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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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
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SYSTEMATIC NAME
IUBMB Comments
L-threonylcarbamoyladenylate:adenine37 in tRNA N6-L-threonylcarbamoyltransferase
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 [3].
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
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
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
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
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
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
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
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
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; 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
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
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
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
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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CRYSTALLIZATION/commentary
ORGANISM
UNIPROT
LITERATURE
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
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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2.3.1.234 N6-L-threonylcarbamoyladenine synthase
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