InterPro : IPR003720

Name  tRNA sulfurtransferase ThiI Short Name  tRNA_STrfase
Type  Family Description  tRNA sulfurtransferase ThiI catalyses the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor [, , ]. In some bacteria, ThiI is a bifunctional enzyme required for the synthesis of both the 4-thiouridine modification in tRNA and the thiazole moiety in the thiamine biosynthesis pathway [].Three domains of ThiI are essential for the thiolation of tRNA: a THUMP domain that binds tRNA (see ) [], an AANH domain that activates the uridine residue by adenylylation [], and a rhodanese domain that transfers sulfur to the activated uridine residue []. Neither the THUMP nor the AANH domain of ThiI are essential for thiamine synthesis, only the rhodanese domain is necessary for synthesis of the thiazole moiety of thiamine [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

2 Contains

Id Name Short Name Type
IPR004114 THUMP THUMP Domain
IPR020536 Thil, AANH domain ThiI_AANH Domain

0 Found In

0 Parent Features

6 Publications

First Author Title Year Journal Volume Pages
Webb E Characterization of thiI, a new gene involved in thiazole biosynthesis in Salmonella typhimurium. 1997 J Bacteriol 179 4399-402
Mueller EG The role of the cysteine residues of ThiI in the generation of 4-thiouridine in tRNA. 2001 J Biol Chem 276 33588-95
Waterman DG Crystal structure of Bacillus anthracis ThiI, a tRNA-modifying enzyme containing the predicted RNA-binding THUMP domain. 2006 J Mol Biol 356 97-110
Wright CM Direct evidence for enzyme persulfide and disulfide intermediates during 4-thiouridine biosynthesis. 2006 Chem Commun (Camb)   3104-6
You D Direct evidence that ThiI is an ATP pyrophosphatase for the adenylation of uridine in 4-thiouridine biosynthesis. 2008 Chembiochem 9 1879-82
Martinez-Gomez NC The rhodanese domain of ThiI is both necessary and sufficient for synthesis of the thiazole moiety of thiamine in Salmonella enterica. 2011 J Bacteriol 193 4582-7

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)