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Information on EC 2.7.7.87 - L-threonylcarbamoyladenylate synthase and Organism(s) Escherichia coli and UniProt Accession P45748

for references in articles please use BRENDA:EC2.7.7.87
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IUBMB Comments
The enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg .
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This record set is specific for:
Escherichia coli
UNIPROT: P45748
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The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sua5 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N6-threonylcarbamoyltransferase
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
ATP:L-threonyl,bicarbonate adenylyltransferase
The enzyme is involved in the synthesis of N6-threonylcarbamoyladenosine37 in tRNAs, with the anticodon NNU, i.e. tRNAIle, tRNAThr, tRNAAsn, tRNALys, tRNASer and tRNAArg [6].
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
L-threonine + ATP + bicarbonate
L-threonylcarbamoyladenylate + diphosphate + H2O
show the reaction diagram
results indicate that the universally conserved YrdC family is involved in the biosynthesis of N6-threonylcarbamoyl adenosine
threonylcarbamoyladenosine i.e. t6A
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?
L-threonine + ATP + bicarbonate
L-threonylcarbamoyladenylate + diphosphate + H2O
show the reaction diagram
additional information
?
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t6A is a universally conserved tRNA modification found at position 37 in the anticodon loop of a subset of tRNA, structural studies predict an important role for t6A in translational fidelity
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
L-threonine + ATP + bicarbonate
L-threonylcarbamoyladenylate + diphosphate + H2O
show the reaction diagram
results indicate that the universally conserved YrdC family is involved in the biosynthesis of N6-threonylcarbamoyl adenosine
threonylcarbamoyladenosine i.e. t6A
-
?
L-threonine + ATP + bicarbonate
L-threonylcarbamoyladenylate + diphosphate + H2O
show the reaction diagram
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
threonylcarbamoyladenosine is a universal modification found at position 37 of ANN decoding tRNAs, which imparts a unique structure to the anticodon loop enhancing its binding to ribosomes in vitro
physiological function
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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fluorescence quenching data indicate that YrdC recognizes the RNA substrate in a sequence-dependent manner by directly interacting with certain bases
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
yrdC protein purified by Ni-NTA affinity chromatography, dialyzed against phosphate-buffered saline and concentrated using a YM-3 Centriprep filter
by Ni-NTA affinity chromatography to a purity of more than 95% by SDS-PAGE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli BL21(DE3) cells transformed with a pET21 derivative (Novagen) vector containing the Escherichia coli yrdC gene
His6-tagged YrdC protein overexpressed in Escherichia coli
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yrdC, yjeE and yeaZ genes from Escherichia coli expressed as N-terminal His6-fusion proteins, YgjD N-terminal as His6-SUMO fusion protein in Escherichia coli
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
El Yacoubi, B.; Lyons, B.; Cruz, Y.; Reddy, R.; Nordin, B.; Agnelli, F.; Williamson, J.R.; Schimmel, P.; Swairjo, M.A.; Crecy-Lagard, V.
The universal YrdC/Sua5 family is required for the formation of threonylcarbamoyladenosine in tRNA
Nucleic Acids Res.
37
2894-2909
2009
Saccharomyces cerevisiae (P32579), Escherichia coli (P45748)
Manually annotated by BRENDA team
Harris, K.A.; Jones, V.; Bilbille, Y.; Swairjo, M.A.; Agris, P.F.
YrdC exhibits properties expected of a subunit for a tRNA threonylcarbamoyl transferase
RNA
17
1678-1687
2011
Escherichia coli
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Harris, K.A.; Shekhtman, A.; Agris, P.F.
Specific RNA-protein interactions detected with saturation transfer difference NMR
RNA Biol.
10
1307-1311
2013
Escherichia coli
Manually annotated by BRENDA team