6.3.5.7: glutaminyl-tRNA synthase (glutamine-hydrolysing)
This is an abbreviated version!
For detailed information about glutaminyl-tRNA synthase (glutamine-hydrolysing), go to the full flat file.
Word Map on EC 6.3.5.7
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6.3.5.7
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gln-trnagln
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gatcabs
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archaea
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aminoacyl-trnas
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trna-dependent
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transamidation
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misacylated
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mischarged
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asp-trnaasn
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aspartyl-trna
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asparaginyl-trna
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aminoacylation
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gln-trna
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methanothermobacter
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glutaminase
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thermautotrophicus
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trnaasn
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non-discriminating
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transamidase
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misaminoacylated
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glnrs
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analysis
- 6.3.5.7
- gln-trnagln
- gatcabs
- archaea
- aminoacyl-trnas
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trna-dependent
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transamidation
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misacylated
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mischarged
- asp-trnaasn
- aspartyl-trna
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asparaginyl-trna
- aminoacylation
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gln-trna
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methanothermobacter
- glutaminase
- thermautotrophicus
- trnaasn
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non-discriminating
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transamidase
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misaminoacylated
- glnrs
- analysis
Reaction
Synonyms
aa-tRNA amidotransferase, AdT, amidotransferase B, amidotransferase C, amidotransferase, glutamyl-transfer ribonucleate (glutamine-specific), aminoacyl-tRNA amidotransferase, BANKA_112750, gatA, GatB, GatCAB, GatCAB amidotransferase, GatDE, Gln4, GlnRS, Glu-AdT, Glu-amidotransferase, Glu-tRNAGln amidotransferase, Glu-tRNAGlnAT, GluAdT GatDE, GluRS, glutamyl-tRNA(Gln) amidotransferase, glutamyl-tRNAGln amidotransferase, nondiscriminating GluRS, PBANKA_071810, PF3D7_0416100, PF3D7_0628800, Qrsl1
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General Information
General Information on EC 6.3.5.7 - glutaminyl-tRNA synthase (glutamine-hydrolysing)
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metabolism
physiological function
eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions of glutaminyl-tRNA synthetase and glutamyl-tRNA synthetase, respectively, and are mutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating luRS to GlnRS
metabolism
Saccharomyces cerevisiae ATCC 204508 / S288c
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eukaryotic tRNAGln and tRNAGlu recognition determinants are found in equivalent positions of glutaminyl-tRNA synthetase and glutamyl-tRNA synthetase, respectively, and are mutually exclusive to a significant degree, with key nucleotides located adjacent to portions of the protein structure that differentiated during the evolution of archaeal nondiscriminating luRS to GlnRS
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inactivation of any of the hGatCAB subunits by siRNA-mediated knock down in HeLa cells leads to accumulation of the Glu-charged form of tRNAGln and defects in respiration can be observed
physiological function
using gel mobility shift assays it is shown that formation of the glutamine transamidosome from Thermotoga maritima, consists of tRNAGln, glutamyltRNA synthase (GluRS) and the heterotrimeric amidotransferase GatCAB. The tail body of GatCAB recognizes the outer corner of the L-shaped tRNAGln in a tRNAGln-specific manner. GatCAB is in the non-productive form: the catalytic body of GatCAB contacts that of GluRS and is located near the acceptor stem of tRNAGln, in an appropriate site to wait for the completion of Glu-tRNAGln formation by GluRS. Hinges are identified between the catalytic and anticodon-binding bodies of GluRS and between the catalytic and tail bodies of GatCAB, which allow both GluRS and GatCAB to adopt the productive and non-productive forms
physiological function
A0A509AHQ9; A0A509AM58
gene encoding GatA is essential to the Plasmodium berghei blood stages
physiological function
knock-down of GatA by siRNA produces a strong defect in mitochondrial translation without affecting the stability of the newly synthesized proteins. Interfered cells present an impairment of the oxidative phosphorylation system and a significant increase in ROS levels. Mitochondrial proteins have no glutamic acid in the position of glutamines
physiological function
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gene encoding GatA is essential to the Plasmodium berghei blood stages
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