Transferases;
Transferring sulfur-containing groups;
Sulfurtransferases
BRITE hierarchy

[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine:uracil in tRNA sulfurtransferase

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 [RN:R03923]

R03923;
(other) R07461
Reaction

ATP [CPD:C00002];
[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine;
uracil in tRNA [CPD:C00868];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138]

The enzyme, found in bacteria and archaea, is activated by EC 2.8.1.7, cysteine desulfurase, 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.

EC 2.8.1.4 created 1984, modified 2017