CATH Classification
Level | CATH Code | Description |
---|---|---|
2 | Mainly Beta | |
2.40 | Beta Barrel | |
2.40.50 | OB fold (Dihydrolipoamide Acetyltransferase, E2P) | |
2.40.50.140 | Nucleic acid-binding proteins |
Domain Context
CATH Clusters
Superfamily | Nucleic acid-binding proteins |
Functional Family |
Enzyme Information
6.1.1.23 |
Aspartate--tRNA(Asn) ligase.
based on mapping to UniProt Q5SIC2
ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-aspartyl-tRNA(Asx).
-!- When this enzyme acts on tRNA(Asp), it catalyzes the same reaction as EC 6.1.1.12. -!- It has, however, diminished discrimination, so that it can also form aspartyl-tRNA(Asn). -!- 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, Thermus thermophilus, to recognize both tRNA(Asp) (GUC anticodon) and tRNA(Asn) (GUU anticodon). -!- The aspartate-tRNA(Asn) is not used in protein synthesis until it is converted by EC 6.3.5.6 into asparaginyl-tRNA(Asn).
|
UniProtKB Entries (1)
Q5SIC2 |
SYDND_THET8
Thermus thermophilus HB8
Aspartate--tRNA(Asp/Asn) ligase
|
PDB Structure
PDB | 3KFU |
External Links | |
Method | X-RAY DIFFRACTION |
Organism | |
Primary Citation |
Crystal structure of a transfer-ribonucleoprotein particle that promotes asparagine formation.
Embo J.
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