A0A6L6ICW1 · A0A6L6ICW1_9ESCH
- ProteintRNA sulfurtransferase
- GenethiI
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids482 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Catalyzes 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. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS.
Catalytic activity
- [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a uridine in tRNA + ATP + H+ + 2 reduced [2Fe-2S]-[ferredoxin] = [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]
- [sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur-carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H+ + L-cysteinyl-[cysteine desulfurase]
Pathway
Cofactor biosynthesis; thiamine diphosphate biosynthesis.
Features
Showing features for binding site, active site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytosol | |
Molecular Function | ATP binding | |
Molecular Function | CCA tRNA nucleotidyltransferase activity | |
Molecular Function | tRNA binding | |
Molecular Function | tRNA-uracil-4 sulfurtransferase activity | |
Biological Process | thiamine biosynthetic process | |
Biological Process | thiamine diphosphate biosynthetic process | |
Biological Process | thiazole biosynthetic process | |
Biological Process | tRNA 4-thiouridine biosynthesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nametRNA sulfurtransferase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Gammaproteobacteria > Enterobacterales > Enterobacteriaceae > Escherichia
Accessions
- Primary accessionA0A6L6ICW1
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for disulfide bond.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Disulfide bond | 344↔456 | Redox-active | ||||
Sequence: CGVISKSPTVKAVKAKIEAEEENFDFSILDRVVEEASNVDIRDIARQAGQETVEVETVSGFGPNDVILDIRAVDEQDDRPLKVEGIDVVSLPFYKLSTQFGDLDQSKTWLLWC |
Keywords
- PTM
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 61-165 | THUMP | ||||
Sequence: LAIRDALTRIPGIHHILEVDDVPFTDMHDIFEKALAQYREQLEGKTFCVRVKRRGKHEFSSIDVERYVGGGLNQHIESARVKLTHPEVTVHLEVEDDRLLLIKGR | ||||||
Domain | 404-480 | Rhodanese | ||||
Sequence: FGPNDVILDIRAVDEQDDRPLKVEGIDVVSLPFYKLSTQFGDLDQSKTWLLWCERGVMSRLQALYLREQGFANVKVY |
Sequence similarities
Belongs to the ThiI family.
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length482
- Mass (Da)54,637
- Last updated2020-10-07 v1
- Checksum53177EEAE5BFB088