CATH Classification
| Level | CATH Code | Description |
|---|---|---|
|
3 | Alpha Beta |
|
3.20 | Alpha-Beta Barrel |
|
3.20.20 | TIM Barrel |
|
3.20.20.105 | Queuine tRNA-ribosyltransferase-like |
Domain Context
CATH Clusters
| Superfamily | Queuine tRNA-ribosyltransferase-like |
| Functional Family | Queuine tRNA-ribosyltransferase |
Enzyme Information
| 2.4.2.29 |
tRNA-guanine(34) transglycosylase.
based on mapping to UniProt P28720
(1) Guanine(34) in tRNA + queuine = queuosine(34) in tRNA + guanine. (2) Guanine(34) in tRNA + 7-aminomethyl-7-carbaguanine = 7-aminomethyl-7- carbaguanine(34) in tRNA + guanine.
-!- Certain prokaryotic and eukaryotic tRNAs contain the modified base queuine at position 34. -!- In eukaryotes queuine is salvaged from food and incorporated into tRNA directly via a base-exchange reaction, replacing guanine. -!- In eubacteria, which produce queuine de novo, the enzyme catalyzes the exchange of guanine with the queuine precursor preQ(1), which is ultimately modified to queuine. -!- The eubacterial enzyme can also use an earlier intermediate, preQ(0), to replace guanine in unmodified tRNA(Tyr) and tRNA(Asn). -!- This enzyme acts after EC 1.7.1.13 in the queuine-biosynthesis pathway.
|
UniProtKB Entries (1)
| P28720 |
TGT_ZYMMO
Zymomonas mobilis subsp. mobilis ZM4 = ATCC 31821
Queuine tRNA-ribosyltransferase
|
PDB Structure
| PDB | 2QZR |
| External Links | |
| Method | X-RAY DIFFRACTION |
| Organism | Escherichia |
| Primary Citation |
Potent Inhibitors of tRNA-Guanine Transglycosylase, an Enzyme Linked to the Pathogenicity of the Shigella Bacterium: Charge-Assisted Hydrogen Bonding.
Angew.Chem.Int.Ed.Engl.
|
