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Information on EC 2.1.1.215 - tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase and Organism(s) Aquifex aeolicus and UniProt Accession O67010
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2.1.1.215 tRNA (guanine26-N2/guanine27-N2)-dimethyltransferaseIUBMB Comments
The enzyme from Aquifex aeolicus is similar to the TRM1 methyltransferases of archaea and eukarya (see EC 2.1.1.216, tRNA (guanine26-N2)-dimethyltransferase). However, it catalyses the double methylation of guanines at both positions 26 and 27 of tRNA.
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The taxonomic range for the selected organisms is: Aquifex aeolicus
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Reaction Schemes
4
+
=
4
+
4
+
guanine26/guanine27 in tRNA
=
4
+
N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
Synonyms
trna (m2(2)g26) methyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA = 4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
reaction mechanism, overview
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SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (guanine26-N2/guanine27-N2)-dimethyltransferase
The enzyme from Aquifex aeolicus is similar to the TRM1 methyltransferases of archaea and eukarya (see EC 2.1.1.216, tRNA (guanine26-N2)-dimethyltransferase). However, it catalyses the double methylation of guanines at both positions 26 and 27 of tRNA.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNACys
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification. A fraction of native tRNACys has a N2-dimethylguanine26/N2-dimethylguanine27 modification. Initially the N2-methylguanine26 modification occurs, and then the second methyl transfer reaction generates N2-dimethylguanine26. The third methyl transfer reaction modifies guanine 27 to N2-methylguanine27 followed by a fourth methylation of N2-methylguanine27 to N2-dimethylguanine27
-
-
?
S-adenosyl-L-methionine + guanine26 in mutant tRNATyr
S-adenosyl-L-homocysteine + N2-methylguanine26 in mutant tRNATyr
mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
-
-
?
S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + guanine27 in tRNATyr
S-adenosyl-L-homocysteine + N2-methylguanine27 in tRNATyr
wild-type tRNATyr contains the sequence adenine26/guanine27
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27
-
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26 in mutant tRNATyr
S-adenosyl-L-homocysteine + N2-dimethylguanine26 in mutant tRNATyr
mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNACys
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNACys
m2G26 formation is faster than the m2G27 formation and disruption of the G27-C43 base pair accelerates velocity of the G27 modification
-
-
?
S-adenosyl-L-methionine + N2-methylguanine27 in tRNATyr
S-adenosyl-L-homocysteine + N2-dimethylguanine27 in tRNATyr
wild-type tRNATyr contains the sequence adenine26/guanine27
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNAPhe
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNAPhe
-
tRNAPhe from yeast
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
-
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
the T-arm in tRNA is the binding site of Trm1, multisite specificity, tRNA-docking modeling, overview
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-
?
additional information
?
-
recognition mechanisms of the Trm1 proteins: Aquifex aeolicus Trm1 recognizes the guanine26 and guanine27 bases from the T-arm. In contrast, archaeal and eukaryotic Trm1 proteins recognize the guanine26 base from the D-stem and variable region. The distance between the T-arm and guanine26 (or guanine27) is longer than the distance between the D-stem, variable region, and guanine26. These differences from binding site to the target guanine base(s) may decide the multisite or single site recognition of the Trm1 proteins
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-
?
additional information
?
-
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recognition mechanisms of the Trm1 proteins: Aquifex aeolicus Trm1 recognizes the guanine26 and guanine27 bases from the T-arm. In contrast, archaeal and eukaryotic Trm1 proteins recognize the guanine26 base from the D-stem and variable region. The distance between the T-arm and guanine26 (or guanine27) is longer than the distance between the D-stem, variable region, and guanine26. These differences from binding site to the target guanine base(s) may decide the multisite or single site recognition of the Trm1 proteins
-
-
?
additional information
?
-
-
Aquifex aeolicus TRm1 may recognize only D-stem structure and guanine26 residue
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-
?
additional information
?
-
-
yeast tRNAPhe and Escherichia coli tRNALeu transcripts are methylated. In contrast, Escherichia coli tRNASer is not methylated, because this tRNA possesses adenine26 sequence instead of guanine26
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-
?
additional information
?
