B5FKT0 (THII_SALDC) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 29, 2013.
Version 40.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: tRNA sulfurtransferase EC=2.8.1.4 Alternative name(s): Sulfur carrier protein ThiS sulfurtransferase Thiamine biosynthesis protein ThiI tRNA 4-thiouridine synthase | ||||
| Gene names |
| ||||
| Organism | Salmonella dublin (strain CT_02021853) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 439851 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella › ![]() |
Protein attributes
| Sequence length | 482 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| 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 By similarity. HAMAP-Rule MF_00021 |
| Catalytic activity | L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. HAMAP-Rule MF_00021 [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP. HAMAP-Rule MF_00021 |
| Pathway | Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP-Rule MF_00021 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule MF_00021. |
| Sequence similarities | Belongs to the ThiI family. Contains 1 rhodanese domain. Contains 1 THUMP domain. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Thiamine biosynthesis |
| Cellular component | Cytoplasm |
| Domain | Redox-active center |
| Ligand | ATP-binding Nucleotide-binding RNA-binding tRNA-binding |
| Molecular function | Transferase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | tRNA thio-modification Inferred from electronic annotation. Source: HAMAP thiamine biosynthetic processInferred from electronic annotation. Source: HAMAP thiamine diphosphate biosynthetic processInferred from electronic annotation. Source: UniProtKB-UniPathway thiazole biosynthetic processInferred from electronic annotation. Source: InterPro |
| Cellular_component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: HAMAP sulfurtransferase activityInferred from electronic annotation. Source: HAMAP tRNA bindingInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 482 | 482 | tRNA sulfurtransferase HAMAP-Rule MF_00021 | PRO_1000090028 | |||||||
Regions | |||||||||||
| Domain | 61 – 165 | 105 | THUMP | ||||||||
| Domain | 404 – 482 | 79 | Rhodanese | ||||||||
| Nucleotide binding | 183 – 184 | 2 | ATP By similarity | ||||||||
Sites | |||||||||||
| Active site | 456 | 1 | Cysteine persulfide intermediate By similarity | ||||||||
| Binding site | 265 | 1 | ATP By similarity | ||||||||
| Binding site | 287 | 1 | ATP; via amide nitrogen By similarity | ||||||||
| Binding site | 296 | 1 | ATP By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 344 ↔ 456 | Redox-active By similarity | |||||||||
Sequences
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References
| [1] | "Complete genome of Salmonella dublin strain CT_02021853." Ravel J., Fricke W.F., White D., McDermott P., Mammel M., Rosovitz M., Leclerc J., Cebula T., Sebastian Y. Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: CT_02021853. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP001144 Genomic DNA. Translation: ACH74329.1. |
| RefSeq | YP_002214379.1. NC_011205.1. |
3D structure databases | |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | 439851.SeD_A0466. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblBacteria | ACH74329; ACH74329; SeD_A0466. |
| GeneID | 6871042. |
| KEGG | sed:SeD_A0466. |
| PATRIC | 18489150. VBISalEnt111443_0542. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| eggNOG | COG0301. |
| HOGENOM | HOG000227469. |
| KO | K03151. |
| OMA | KLFPEIM. |
| ProtClustDB | PRK01269. |
Enzyme and pathway databases | |
| BioCyc | SENT439851:GH2Z-459-MONOMER. |
| UniPathway | UPA00060. |
Family and domain databases | |
| Gene3D | 3.40.250.10. 1 hit. 3.40.50.620. 1 hit. |
| HAMAP | MF_00021. ThiI. |
| InterPro | IPR001763. Rhodanese-like_dom. IPR014729. Rossmann-like_a/b/a_fold. IPR026340. Thiazole_biosynth_dom. IPR003720. ThiI. IPR020536. ThiI_C_dom. IPR004114. THUMP. [Graphical view] |
| Pfam | PF02568. ThiI. 1 hit. PF02926. THUMP. 1 hit. [Graphical view] |
| SMART | SM00981. THUMP. 1 hit. [Graphical view] |
| SUPFAM | SSF52821. Rhodanese-like. 1 hit. |
| TIGRFAMs | TIGR04271. ThiI_C_thiazole. 1 hit. TIGR00342. TIGR00342. 1 hit. |
| PROSITE | PS50206. RHODANESE_3. 1 hit. PS51165. THUMP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | THII_SALDC | ||||||||
| Accession | Primary (citable) accession number: B5FKT0 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
