Modomics - A Database of RNA Modifications

Full name: tRNA glutamyl-Q(34) synthetase
Synonym: YadB
GI: 85674352
Orf: b0144
COG: COG0008
UniProt: P27305
Structures: | 1NZJ | 4A91 |
Enzyme type: aminoacyl-tRNA synthetase-like
Position of modification - modification: t:34 - gluQ


The aminoacylation reaction occurs on one of the two free hydroxyl group of Q-base attached to the wobble position 34 of tRNAAsp. The glutamic acid is activated by the formation of an adenylate derivative (Glu-AMP) through a reaction with ATP.

Protein sequence:


Enzymatic activities:

Reaction Substrate Type Position
Q:gluQ tRNA (t) Asp/GUC/prokaryotic cytosol 34


Title Authors Journal Details PubMed Id DOI
A truncated aminoacyl-tRNA synthetase modifies RNA. Salazar JC, Ambrogelly A, Crain PF, McCloskey JA, Soll D Proc Natl Acad Sci U S A [details] 15096612 -
The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity. Campanacci V, Dubois DY, Becker HD, Kern D, Spinelli S, Valencia C, Pagot F, Salomoni A, Grisel S, Vincentelli R, Bignon C, Lapointe J, Giege R, Cambillau C J Mol Biol [details] 15003446 -
Glu-Q-tRNA(Asp) synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNA(Asp) anticodon. Blaise M, Becker HD, Lapointe J, Cambillau C, Giege R, Kern D Biochimie [details] 16164993 -
An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp. Dubois DY, Blaise M, Becker HD, Campanacci V, Keith G, Giege R, Cambillau C, Lapointe J, Kern D Proc Natl Acad Sci U S A [details] 15096594 -
A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon. Blaise M, Becker HD, Keith G, Cambillau C, Lapointe J, Giege R, Kern D Nucleic Acids Res [details] 15150343 -
Crystal structure of glutamyl-queuosine tRNAAsp synthetase complexed with L-glutamate: structural elements mediating tRNA-independent activation of glutamate and glutamylation of tRNAAsp anticodon. Blaise M, Olieric V, Sauter C, Lorber B, Roy B, Karmakar S, Banerjee R, Becker HD, Kern D J Mol Biol [details] 18602926 -



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