CATH Classification

Domain Context

CATH Clusters

Superfamily HUPs
Functional Family Probable tRNA sulfurtransferase

Enzyme Information

2.8.1.4
tRNA uracil 4-sulfurtransferase.
based on mapping to UniProt Q9X220
ATP + [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-sulfur] cluster.
-!- The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, which transfers a sulfur atom to an internal L-cysteine residue, forming a cysteine persulfide. -!- The activated enzyme then transfers the sulfur to a uridine in a tRNA chain in a reaction that requires ATP. -!- The enzyme from the bacterium Escherichia coli forms 4-thiouridine only at position 8 of tRNA. -!- The enzyme also participates in the biosynthesis of the thiazole moiety of thiamine, but different domains are involved in the two processes.

UniProtKB Entries (1)

Q9X220
THII_THEMA
Thermotoga maritima MSB8
Probable tRNA sulfurtransferase

PDB Structure

PDB 4KR9
External Links
Method X-RAY DIFFRACTION
Organism
Primary Citation
Crystal structure of a 4-thiouridine synthetase-RNA complex reveals specificity of tRNA U8 modification.
Neumann, P., Lakomek, K., Naumann, P.T., Erwin, W.M., Lauhon, C.T., Ficner, R.
Nucleic Acids Res.