-
-
Trm1 catalyzes methyl transfers to class II tRNAs as well as all class I tRNAs, the size and sequence of the variable region are not recognized by Aquifex aeolicus Trm1, all tRNA transcripts are methylated. tRNA recognition mechanism of multisite specific Trm1, Asp132 is a catalytic center, structure-function analysis, overview
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-methylguanine26/guanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-methylguanine27 in tRNA
-
-
-
?
S-adenosyl-L-methionine + N2-dimethylguanine26/N2-methylguanine27
S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27
-
-
-
?
S-adenosyl-L-methionine + N2-methylguanine26/guanine27 in tRNA
S-adenosyl-L-homocysteine + N2-dimethylguanine26/guanine27 in tRNA
-
-
-
?
4 S-adenosyl-L-methionine + guanine26/guanine27 in tRNA
4 S-adenosyl-L-homocysteine + N2-dimethylguanine26/N2-dimethylguanine27 in tRNA
-
-
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00009
guanine26 in mutant tRNATyr
pH 7.5, 55°C, mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27
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0.00009
guanine26 in mutant tRNATyr
pH 7.5, 55°C, mutant tRNATyr in which the wilde-type adenine26/guanine27 sequence is substituted with guanine26/adenine27, additional point mutation C43U
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0.00008
guanine27 in tRNATyr
pH 7.5, 55°C, tRNA Tyr with wild-type sequence adenine26/guanine27 and mutation C43U
-
0.00017
guanine27 in tRNATyr
pH 7.5, 55°C, wild-type tRNATyr contains the sequence adenine26/guanine27
-
0.00017
S-adenosyl-L-methionine
-
pH 7.5, 55°C, recombinant wild-type enzyme
0.00067
S-adenosyl-L-methionine
-
pH 7.5, 55°C, recombinant mutants L60A, F140A, and E113A
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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archaeal and eukaryotic tRNA (N2,N2-guanine)-dimethyltransferase, Trm1, produces N2,N2-dimethylguanine at position 26 in tRNA. In contrast, Trm1 from Aquifex aeolicus, a hyper-thermophilic eubacterium, modifies G27 as well as G26. The overall structure of Aquifex aeolicus Trm1 is similar to that of archaeal Trm1, although there is a zinc-cysteine cluster in the C-terminal domain of Aquifex aeolicus Trm1
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Trm1 from Aquifex aeolicus contains a zinc-cysteine cluster in the C-terminal domain. The N-terminal domain is a typical catalytic domain of S-adenosyl-L-methionine-dependent methyltransferases. Overall structure, structure comparisons, and structure-function analysis, overview
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D130A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E113A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E6A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F134A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
F140A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
H110A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H219A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H274A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
I65A
-
site-directed mutagenesis, the mutant shows increased activity compared to the wild-type enzyme
I85A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K170A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
K283A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L60A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N29A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R179A
-
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R192A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
R31A
-
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Awai, T.; Kimura, S.; Tomikawa, C.; Ochi, A.; Ihsanawati, A.; Bessho, Y.; Yokoyama, S.; Ohno, S.; Nishikawa, K.; Yokogawa, T.; Suzuki, T.; Hori, H.
Aquifex aeolicus tRNA (N2,N2-guanine)-dimethyltransferase (Trm1) catalyzes transfer of methyl groups not only to guanine 26 but also to guanine 27 in tRNA
J. Biol. Chem.
284
20467-20478
2009
Aquifex aeolicus (O67010), Aquifex aeolicus
Takeda, H.; Hori, H.; Endo, Y.
Identification of Aquifex aeolicus tRNA (m2(2)G26) methyltransferase gene
Nucleic Acids Res. Suppl.
2002
229-230
2002
Aquifex aeolicus
Awai, T.; Takehara, T.; Takeda, H.; Hori, H.
Aquifex aeolicus Trm1[tRNA (m2(2)G26) methyltransferase] has a novel recognition mechanism of the substrate RNA
Nucleic Acids Symp. Ser.
49
303-304
2005
Aquifex aeolicus
Awai, T.; Ochi, A.; Ihsanawati, A.; Sengoku, T.; Hirata, A.; Bessho, Y.; Yokoyama, S.; Hori, H.
Substrate tRNA recognition mechanism of a multisite-specific tRNA methyltransferase, Aquifex aeolicus Trm1, based on the X-ray crystal structure
J. Biol. Chem.
286
35236-35246
2011
Aquifex aeolicus
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