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 | Glutamyl-tRNA(Gln) amidotransferase subunit A |
Enzyme Information
6.3.5.7 |
Glutaminyl-tRNA synthase (glutamine-hydrolyzing).
based on mapping to UniProt Q03557
ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate.
-!- In systems lacking discernible 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 reaction). -!- Ammonia or asparagine can substitute for the preferred substrate glutamine.
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UniProtKB Entries (1)
P53260 |
GATF_YEAST
Saccharomyces cerevisiae S288C
Glutamyl-tRNA(Gln) amidotransferase subunit F, mitochondrial
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PDB Structure
PDB | 4N0H |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal structure of Saccharomyces cerevisiae mitochondrial GatFAB reveals a novel subunit assembly in tRNA-dependent amidotransferases
Nucleic Acids Res.
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