KEGG   ENZYME: 2.8.1.4Help
Entry
EC 2.8.1.4                  Enzyme                                 

Name
tRNA uracil 4-sulfurtransferase;
thiI (gene name);
transfer ribonucleate sulfurtransferase (ambiguous);
RNA sulfurtransferase (ambiguous);
ribonucleate sulfurtransferase (ambiguous);
transfer RNA sulfurtransferase (ambiguous);
transfer RNA thiolase (ambiguous);
L-cysteine:tRNA sulfurtransferase (incorrect);
tRNA sulfurtransferase (ambiguous)
Class
Transferases;
Transferring sulfur-containing groups;
Sulfurtransferases
BRITE hierarchy
Sysname
[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine:uracil in tRNA sulfurtransferase
Reaction(IUBMB)
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]
Reaction(KEGG)
Substrate
ATP [CPD:C00002];
[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine;
uracil in tRNA [CPD:C00868];
reduced ferredoxin [iron-sulfur] cluster [CPD:C00138]
Product
AMP [CPD:C00020];
diphosphate [CPD:C00013];
4-thiouracil in tRNA;
[ThiI sulfur-carrier protein]-L-cysteine;
oxidized ferredoxin [iron-sulfur] cluster [CPD:C00139]
Comment
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.
History
EC 2.8.1.4 created 1984, modified 2017
Reference
1  [PMID:5541999]
  Authors
Abrell JW, Kaufman EE, Lipsett MN.
  Title
The biosynthesis of 4-thiouridylate. Separation and purification of two enzymes in the transfer ribonucleic acid-sulfurtransferase system.
  Journal
J. Biol. Chem. 246 (1971) 294-301.
Reference
2  [PMID:5334200]
  Authors
Hayward RS, Weiss SB.
  Title
RNA thiolase: the enzymatic transfer of sulfur from cysteine to sRNA in Escherichia coli extracts.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 55 (1966) 1161-8.
Reference
3  [PMID:5334201]
  Authors
Lipsett MN, Peterkofsky A.
  Title
Enzymatic thiolation of E. coli sRNA.
  Journal
Proc. Natl. Acad. Sci. U. S. A. 55 (1966) 1169-74.
Reference
4  [PMID:4987417]
  Authors
Wong TW, Weiss SB, Eliceiri GL, Bryant J.
  Title
Ribonucleic acid sulfurtransferase from Bacillus subtilis W168. Sulfuration with beta-mercaptopyruvate and properties of the enzyme system.
  Journal
Biochemistry. 9 (1970) 2376-86.
Reference
5  [PMID:10753862]
  Authors
Kambampati R, Lauhon CT
  Title
Evidence for the transfer of sulfane sulfur from IscS to ThiI during the in vitro biosynthesis of 4-thiouridine in Escherichia coli tRNA.
  Journal
J. Biol. Chem. 275 (2000) 10727-30.
Reference
6  [PMID:11443125]
  Authors
Mueller EG, Palenchar PM, Buck CJ
  Title
The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA.
  Journal
J. Biol. Chem. 276 (2001) 33588-95.
Reference
7  [PMID:15037613]
  Authors
Lauhon CT, Erwin WM, Ton GN
  Title
Substrate specificity for 4-thiouridine modification in Escherichia coli.
  Journal
J. Biol. Chem. 279 (2004) 23022-9.
Reference
8  [PMID:24705700]
  Authors
Neumann P, Lakomek K, Naumann PT, Erwin WM, Lauhon CT, Ficner R
  Title
Crystal structure of a 4-thiouridine synthetase-RNA complex reveals specificity of tRNA U8 modification.
  Journal
Nucleic. Acids. Res. 42 (2014) 6673-85.
Reference
9  [PMID:27791189]
  Authors
Liu Y, Vinyard DJ, Reesbeck ME, Suzuki T, Manakongtreecheep K, Holland PL, Brudvig GW, Soll D
  Title
A [3Fe-4S] cluster is required for tRNA thiolation in archaea and eukaryotes.
  Journal
Proc. Natl. Acad. Sci. U. S. A.  (2016) .
Other DBs
ExplorEnz - The Enzyme Database: 
IUBMB Enzyme Nomenclature: 
ExPASy - ENZYME nomenclature database: 
BRENDA, the Enzyme Database: 
CAS: 
9055-57-6

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