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Information on EC 2.7.7.87 - L-threonylcarbamoyladenylate synthase and Organism(s) Saccharomyces cerevisiae and UniProt Accession P32579

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:
Saccharomyces cerevisiae
UNIPROT: P32579
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The taxonomic range for the selected organisms is: Saccharomyces cerevisiae
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
sua5 protein, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ScKEOPS
-
protein complex
Sua5 protein
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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 SUA5 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
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 SUA5 family is involved in the biosynthesis of N6-threonylcarbamoyl adenosine
threonylcarbamoyladenosine i.e. t6A
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Mn2+
-
stimulating effect, it increases the yield of the reaction to 38%
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.00011
L-threonine
-
pH 8.0, temperature not specified in the publication
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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
malfunction
-
the loss of SUA5 causes increased leaky scanning through AUG codons, +1 frameshifting, and nonsense suppression. In addition, the loss of SUA5 amplifies the 20S RNA virus found in Saccharomyces cerevisiae, possibly through an internal ribosome entry site-mediated mechanism
physiological function
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
gravity-flow chromatography on an Ni-NTA resin column, not associated with tRNAs when purified
-
Ni-NTA affinity chromatography
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
full length Sua5 expressed in Escherichia coli BL21 (DE3) CodonPlus cells harboring an N-terminal hexa-histidine tag
-
ScSua5 gene amplified by PCR using genomic DNA from Saccharomyces cerevisiae, fused to a hexa-histidine tag at its 3'-end and cloned into pET21d vector and transformed in Escherichia coli
-
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
Lin, C.A.; Ellis, S.R.; True, H.L.
The Sua5 protein is essential for normal translational regulation in yeast
Mol. Cell. Biol.
30
354-363
2010
Saccharomyces cerevisiae
Manually annotated by BRENDA team
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, Saccharomyces cerevisiae
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team