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IUBMB CommentsThe enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg .
Synonyms
Kae1, Qri7, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein KAE1, t6A synthase, tRNA N6-adenosine threonylcarbamoyltransferase, TsaD, YdiE,
ygjD,
more
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
L-threonylcarbamoyladenylate + adenine37 in tRNA

AMP + N6-L-threonylcarbamoyladenine37 in tRNA
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
the enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
the enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
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isoform Qri7 and protein Sua5 are sufficient for N6-threonylcarbamoyladenosine biosynthesis in vitro
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L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
L-threonylcarbamoyladenylate + adenine37 in tRNA

AMP + N6-L-threonylcarbamoyladenine37 in tRNA
the enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg
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-
?
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
the enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg
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-
?
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physiological function

the enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg
physiological function
isoform Kae1 is part of a larger macromolecular assembly called KEOPS with Kae1, Bud32, Cgi121, Gon7 and Pcc1 subunits. Kae1 provides a core essential function that other subunits within KEOPS have evolved to support. Isoform Qri7 complements isoform Kae1 function and complements the function of all subunits
physiological function
isoform Qri7 complements isoform Kae1 function and complements the function of all subunits of a larger macromolecular assembly called KEOPS with Kae1, Bud32, Cgi121, Gon7 and Pcc1 subunits, in growth, N6-threonylcarbamoyladenosine biosynthesis and, to a partial degree, telomeremaintenance. Qri7 alone is sufficient for N6-threonylcarbamoyladenosine biosynthesis with protein Sua5 in vitro
physiological function
N6-threonylcarbamoyladenonsine biosynthesis in Bacillus subtilis requires the four proteins Ywl/TsaC, YdiB/TsaE, YdiC/TsaB and YdiE/TsaD. YwlC catalyzes the conversion of L-threonine, bicarbonate/CO2 and ATP to give the intermediate L-threonylcarbamoyl-AMP and diphosphate as products. Purified L-threonylcarbamoyl-AMP is efficiently processed to N6-threonylcarbamoyladenonsine by the YdiBCE proteins in the presence of tRNA substrates. This reaction is ATP independent in vitro. Data suggest channeling of the intermediate
physiological function
proteins YgjD, YrdC, YjeE, and YeaZ are both necessary and sufficient for threonylcarbamoyl adenosine biosynthesis in vitro. tRNA N6-adenosine threonylcarbamoyltransferase YgjD binds to YjeE, but not to YeaZ
physiological function
the ATPase activity of subunit YjeE is strongly activated by the subunits YgjD-YeaZ heterodimer. Ygjd-YeaZ and YjeE form a compact ternary complex only in presence of ATP. The formation of the ternary YgjD-YeaZ-YjeE complex is required for the in vitro biosynthesis of N6-threonylcarbamoyladenosine but not its ATPase activity
physiological function
threonylcarbamoyl-AMP synthase Sua5 catalyzes the first step leading to the threonyl-carbamoyl-AMP intermediate. Proteins Qri7 and Sua5 together constitute the mitochondrial pathway for the biosynthesis of N6-threonylcarbamoyladenosine. The import of cytoplasmic Sua5 into the mitochondria is required for this organelle to be functional. In vitro, yeast Qri7 can function with either Sua5 or Escherichia coli TsaC. In vivo, Qri7 requires Sua5
physiological function
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N6-threonylcarbamoyladenonsine biosynthesis in Bacillus subtilis requires the four proteins Ywl/TsaC, YdiB/TsaE, YdiC/TsaB and YdiE/TsaD. YwlC catalyzes the conversion of L-threonine, bicarbonate/CO2 and ATP to give the intermediate L-threonylcarbamoyl-AMP and diphosphate as products. Purified L-threonylcarbamoyl-AMP is efficiently processed to N6-threonylcarbamoyladenonsine by the YdiBCE proteins in the presence of tRNA substrates. This reaction is ATP independent in vitro. Data suggest channeling of the intermediate
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physiological function
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the enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, which is found in tRNAs with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg
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crystal structure of the heterodimer YgjD-YeaZ at 2.3 A shows the presence of a molecule of ADP bound at an atypical site situated at the YgjD-YeaZ interface
2.9 A crystal structure of isoform Qri7 reveals a simple homodimer arrangement that is supplanted by the heterodimerization of YgjD with protein YeaZ
in complex with AMP, to 2.94 A resolution. Two molecules per asymmetric unit, forming a dimer. On the dimerization surface of Qri7, the side chains of Trp136 form hydrogen bonds to the carbonyl groups of the main chains of Ala135 and Arg104, and Gln87 forms hydrogen bonds to the side chains of Asp127 and Lys130. Ala88, Ile90, Gly124, Phe128, Gly131 and Val134 of chains A and B form a hydrophobic surface and contribute to hydrophobic interactions
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Lauhon, C.T.
Mechanism of N6-threonylcarbamoyladenonsine (t6A) biosynthesis: isolation and characterization of the intermediate threonylcarbamoyl-AMP
Biochemistry
51
8950-8963
2012
Bacillus subtilis (O05518), Bacillus subtilis 168 (O05518)
brenda
Deutsch, C.; El Yacoubi, B.; de Crecy-Lagard, V.; Iwata-Reuyl, D.
Biosynthesis of threonylcarbamoyl adenosine (t6A), a universal tRNA nucleoside
J. Biol. Chem.
287
13666-13673
2012
Escherichia coli (P05852)
brenda
Perrochia, L.; Crozat, E.; Hecker, A.; Zhang, W.; Bareille, J.; Collinet, B.; van Tilbeurgh, H.; Forterre, P.; Basta, T.
In vitro biosynthesis of a universal t6A tRNA modification in Archaea and Eukarya
Nucleic Acids Res.
41
1953-1964
2013
Pyrococcus abyssi (Q9UXT7), Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543 (Q9UXT7)
brenda
Wan, L.C.K.; Mao, D.Y.L.; Neculai, D.; Strecker, J.; Chiovitti, D.; Kurinov, I.; Poda, G.; Thevakumaran, N.; Yuan, F.; Szilard, R.K.; Lissina, E.; Nislow, C.; Caudy, A.A.; Durocher, D.; Sicheri, F.
Reconstitution and characterization of eukaryotic N6-threonylcarbamoylation of tRNA using a minimal enzyme system
Nucleic Acids Res.
41
6332-6346
2013
Saccharomyces cerevisiae (P43122), Saccharomyces cerevisiae (P36132)
brenda
Tominaga, T.; Kobayashi, K.; Ishii, R.; Ishitani, R.; Nureki, O.
Structure of Saccharomyces cerevisiae mitochondrial Qri7 in complex with AMP
Acta Crystallogr. Sect. F
70
1009-1014
2014
Saccharomyces cerevisiae (P43122)
brenda
Thiaville, P.C.; El Yacoubi, B.; Perrochia, L.; Hecker, A.; Prigent, M.; Thiaville, J.J.; Forterre, P.; Namy, O.; Basta, T.; de Crecy-Lagard, V.
Cross kingdom functional conservation of the core universally conserved threonylcarbamoyladenosine tRNA synthesis enzymes
Eukaryot. Cell
13
1222-1231
2014
Saccharomyces cerevisiae (P43122)
brenda
Zhang, W.; Collinet, B.; Perrochia, L.; Durand, D.; Van Tilbeurgh, H.
The ATP-mediated formation of the YgjD-YeaZ-YjeE complex is required for the biosynthesis of tRNA t6A in Escherichia coli
Nucleic Acids Res.
43
1804-1817
2014
Escherichia coli (P05852)
brenda