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Information on EC 2.1.1.268 - tRNAThr (cytosine32-N3)-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession Q08641

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     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.268 tRNAThr (cytosine32-N3)-methyltransferase
IUBMB Comments
The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer.
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Saccharomyces cerevisiae
UNIPROT: Q08641
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
abp140, trm140, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
S-adenosyl-L-methionine + cytosine32 in tRNAThr = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
show the reaction diagram
(1)
S-adenosyl-L-methionine + cytosine32 in tRNASer = S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
show the reaction diagram
(2)
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNAThr (cytosine32-N3)-methyltransferase
The enzyme from Saccharomyces cerevisiae specifically methylates cytosine32 in tRNAThr and in tRNASer.
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 + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
show the reaction diagram
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
show the reaction diagram
S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
show the reaction diagram
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
show the reaction diagram
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?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr(CGU)
show the reaction diagram
G35 and U36 of tRNAThr(CGU) are required for m3C formation. Trm140 specifically binds tRNAThr substrates, overview. Best tRNAThr substrate is tRNATyr(GUA), lower activity occurs with tRNAThr(CGU), tRNAThr(IGU), and tRNAThr(UGU)
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additional information
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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
S-adenosyl-L-methionine + cytosine32 in tRNA1Ser
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Ser
show the reaction diagram
tRNASer1 = tRNASer(UGA). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
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?
S-adenosyl-L-methionine + cytosine32 in tRNA1Thr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNA1Thr
show the reaction diagram
tRNAThr1 = tRNAThr(IGU). Because position 32 of tRNA has an important role in accurate codon recognition, N3-methylcytosine32 formation in tRNAThr1 or tRNASer1 might play a role in modulating codon recognition and translational efficiency
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S-adenosyl-L-methionine + cytosine32 in tRNASer
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNASer
show the reaction diagram
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?
S-adenosyl-L-methionine + cytosine32 in tRNAThr
S-adenosyl-L-homocysteine + N3-methylcytosine32 in tRNAThr
show the reaction diagram
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?
additional information
?
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Trm140 interacts with Ses1, a cytoplasmic serine-tRNA ligase (EC 6.1.1.11). Ses1 stimulates m3C formation of tRNASer species
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ses1
seryl-tRNA synthetase Ses1 greatly stimulates m3C modification of tRNASer(CGA) and tRNASer(UGA) in vitro
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
subcellular localization of ABP140 to actin filaments is not involved in tRNA modification
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
in the yeast Saccharomyces cerevisiae, formation of m3C32 requires Trm140 for six tRNA substrates, including three tRNAThr species and three tRNASer species, whereas in Schizosaccharomyces pombe, two Trm140 homologues are used, one for tRNAThr and one for tRNASer. The occurrence of a single Trm140 homologue is conserved broadly among Ascomycota, whereas multiple Trm140-related homologues are found in metazoans and other fungi
malfunction
physiological function
additional information
enzyme Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates. Trm140 recognizes G35-U36-t6A37 of the anticodon loop of tRNAThr substrates, and this sequence is an identity element because it can be used to direct m3C modification of tRNAPhe. Trm140 recognition of tRNASer substrates is different, since their anticodons do not share G35-U36 and do not have any nucleotides in common. Rather, specificity of Trm140 for tRNASer is achieved by seryl-tRNA synthetase and the distinctive tRNASer V-loop, as well as by t6A37 and i6A37
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
71486
2 * 71486, the homodimer is formed through covalent linkage(s) other than disulfide bond, calculated from sequence, SDS-PAGE
71500
2 * 71500, the homodimer is formed through covalent linkage(s) other than disulfide bond, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D466A
no formation of N3-methylcytosine32
D547A
decreased activity
delD602-Q621
no formation of N3-methylcytosine32
additional information
construction of a deletion trm140DELTA strain
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichi coli
expression of hexahistidine-tagged Abp140p in Saccharomces cerevisiae
gene ABP140, recombinant expression in Saccharomyces cerevisiae, coexpression with yeast enzyme Ses1
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
D'Silva, S.; Haider, S.J.; Phizicky, E.M.
A domain of the actin binding protein Abp140 is the yeast methyltransferase responsible for 3-methylcytidine modification in the tRNA anti-codon loop
RNA
17
1100-1110
2011
Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Noma, A.; Yi, S.; Katoh, T.; Takai, Y.; Suzuki, T.; Suzuki, T.
Actin-binding protein ABP140 is a methyltransferase for 3-methylcytidine at position 32 of tRNAs in Saccharomyces cerevisiae
RNA
17
1111-1119
2011
Homo sapiens (Q6P1Q9), Homo sapiens, Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Han, L.; Marcus, E.; DSilva, S.; Phizicky, E.
S. cerevisiae Trm140 has two recognition modes for 3-methylcytidine modification of the anticodon loop of tRNA substrates
RNA
23
406-419
2017
Saccharomyces cerevisiae (Q08641), Saccharomyces cerevisiae ATCC 204508 (Q08641)
Manually annotated by BRENDA team