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Information on EC 6.1.1.24 - glutamate-tRNAGln ligase and Organism(s) Thermotoga maritima and UniProt Accession Q9X2I8

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EC Tree
IUBMB Comments
When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate---tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon . This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln.
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Thermotoga maritima
UNIPROT: Q9X2I8
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The taxonomic range for the selected organisms is: Thermotoga maritima
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
glu-q-rs, nd-glurs, non-discriminating glutamyl-trna synthetase, glxrs, nondiscriminating glurs, tm1875, nondiscriminating glutamyl-trna synthetase, non-discriminating glurs, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Glutamyl-tRNA synthetase
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nondiscriminating GluRS
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nondiscriminating glutamyl-tRNA synthetase
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TM1875
GluRS
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nondiscriminating glutamyl-tRNA synthetase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Aminoacylation
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PATHWAY SOURCE
PATHWAYS
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SYSTEMATIC NAME
IUBMB Comments
L-glutamate:tRNAGlx ligase (AMP-forming)
When this enzyme acts on tRNAGlu, it catalyses the same reaction as EC 6.1.1.17, glutamate---tRNA ligase. It has, however, diminished discrimination, so that it can also form glutamyl-tRNAGln. This relaxation of specificity has been found to result from the absence of a loop in the tRNA that specifically recognizes the third position of the anticodon [1]. This accounts for the ability of this enzyme in, for example, Bacillus subtilis, to recognize both tRNA1Gln (UUG anticodon) and tRNAGlu (UUC anticodon) but not tRNA2Gln (CUG anticodon). The ability of this enzyme to recognize both tRNAGlu and one of the tRNAGln isoacceptors derives from their sharing a major identity element, a hypermodified derivative of U34 (5-methylaminomethyl-2-thiouridine). The glutamyl-tRNAGln is not used in protein synthesis until it is converted by EC 6.3.5.7, glutaminyl-tRNA synthase (glutamine-hydrolysing), into glutaminyl-tRNAGln.
CAS REGISTRY NUMBER
COMMENTARY hide
9068-76-2
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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 + Glu + tRNAGln
AMP + diphosphate + L-glutamyl-tRNAGln
show the reaction diagram
the glutamylation ability of tRNAGln by ND-GluRS is measured in the presence of the bacterial Glu-tRNAGln amidotransferase GatCAB. Glutamylation efficiency is not affected even in the presence of excess GatCAB
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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
additional information
?
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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
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
ND-GluRS produces the intermediate Glu-tRNAGln, which is converted to Gln-tRNAGln by Glu-tRNAGln amidotransferase. GluRS avoids competition with Glu-tRNAGln amidotransferase GatCAB and glutamylates tRNAGln
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the crystal structure of the Thermotoga maritima ND-GluRS, TM1875, is determined in complex with a Glu-AMP analogue at 2.0 A resolution. ND-GluRS contains a characteristic structure in the connective-peptide domain, which is inserted into the catalytic Rossmann-fold domain
TM1875 in complex with a Glu-AMP analogue, mixing of 0.0018 ml of 15 mg/ml protein in 20 mM Tris-HCl, pH 7.0, containing 5 mM MgCl2, 10 mM 2-mercaptoethanol, 50 mM NaCl, and 1 mM L-glutamylsulfamoyl adenosine, with 0.0018 ml reservoir solution containing 100 mM HEPES-NaOH, pH 7.5, 8% ethylene glycol and 15% PEG 8000, and 0.0004 ml of 30% D-sorbitol, equilibration against 0.5 ml reservoir solution, 20°C, 1 week, X-ray diffraction structure determination and analysis at 2.0 A resolution
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant TM1875 from Escherichia coli strain Rosetta2 (DE3) by anion exchange chromatography and gel filtration
using ion-exchange column chromatography and gel-filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
TM1875, sequence comparisons, expression in Escherichia coli strain Rosetta2(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Ito, T.; Kiyasu, N.; Matsunaga, R.; Takahashi, S.; Yokoyama, S.
Structure of nondiscriminating glutamyl-tRNA synthetase from Thermotoga maritima
Acta Crystallogr. Sect. D
66
813-820
2010
Thermotoga maritima (Q9X2I8), Thermotoga maritima
Manually annotated by BRENDA team