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Information on EC 2.1.1.229 - tRNA (carboxymethyluridine34-5-O)-methyltransferase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P49957

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IUBMB Comments
The enzyme catalyses the posttranslational modification of uridine residues at the wobble position 34 of the anticodon loop of tRNA.
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This record set is specific for:
Saccharomyces cerevisiae
UNIPROT: P49957
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
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S-adenosyl-L-methionine
+
carboxymethyluridine34 in tRNA
=
S-adenosyl-L-homocysteine
+
5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
+
carboxymethyluridine34 in tRNA
=
+
5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
Synonyms
trna methyltransferase 9, trm9p, trm9-trm112, yml014w, more
PATHWAY SOURCE
PATHWAYS
-
-, -
SYSTEMATIC NAME
IUBMB Comments
S-adenosyl-L-methionine:tRNA (carboxymethyluridine34-5-O)-methyltransferase
The enzyme catalyses the posttranslational modification of uridine residues at the wobble position 34 of the anticodon loop of tRNA.
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 + carboxymethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
show the reaction diagram
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNAArg3
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNAGlU
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
show the reaction diagram
-
-
-
?
S-adenosyl-L-methionine + carboxymethyl-2-thiouridine34 in tRNA
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)-2-thiouridine34 in tRNA
show the reaction diagram
-
Trm9-Trm112, subunit Trm112 is required for the activity, but role of Sc Trm112 in the complex is not for catalysis
-
-
?
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
show the reaction diagram
additional information
?
-
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 + carboxymethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
show the reaction diagram
Trm9 methylates the uridine wobble base of tRNAArg(UCU) and tRNAGlU(UUC)
-
-
?
S-adenosyl-L-methionine + carboxymethyl-2-thiouridine34 in tRNA
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)-2-thiouridine34 in tRNA
show the reaction diagram
-
Trm9-Trm112, subunit Trm112 is required for the activity, but role of Sc Trm112 in the complex is not for catalysis
-
-
?
S-adenosyl-L-methionine + carboxymethyluridine34 in tRNA
S-adenosyl-L-homocysteine + 5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
show the reaction diagram
additional information
?
-
-
alternative mechanisms in formation of the 5-carboxymethyluridine34 side chain at wobble position, overview
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
S-adenosyl-L-methionine
-
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Trm112p
when produced in Escherichia coli, Trm112p forms a complex with Trm9p, which renders the latter soluble. This recombinant complex catalyzes the formation of mcm5U34 (5-methoxycarbonylmethyluridine) on tRNA in vitro but not mcm5s2U34 (5-methoxycarbonylmethyl-2-thiouridine)
-
Trm112 p
-
the presence of Trm112p dramatically improves the methyltransferase activity of Trm9p in vitro
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
physiological function
Trm9 prevents cell death via translational enhancement of DNA damage response proteins. Trm9-specific tRNA modifications enhance codon-specific translation elongation and promote increased levels of key damage response proteins
evolution
-
the mcm5U family of modifications is found only in eukaryotes and is implicated in efficient reading of AGA and AAG codons by tRNAArg (UCU) and tRNAGlu(UUC), respectively in Saccharomyyces cerevisiae. Trm112 partners with several methyltransferases involved in diverse translational processes and has distinct roles in other methyltransferase complexes
malfunction
metabolism
-
Trm9p and Trm112p function together at the final step in formation of 5-methoxycarbonylmethyl-uridine in tRNA by using the intermediate 5-carbamoylmethyluridine as a substrate
physiological function
-
at position 34, the majority of yeast cytosolic tRNA species that have a uridine are modified to 5-carbamoylmethyluridine, 5-carbamoylmethyl-2'-O-methyluridine, 5-methoxycarbonylmethyl-uridine or 5-methoxycarbonylmethyl-2-thiouridine. The formation of 5-methoxycarbonylmethyl-uridine and 5-carbamoylmethyluridine side chains involves a complex pathway, where the last step in formation of mcm5 is a methyl esterification of 5-carboxymethyl dependent on the Trm9 and Trm112 proteins. Both Trm9 and Trm112 are required for the last step in formation of 5-methoxycarbonylmethyl side chains at wobble uridines
additional information
-
different catalytic subunits, e.g. Trm9, engage the same partner protein Trm112 to direct different chemical modifications on different residues
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterodimer
-
the enzyme is formed by catalytic subunit Trm9 and regulatory subunit Trm112
additional information
-
different catalytic subunits engage the same partner protein Trm112 to direct different chemical modifications on different residues
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
co-purification of His-tagged Trm9p with untagged Trm112p as a complex from Escherichia coli strain BL21(DE3)pLysS by nickel affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of GST-Trm9 fusion protein in Escherichia coli DH5alpha cells
co-expression of His-tagged Trm9p with untagged Trm112p in Escherichia coli strain BL21(DE3)pLysS, Trm9p/Trm112p complex formation
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Kalhor, H.R.; Clarke, S.
Novel methyltransferase for modified uridine residues at the wobble position of tRNA
Mol. Cell. Biol.
23
9283-9292
2003
Saccharomyces cerevisiae (P49957), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Mazauric, M.H.; Dirick, L.; Purushothaman, S.K.; Bjrk, G.R.; Lapeyre, B.
Trm112p is a 15-kDa zinc finger protein essential for the activity of two tRNA and one protein methyltransferases in yeast
J. Biol. Chem.
285
18505-18515
2010
Saccharomyces cerevisiae (P49957), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Begley, U.; Dyavaiah, M.; Patil, A.; Rooney, J.P.; DiRenzo, D.; Young, C.M.; Conklin, D.S.; Zitomer, R.S.; Begley, T.J.
Trm9-catalyzed tRNA modifications link translation to the DNA damage response
Mol. Cell
28
860-870
2007
Saccharomyces cerevisiae (P49957), Saccharomyces cerevisiae
Manually annotated by BRENDA team
Jablonowski, D.; Zink, S.; Mehlgarten, C.; Daum, G.; Schaffrath, R.
tRNAGlu wobble uridine methylation by Trm9 identifies Elongator's key role for zymocin-induced cell death in yeast
Mol. Microbiol.
59
677-688
2006
Saccharomyces cerevisiae (P49957)
Manually annotated by BRENDA team
Chen, C.; Huang, B.; Anderson, J.T.; Bystroem, A.S.
Unexpected accumulation of ncm5U and ncm5S2U in a trm9 mutant suggests an additional step in the synthesis of mcm5U and mcm5S2U
PLoS ONE
6
e20783
2011
Saccharomyces cerevisiae
Manually annotated by BRENDA team
Guy, M.P.; Phizicky, E.M.
Two-subunit enzymes involved in eukaryotic post-transcriptional tRNA modification
RNA Biol.
11
1608-1618
2014
Saccharomyces cerevisiae
Manually annotated by BRENDA team