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Information on EC 6.3.5.7 - glutaminyl-tRNA synthase (glutamine-hydrolysing) and Organism(s) Homo sapiens and UniProt Accession O75879

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EC Tree
IUBMB Comments
In systems lacking discernible glutamine---tRNA ligase (EC 6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In the first step, a nondiscriminating ligase (EC 6.1.1.24, glutamate---tRNAGln ligase) mischarges tRNAGln with glutamate, forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this enzyme). A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. Some bacterial GatCAB complexes also has the activity of EC 6.3.5.6 (asparaginyl-tRNA synthase [glutamine-hydrolysing]).
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Homo sapiens
UNIPROT: O75879
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Word Map
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
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Synonyms
gatde, glu-adt, qrsl1, gatcab amidotransferase, glu-trnagln amidotransferase, glutamyl-trnagln amidotransferase, glutamyl-trna(gln) amidotransferase, amidotransferase b, aminoacyl-trna amidotransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
amidotransferase B
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amidotransferase C
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amidotransferase, glutamyl-transfer ribonucleate (glutamine-specific)
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Glu-AdT
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Glu-tRNAGln amidotransferase
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Glu-tRNAGlnAT
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glutamyl-tRNA(Gln) amidotransferase
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glutamyl-tRNAGln amidotransferase
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SYSTEMATIC NAME
IUBMB Comments
L-glutamyl-tRNAGln:L-glutamine amido-ligase (ADP-forming)
In systems lacking discernible glutamine---tRNA ligase (EC 6.1.1.18), glutaminyl-tRNAGln is formed by a two-enzyme system. In the first step, a nondiscriminating ligase (EC 6.1.1.24, glutamate---tRNAGln ligase) mischarges tRNAGln with glutamate, forming glutamyl-tRNAGln. The glutamyl-tRNAGln is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNAGln (glutamyl-tRNAGlu is not a substrate for this enzyme). A glutaminase subunit (cf. EC 3.5.1.2, glutaminase) produces an ammonia molecule that is transferred by a 30 A tunnel to a synthase subunit, where it is ligated to the carboxy group that has been activated by phosphorylation. Some bacterial GatCAB complexes also has the activity of EC 6.3.5.6 (asparaginyl-tRNA synthase [glutamine-hydrolysing]).
CAS REGISTRY NUMBER
COMMENTARY hide
52232-48-1
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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 + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
show the reaction diagram
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?
ATP + Glu-tRNAGln + L-glutamine
ADP + phosphate + Gln-tRNAGln + L-glutamate
show the reaction diagram
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?
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
subunit B
UniProt
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
inactivation of any of the hGatCAB subunits by siRNA-mediated knock down in HeLa cells leads to accumulation of the Glu-charged form of tRNAGln and defects in respiration can be observed
physiological function
inactivation of any of the hGatCAB subunits by siRNA-mediated knock down in HeLa cells leads to accumulation of the Glu-charged form of tRNAGln and defects in respiration can be observed
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GATB_HUMAN
557
0
61864
Swiss-Prot
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
132000
gel filtration, GatABC complex
132000
gel filtration, GatABC complex
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trimer
1 * subunit A plus 1 * subunit B plus 1 * subunit C
trimer
1 * subunit A plus 1 * subunit B plus 1 * subunit C
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nagao, A.; Suzuki, T.; Katoh, T.; Sakaguchi, Y.; Suzuki, T.
Biogenesis of glutaminyl-mt tRNAGln in human mitochondria
Proc. Natl. Acad. Sci. USA
106
16209-16214
2009
Homo sapiens (O43716), Homo sapiens (O75879), Homo sapiens (Q9H0R6)
Manually annotated by BRENDA team