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B5FKT0 (THII_SALDC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Name:thiI
Ordered Locus Names:SeD_A0466
OrganismSalmonella dublin (strain CT_02021853) [Complete proteome] [HAMAP]
Taxonomic identifier439851 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length482 AA.
Sequence statusComplete.
Protein existenceInferred 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 processThiamine biosynthesis
   Cellular componentCytoplasm
   DomainRedox-active center
   LigandATP-binding
Nucleotide-binding
RNA-binding
tRNA-binding
   Molecular functionTransferase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processtRNA thio-modification

Inferred from electronic annotation. Source: UniProtKB-HAMAP

thiamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

thiamine diphosphate biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

thiazole biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

sulfurtransferase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482tRNA sulfurtransferase HAMAP-Rule MF_00021
PRO_1000090028

Regions

Domain61 – 165105THUMP
Domain404 – 48279Rhodanese
Nucleotide binding183 – 1842ATP By similarity

Sites

Active site4561Cysteine persulfide intermediate By similarity
Binding site2651ATP By similarity
Binding site2871ATP; via amide nitrogen By similarity
Binding site2961ATP By similarity

Amino acid modifications

Disulfide bond344 ↔ 456Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
B5FKT0 [UniParc].

Last modified October 14, 2008. Version 1.
Checksum: C5904AE5D6B17D68

FASTA48254,861
        10         20         30         40         50         60 
MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR 

        70         80         90        100        110        120 
LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALAQYRE QLEGKTFCVR VKRRGKHEFS 

       130        140        150        160        170        180 
SIEVERYVGG GLNQHIESAR VKLTNPDVTV HLEVEDDRLL LIKGRYEGIG GFPIGTQEDV 

       190        200        210        220        230        240 
LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGAAHEIGV RQVAHYLWNR FGSSHRVRFV 

       250        260        270        280        290        300 
AINFEPVVGE ILEKVDDGQM GVVLKRMMVR AASKVAERYG VQALVTGEAL GQVSSQTLTN 

       310        320        330        340        350        360 
LRLIDNVSDT LILRPLISYD KEHIINLARQ IGTEDFARTM PEYCGVISKS PTVKAIKAKI 

       370        380        390        400        410        420 
EAEEENFDFS ILDKVVEEAN NVDIREIAQQ TQQEVVEVET VSGFGPNDVI LDIRSVDEQD 

       430        440        450        460        470        480 
DKPLKVEGVD VVSLPFYKLS TKFGDLDQSK TWLLWCERGV MSRLQALYLR EQGFENVKVY 


RP 

« Hide

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.
RefSeqYP_002214379.1. NC_011205.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING439851.SeD_A0466.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACH74329; ACH74329; SeD_A0466.
PATRIC18489150. VBISalEnt111443_0542.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0301.
HOGENOMHOG000227469.
OMAKLFPEIM.
OrthoDBEOG6TBHGR.
ProtClustDBPRK01269.

Enzyme and pathway databases

BioCycSENT439851:GH2Z-459-MONOMER.
UniPathwayUPA00060.

Family and domain databases

Gene3D3.40.250.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPMF_00021. ThiI.
InterProIPR001763. Rhodanese-like_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR026340. Thiazole_biosynth_dom.
IPR020536. ThiI_C_dom.
IPR004114. THUMP.
IPR003720. tRNA_STrfase.
[Graphical view]
PfamPF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view]
SMARTSM00981. THUMP. 1 hit.
[Graphical view]
SUPFAMSSF52821. SSF52821. 1 hit.
TIGRFAMsTIGR04271. ThiI_C_thiazole. 1 hit.
TIGR00342. TIGR00342. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS51165. THUMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHII_SALDC
AccessionPrimary (citable) accession number: B5FKT0
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: October 14, 2008
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways