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Q32JI1 (THII_SHIDS) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 63. 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:SDY_0307
OrganismShigella dysenteriae serotype 1 (strain Sd197) [Reference proteome] [HAMAP]
Taxonomic identifier300267 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482tRNA sulfurtransferase HAMAP-Rule MF_00021
PRO_1000074278

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
Q32JI1 [UniParc].

Last modified December 6, 2005. Version 1.
Checksum: 00FAB35849600966

FASTA48254,962
        10         20         30         40         50         60 
MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR 

        70         80         90        100        110        120 
LTIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALVQYRD QLEGKTFCVR VKRSGKHDFS 

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

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

       250        260        270        280        290        300 
AINFEPVVGE ILEKIDDGQM GVILKRMMVR AASKVAERYG VQALVTGEAL GQVSSQTLTN 

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

       370        380        390        400        410        420 
EAEEEKFDFS ILDKVVEEAN NVDIREIAQQ TEQEVVEVET VNDCGPNDVI LDIRSVDEQE 

       430        440        450        460        470        480 
DKPLKVEGID VVSLPFYKLS TKFGDLDQNR TWLLWCERGV MSRLQALYLR EQGFNNVKVY 


RP 

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References

[1]"Genome dynamics and diversity of Shigella species, the etiologic agents of bacillary dysentery."
Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J., Xu J. expand/collapse author list , Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J., Jin Q.
Nucleic Acids Res. 33:6445-6458(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sd197.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000034 Genomic DNA. Translation: ABB60526.1.
RefSeqYP_402015.1. NC_007606.1.

3D structure databases

ProteinModelPortalQ32JI1.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING300267.SDY_0307.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB60526; ABB60526; SDY_0307.
GeneID3799691.
KEGGsdy:SDY_0307.
PATRIC18689724. VBIShiDys99784_0352.

Phylogenomic databases

eggNOGCOG0301.
HOGENOMHOG000227469.
KOK03151.
OMAKLFPEIM.
OrthoDBEOG6TBHGR.

Enzyme and pathway databases

BioCycSDYS300267:GJEW-306-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_AANH.
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_SHIDS
AccessionPrimary (citable) accession number: Q32JI1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: December 6, 2005
Last modified: July 9, 2014
This is version 63 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