Information on EC 2.3.1.234 - N6-L-threonylcarbamoyladenine synthase

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The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota

EC NUMBER
COMMENTARY hide
2.3.1.234
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RECOMMENDED NAME
GeneOntology No.
N6-L-threonylcarbamoyladenine synthase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
L-threonylcarbamoyladenylate + adenine37 in tRNA = AMP + N6-L-threonylcarbamoyladenine37 in tRNA
show the reaction diagram
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
N6-L-threonylcarbamoyladenosine37-modified tRNA biosynthesis
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threonine metabolism
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
Manually annotated by BRENDA team
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SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
show the reaction diagram
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-threonylcarbamoyladenylate + adenine37 in tRNA
AMP + N6-L-threonylcarbamoyladenine37 in tRNA
show the reaction diagram
Q9UXT7
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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presence of metal ions in the crystal structures
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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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
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Pyrococcus abyssi (strain GE5 / Orsay)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
Kae1 is part of a conserved protein complex named kinase, endopeptidase and other proteins of small size (KEOPS)
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
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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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
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