BRENDA home
History
Information on EC 2.3.1.234 - N6-L-threonylcarbamoyladenine synthase
for references in articles please use BRENDA:EC2.3.1.234Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
2.3.1.234 N6-L-threonylcarbamoyladenine synthaseIUBMB Comments
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 .
Specify your search results
The enzyme appears in viruses and cellular organisms
Reaction Schemes
+
adenine37 in tRNA
=
+
Synonyms
Kae1, Qri7, t(6)A synthase, t(6)A37 threonylcarbamoyladenosine biosynthesis protein KAE1, t6A synthase, tRNA N6-adenosine threonylcarbamoyltransferase, TsaD, YdiE, ygjD, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Kae1
Qri7
t(6)A37 threonylcarbamoyladenosine biosynthesis protein KAE1
-
t6A synthase
TsaD
YdiE
ygjD
Kae1
Kae1 is part of a conserved protein complex named kinase, endopeptidase and other proteins of small size (KEOPS)
Kae1
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
Kae1 is part of a conserved protein complex named kinase, endopeptidase and other proteins of small size (KEOPS)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-threonylcarbamoyladenylate + adenine37 in tRNA = AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PATHWAY SOURCE
PATHWAYS
BRENDA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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].
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
-
-
?
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
-
-
?
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
-
-
?
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
-
-
-
?
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
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
-
-
?
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
-
-
?
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
-
isoform Qri7 and protein Sua5 are sufficient for N6-threonylcarbamoyladenosine biosynthesis in vitro
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
-
-
?
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
presence of metal ions in the crystal structures
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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
-
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
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
-
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
-
Show AA Sequence and Transmembrane Helices (51292 entries)
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Longer loading times are possible. Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
Kae1 is part of a conserved protein complex named kinase, endopeptidase and other proteins of small size (KEOPS)
additional information
Pyrococcus abyssi GE5 / CNCM I-1302 / DSM 25543
-
Kae1 is part of a conserved protein complex named kinase, endopeptidase and other proteins of small size (KEOPS)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 2.3.1.234)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
About BRENDA
Help
Download
Contribution
member of
curated at
curated at
Server: brenda3 Ver: 9edf756-main (2022-05-17 10:30:03 +0200)