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Information on EC 2.1.1.229 - tRNA (carboxymethyluridine34-5-O)-methyltransferase and Organism(s) Mus musculus and UniProt Accession Q80Y20

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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:
Mus musculus
UNIPROT: Q80Y20
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The taxonomic range for the selected organisms is: Mus musculus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
+
carboxymethyluridine34 in tRNA
=
+
5-(2-methoxy-2-oxoethyl)uridine34 in tRNA
Synonyms
trna methyltransferase 9, trm9p, trm9-trm112, yml014w, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
TRM112
interaction of ALKBH8 with a small accessory protein, TRM112, is required to form a functional tRNA methyltransferase
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
mcm5U, mcm5Um, and mcm5s2U are detected in total tRNA from wild-type livers but are completely absent from total tRNA from Alkbh8-/- mice. Substantial amounts of cm5U, the putative unmethylated precursor of mcm5U, is detected in total tRNA from Alkbh8-/- mice but not in total tRNA from wild-type mice. Despite the complete loss of all of these uridine modifications, Alkbh8-/- mice appear normal. However, the selenocysteine-specific tRNA is aberrantly modified in the Alkbh8-/- mice, and for the selenoprotein Gpx1, a reduced recoding of the UGA stop codon to selenocysteine is observed
physiological function
ALKBH8-mediated methylation is a prerequisite for the thiolation and 2'-O-ribose methylation that form 5-methoxycarbonylmethyl-2-thiouridine and 5-methoxycarbonylmethyl-2'-O-methyluridine, respectively
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
ALKB8_MOUSE
664
0
74768
Swiss-Prot
other Location (Reliability: 5)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
ALKBH8 and TRM112 form a functional tRNA methyltransferase complex (Trm112 is an accessory protein required for several methyltransferases)
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Songe-Moller, L.; van den Born, E.; Leihne, V.; Vagbo C.B.; Kristoffersen, T.; Krokan, H.E.; Kirpekar, F.; Falnes, P.O.; Klungland, A.
Mammalian ALKBH8 possesses tRNA methyltransferase activity required for the biogenesis of multiple wobble uridine modifications implicated in translational decoding
Mol. Cell. Biol.
30
1814-1827
2010
Mus musculus (Q80Y20)
Manually annotated by BRENDA team