CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.30 | 2-Layer Sandwich |
|
3.30.70 | Alpha-Beta Plaits |
|
3.30.70.3550 | Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal domain |
Domain Context
CATH Clusters
| Superfamily | Leucyl/phenylalanyl-tRNA-protein transferase, N-terminal domain |
| Functional Family | Leucyl/phenylalanyl-tRNA--protein transferase |
Enzyme Information
| 2.3.2.6 |
Lysine/arginine leucyltransferase.
based on mapping to UniProt P0A8P1
(1) L-leucyl-tRNA(Leu) + N-terminal L-lysyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-lysyl-[protein]. (2) L-leucyl-tRNA(Leu) + N-terminal L-arginyl-[protein] = tRNA(Leu) + N-terminal L-leucyl-L-arginyl-[protein].
-!- Participates in the N-end rule protein degradation pathway in certain bacteria, by attaching the primary destabilizing residue L-leucine to the N-termini of proteins that have an N-terminal L-arginine or L-lysine residue. -!- Once modified, the proteins are recognized by EC 3.4.21.92. -!- The enzyme also transfers L-phenylalanine in vitro, but this has not been observed in vivo. -!- Cf. EC 2.3.2.8 and EC 2.3.2.29.
|
UniProtKB Entries (1)
| P0A8P1 |
LFTR_ECOLI
Escherichia coli K-12
Leucyl/phenylalanyl-tRNA--protein transferase
|
PDB Structure
| PDB | 2Z3P |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Protein-based peptide-bond formation by aminoacyl-tRNA protein transferase
Nature
|
