of 2'-O-methylated uridine in position 32 of the anticodon loop in tRNAGln1(UUG) and tRNAGln2(CUG)
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?
additional information
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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required
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00067
nucleoside32 in EctRNAfMet1(CAU)
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pH 9.0, 37C, recombinant wild-type enzyme
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0.00081
nucleoside32 in EctRNAfMet2(CAU)
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pH 9.0, 37C, recombinant wild-type enzyme
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0.00988
nucleoside32 in EctRNAGln1(UUG)
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pH 9.0, 37C, recombinant wild-type enzyme
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0.00579
nucleoside32 in EctRNAGln2(CUG)
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pH 9.0, 37C, recombinant wild-type enzyme
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0.01182
nucleoside32 in EctRNASer1(UGA)
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pH 9.0, 37C, recombinant wild-type enzyme
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0.00094
nucleoside32 in EctRNATrp1(CCA)
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pH 9.0, 37C, recombinant wild-type enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.0253
nucleoside32 in EctRNAfMet1(CAU)
Escherichia coli
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pH 9.0, 37C, recombinant wild-type enzyme
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0.0237
nucleoside32 in EctRNAfMet2(CAU)
Escherichia coli
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pH 9.0, 37C, recombinant wild-type enzyme
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0.02
nucleoside32 in EctRNAGln1(UUG)
Escherichia coli
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pH 9.0, 37C, recombinant wild-type enzyme
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0.0235
nucleoside32 in EctRNAGln2(CUG)
Escherichia coli
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pH 9.0, 37C, recombinant wild-type enzyme
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0.0383
nucleoside32 in EctRNASer1(UGA)
Escherichia coli
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pH 9.0, 37C, recombinant wild-type enzyme
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0.0218
nucleoside32 in EctRNATrp1(CCA)
Escherichia coli
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pH 9.0, 37C, recombinant wild-type enzyme
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
9
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assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
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gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
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2 * 29168, calculated from sequence; 2 * 30000, SDS-PAGE in presence of 7.5% 2-mercaptoethanol
additional information
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant C-terminally His6-tagged wild-type enzyme, hanging drop vapour diffusion method, mixing of 10 mg/ml of protein 20 mM Tris-HCl, pH 7.5, 100 mM NaCl, 10 mM MgCl2, and 2 mM S-adenosyl-L-homocysteine, with 3.6 M NaCl and 0.1 M HEPES, pH 8.2, 20C, 2 months, X-ray diffraction structure determination and analysis, full-length EcTrmJ forms an unusual dimer in the asymmetric unit, with both the catalytic SPOUT domain and C-terminal extension forming separate dimeric associations in the crystal structure, molecular replacement
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crystal structure of the catalytic domain
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged wild-type enzyme and deletion mutants from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression of C-terminally His6-tagged wild-type enzyme and deletion mutants in Escherichia coli strain BL21(DE3)
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E225A
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site-directed mutagenesis, inactive mutant
F199A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
G231A
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site-directed mutagenesis, inactive mutant
I228A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
L229A
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site-directed mutagenesis, inactive mutant
E225A
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site-directed mutagenesis, inactive mutant
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F199A
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site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
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G231A
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site-directed mutagenesis, inactive mutant
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L229A
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site-directed mutagenesis, inactive mutant
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additional information
Show AA Sequence (4585 entries)
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