CATH Classification
Level | CATH Code | Description |
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3 | Alpha Beta |
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3.90 | Alpha-Beta Complex |
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3.90.1300 | Amidase signature (AS) enzymes |
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3.90.1300.10 | Amidase signature (AS) domain |
Domain Context
CATH Clusters
Superfamily | Amidase signature (AS) domain |
Functional Family |
Enzyme Information
6.3.5.7 |
Glutaminyl-tRNA synthase (glutamine-hydrolyzing).
based on mapping to UniProt O66610
ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
-!- In systems lacking discernible glutamine--tRNA ligase (EC 6.1.1.18), glutaminyl-tRNA(Gln) is formed by a two-enzyme system. -!- In the first step, a nondiscriminating ligase (EC 6.1.1.24) mischarges tRNA(Gln) with glutamate, forming glutamyl-tRNA(Gln). -!- The glutamyl-tRNA(Gln) is not used in protein synthesis until the present enzyme converts it into glutaminyl-tRNA(Gln) (glutamyl- tRNA(Glu) is not a substrate for this enzyme). -!- A glutaminase subunit (cf. EC 3.5.1.2) 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.
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UniProtKB Entries (1)
O66766 |
GATB_AQUAE
Aquifex aeolicus VF5
Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B
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PDB Structure
PDB | 3H0M |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Insights into tRNA-Dependent Amidotransferase Evolution and Catalysis from the Structure of the Aquifex aeolicus Enzyme
J.Mol.Biol.
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