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P55913 (THII_SALTY) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:STM0425
OrganismSalmonella typhimurium
Taxonomic identifier90371 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Salmonella

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 MF_00021

Catalytic activity

L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide. HAMAP MF_00021

[IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP. HAMAP MF_00021

Pathway

Cofactor biosynthesis; thiamine diphosphate biosynthesis. HAMAP MF_00021

Subcellular location

Cytoplasm HAMAP 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
Reference proteome
Gene Ontology (GO)
   Biological processthiamine biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

tRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 482482tRNA sulfurtransferase HAMAP MF_00021
PRO_0000154860

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

Experimental info

Sequence conflict3651E → R in AAB39648. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P55913 [UniParc].

Last modified December 15, 1998. Version 2.
Checksum: 41CC9EE3740CE5D2

FASTA48254,831
        10         20         30         40         50         60 
MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR 

        70         80         90        100        110        120 
LVIRDALTRI 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 EQGFANVKVY 


RP

« Hide

References

« Hide 'large scale' references
[1]"Characterization of thiI, a new gene involved in thiazole biosynthesis in Salmonella typhimurium."
Webb E., Claas K., Downs D.M.
J. Bacteriol. 179:4399-4402(1997) [PubMed: 9209060] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: LT2.
[2]"Complete genome sequence of Salmonella enterica serovar Typhimurium LT2."
McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P., Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D., Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E. expand/collapse author list , Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R., Wilson R.K.
Nature 413:852-856(2001) [PubMed: 11677609] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LT2 / SGSC1412 / ATCC 700720.
[3]Metcalf W.W., Jiang W., Wanner B.L.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 365-482.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		U94901 Genomic DNA. Translation: AAB63031.1.
AE006468 Genomic DNA. Translation: AAL19379.1.
U69493 Genomic DNA. Translation: AAB39648.1.
PIRT46944.
RefSeqNP_459420.1. NC_003197.1.

3D structure databases

ProteinModelPortalP55913.
ModBaseSearch...

Proteomic databases

PRIDEP55913.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1251944.
GenomeReviewsGene locus STM0425 in contig AE006468_GR.
KEGGstm:STM0425.
NMPDRfig|99287.1.peg.410.
PATRIC32379185. VBISalEnt20916_0454.

Phylogenomic databases

HOGENOMHBG646072.
OMAGYPIGTQ.
ProtClustDBPRK01269.

Enzyme and pathway databases

BioCycSTYP99287:STM0425-MONOMER.

Family and domain databases

HAMAPMF_00021. ThiI.
[Tree]
InterProIPR001763. Rhodanese-like.
IPR014729. Rossmann-like_a/b/a_fold.
IPR003720. ThiI.
IPR020536. ThiI_C.
IPR004114. THUMP.
[Graphical view]
Gene3DG3DSA:3.40.250.10. Rhodanese-like. 1 hit.
G3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
KOK03151.
PfamPF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view]
SMARTSM00981. THUMP. 1 hit.
[Graphical view]
SUPFAMSSF52821. Rhodanese-like. 1 hit.
TIGRFAMsTIGR00342. TIGR00342. 1 hit.
PROSITEPS50206. RHODANESE_3. 1 hit.
PS51165. THUMP. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTHII_SALTY
AccessionPrimary (citable) accession number: P55913
Secondary accession number(s): O06955
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: December 15, 1998
Last modified: January 25, 2012
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Uncharacterized protein families (UPF)

List of uncharacterized protein family (UPF) entries

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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