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Information on EC 6.1.1.3 - threonine-tRNA ligase and Organism(s) Pyrococcus abyssi and UniProt Accession Q9UZ14

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Pyrococcus abyssi
UNIPROT: Q9UZ14 not found.
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The taxonomic range for the selected organisms is: Pyrococcus abyssi
The enzyme appears in selected viruses and cellular organisms
Synonyms
threonyl-trna synthetase, thrrs, thr-trna synthetase, mitochondrial threonyl-trna synthetase, threonyl trna synthetase, threonine-trna ligase, threonyl-transfer ribonucleic acid synthetase, bathrrs, apthrrs-1, apthrrs-2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Threonyl-tRNA synthetase
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Synthetase, threonyl-transfer ribonucleate
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Threonine translase
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Threonine--tRNA ligase
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Threonine-transfer ribonucleate synthetase
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Threonyl-ribonucleic synthetase
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Threonyl-transfer ribonucleate synthetase
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Threonyl-transfer ribonucleic acid synthetase
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Threonyl-transfer RNA synthetase
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Threonyl-tRNA synthetase
ThrRS
TRS
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
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esterification
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Aminoacylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-threonine:tRNAThr ligase (AMP-forming)
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CAS REGISTRY NUMBER
COMMENTARY hide
9023-46-5
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
additional information
?
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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
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
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-
?
ATP + L-threonine + tRNAThr
AMP + diphosphate + L-threonyl-tRNAThr
show the reaction diagram
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r
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant D-aminoacyl-tRNA deacylase-like domain with bound Ser3AA, hanging drop vapor diffusion method, mixing of equal volumes of protein, ligand and reservoir solution, crystallization from 0.2 M (NH4)2SO4, 0.1 M sodium cacodylate, pH 6.5, and 30% PEG 8000 and 0.1 M HEPES, pH 7.0, and 25% PEG 3350, purified recombinant D-aminoacyl-tRNA deacylase-like domain with bound SerAMS, using 0.1 M Bis-Tris, pH 6.5, and 25% PEG 3350, and the serine Pab-NTD–L-serine cocrystals from 0.1 M HEPES pH 7.0 and 25% PEG 8000, X-ray diffraction structure determination and analysis at 1.86-2.25 A resolution, overview
purified ultrafiltrated recombinant residues 1-183, hanging drop vapour diffusion method, protein solution, containing 50 mM Tris-HCl, pH 7.5, and 50 mM NaCl, drops of varying volumes against 0.75 ml reservoir solution, at room temperature or at 4°C, preliminary X-ray diffraction for structure determination at 1.95 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E134A
site-directed mutagenesis, the mutation has no effect on the deacylation activity
H83A
site-directed mutagenesis, the mutant possesses the editing activity albeit with a slower rate compared to the wild-type enzyme
K121A
no expression for the alanine mutant
K121M
site-directed mutagenesis, substitution of Lys121 to serine does not abolish Ser-tRNAThr deacylation activity
K121S
site-directed mutagenesis, substitution of Lys121 to serine results in a complete abolition of Ser-tRNAThr deacylation activity
M129K
site-directed mutagenesis, the mutant shows binding not only to L-serine but also to a variety of other L-amino acids that are tested in addition to binding to various D-amino acids, overview
Y120A
site-directed mutagenesis, the mutation has no effect on the deacylation activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant D-aminoacyl-tRNA deacylase-like domains from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
recombinant residues 1-183 from Escherichia coli strain BL21(DE3) by ion exchange chromatography, ammonium sulfate fractionation and gel filtration to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
overexpression of His-tagged wild-type and mutant D-aminoacyl-tRNA deacylase-like domains in Escherichia coli strain BL21(DE3), mutant M129K is located in inclusion bodies
DNA and amino acid sequence determination of residues 1-183, expression in Escherichia coli strain BL21(DE3)
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant mutant M129K D-aminoacyl-tRNA deacylase-like domain from inclusion bodies after expression in Escherichia coli strain BL21(DE3) in 0.1 M phosphate buffer at pH 8.0 containing 6 M guanidinium hydrochloride and 10 mM Tris-HCl, followed by nickel affinity chromatography, the denatured protein is refolded stepwise by dialysis in 0.1 M phosphate buffer, pH 8.0, containing 10 mM Tris-HCl
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Dwivedi, S.; Kruparani, S.P.; Sankaranarayanan, R.
Cloning, expression, purification, crystallization and preliminary X-ray crystallographic investigations of a unique editing domain from archaebacteria
Acta Crystallogr. Sect. D
60
1662-1664
2004
Pyrococcus abyssi
Manually annotated by BRENDA team
Hussain, T.; Kruparani, S.P.; Pal, B.; Dock-Bregeon, A.C.; Dwivedi, S.; Shekar, M.R.; Sureshbabu, K.; Sankaranarayanan, R.
Post-transfer editing mechanism of a D-aminoacyl-tRNA deacylase-like domain in threonyl-tRNA synthetase from archaea
EMBO J.
25
4152-4162
2006
Pyrococcus abyssi (Q9UZ14), Pyrococcus abyssi
Manually annotated by BRENDA team
Malde, A.K.; Mark, A.E.
Binding and enantiomeric selectivity of threonyl-tRNA synthetase
J. Am. Chem. Soc.
131
3848-3849
2009
Pyrococcus abyssi (Q9UZ14)
Manually annotated by BRENDA team
Ahmad, S.; Muthukumar, S.; Kuncha, S.K.; Routh, S.B.; Yerabham, A.S.; Hussain, T.; Kamarthapu, V.; Kruparani, S.P.; Sankaranarayanan, R.
Specificity and catalysis hardwired at the RNA-protein interface in a translational proofreading enzyme
Nat. Commun.
6
7552
2015
Methanocaldococcus jannaschii (Q58597), Pyrococcus furiosus (Q8U176), Pyrococcus abyssi (Q9UZ14), Pyrococcus furiosus ATCC 43587 (Q8U176), Methanocaldococcus jannaschii ATCC 43067 (Q58597)
Manually annotated by BRENDA team