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Information on EC 2.1.1.213 - tRNA (guanine10-N2)-dimethyltransferase and Organism(s) Pyrococcus abyssi and UniProt Accession Q9UY84

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     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.213 tRNA (guanine10-N2)-dimethyltransferase
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This record set is specific for:
Pyrococcus abyssi
UNIPROT: Q9UY84 not found.
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  • 2.1.1.213
  • carotenoid
  • dioxygenase
  • thiouridine
  • acyclic
  • thump
The taxonomic range for the selected organisms is: Pyrococcus abyssi
The expected taxonomic range for this enzyme is: Archaea, Bacteria
Synonyms
pab1283, trna:m2(2)g10 methyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N(2),N(2)-dimethylguanosine tRNA methyltransferase
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PabTrm-m2 2G10 enzyme
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-
tRNA:m2(2)G10 methyltransferase
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-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + guanine10 in tRNA = S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
(1a)
S-adenosyl-L-methionine + N2-methylguanine10 in tRNA = S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
(1b)
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine10-N2)-dimethyltransferase
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2 S-adenosyl-L-methionine + guanine10 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
depending on the experimental conditions used, as well as the tRNA substrate tested, the enzymatic reaction leads to the formation of either N2-methyl or N2-dimethylguanosine. N2-Dimethylguanine10 accumulates during incubation at 50°C, whereas the formation of N2-methylguanine10 appears to be a transient intermediate. At 30°C, N2-dimethylguanine10 is efficiently formed, whereas the formation of N2-methylguanine10 is considerably slowed compared with that at higher temperatures
-
-
?
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
depending on the experimental conditions used, as well as the tRNA substrate tested, the enzymatic reaction leads to the formation of either N2-methyl or N2-dimethylguanosine. N2-Dimethylguanine10 accumulates during incubation at 50°C, whereas the formation of N2-methylguanine10 appears to be a transient intermediate. At 30°C, N2-dimethylguanine10 is efficiently formed, whereas the formation of N2-methylguanine10 is considerably slowed compared with that at higher temperatures
-
-
?
2 S-adenosyl-L-methionine + guanine10 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
-
identity elements required for the efficient formation of N2-dimethylguanine10: uracil25 and a V-loop of four nucleotides are major determinants for the formation of N2-dimethylguanine10, whereas the identity of the 13-22 base-pair clearly influences the rate of N2-dimethylguanine10 formation. The integrity of the T-arm prolonged with the amino acid acceptor stem is an important structural element for the dimethylation step catalysed by PabTrm-m2 2G10 enzyme
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-
?
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
model for a potential binding mode for the THUMP domain, which may be common to various RNA modification enzymes that specifically modify nucleotides in the 3D-core of the tRNA molecule
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-
?
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
2 S-adenosyl-L-methionine + guanine10 in tRNA
2 S-adenosyl-L-homocysteine + N2-dimethylguanine10 in tRNA
show the reaction diagram
depending on the experimental conditions used, as well as the tRNA substrate tested, the enzymatic reaction leads to the formation of either N2-methyl or N2-dimethylguanosine. N2-Dimethylguanine10 accumulates during incubation at 50°C, whereas the formation of N2-methylguanine10 appears to be a transient intermediate. At 30°C, N2-dimethylguanine10 is efficiently formed, whereas the formation of N2-methylguanine10 is considerably slowed compared with that at higher temperatures
-
-
?
S-adenosyl-L-methionine + guanine10 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine10 in tRNA
show the reaction diagram
depending on the experimental conditions used, as well as the tRNA substrate tested, the enzymatic reaction leads to the formation of either N2-methyl or N2-dimethylguanosine. N2-Dimethylguanine10 accumulates during incubation at 50°C, whereas the formation of N2-methylguanine10 appears to be a transient intermediate. At 30°C, N2-dimethylguanine10 is efficiently formed, whereas the formation of N2-methylguanine10 is considerably slowed compared with that at higher temperatures
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mg2+
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yield of G10 dimethylation in transcript of tRNAAsp greatly depends on the presence of Mg2+, with an optimal concentration around 5 mM. In contrast, formation of N2-monomethylguanine10 is not strictly dependent on the presence of Mg2+
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain GE5
SwissProt
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
39000
1 * 39000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 39000, SDS-PAGE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
102
midpoint melting temperature
86
noticeable unfolding of the protein (more than 5%) is detected above 86°C
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purification of recombinant THUMPalpha module
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression in Escherichia coli
construction of a N-terminal 6His-tagged THUMPalpha overexpressing plasmid, expression in Escherichia coli. THUMP i.e. (THioUridine synthases, RNA Methyltransferases and Pseudo-uridine synthases)-containing N-terminal domain
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Armengaud, J.; Urbonavicius, J.; Fernandez, B.; Chaussinand, G.; Bujnicki, J.M.; Grosjean, H.
N2-Methylation of guanosine at position 10 in tRNA is catalyzed by a THUMP domain-containing, S-adenosylmethionine-dependent methyltransferase, conserved in archaea and eukaryota
J. Biol. Chem.
279
37142-37152
2004
Pyrococcus abyssi (Q9UY84)
Manually annotated by BRENDA team
Urbonavicius, J.; Armengaud, J.; Grosjean, H.
Identity elements required for enzymatic formation of N2,N2-dimethylguanosine from N2-monomethylated derivative and its possible role in avoiding alternative conformations in archaeal tRNA
J. Mol. Biol.
357
387-399
2006
Pyrococcus abyssi
Manually annotated by BRENDA team
Gabant, G.; Auxilien, S.; Tuszynska, I.; Locard, M.; Gajda, M.J.; Chaussinand, G.; Fernandez, B.; Dedieu, A.; Grosjean, H.; Golinelli-Pimpaneau, B.; Bujnicki, J.M.; Armengaud, J.
THUMP from archaeal tRNA:m22G10 methyltransferase, a genuine autonomously folding domain
Nucleic Acids Res.
34
2483-2494
2006
Pyrococcus abyssi
Manually annotated by BRENDA team