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Q0I3G4 (THII_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 61. 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:HS_0902
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length484 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 – 484484tRNA sulfurtransferase HAMAP-Rule MF_00021
PRO_1000074229

Regions

Domain61 – 165105THUMP
Domain404 – 48481Rhodanese
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
Q0I3G4 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 8D24364396FA415B

FASTA48454,756
        10         20         30         40         50         60 
MKFIIKLFPE IMIKSESVRK RFVKILTGNI RNVLNKYDDT VAVVKHWDYI EVRSKNIENR 

        70         80         90        100        110        120 
ILLVELLGRI PGIHHFLEVE EKPFVTLHDI FEQTLSDVAT QIENKTFCVR VKRKGKHDFS 

       130        140        150        160        170        180 
SLDAERYIGG GLNQAVASAK VQLSKPDVTV RIDIENDKMM LIKARHQGIG GYPIGTQEDV 

       190        200        210        220        230        240 
LSLISGGFDS GVSSYMLIRR GSRVHYCFFN LGGATHEIGV KQMAYHIWKR FSGSHKVRFV 

       250        260        270        280        290        300 
AINFEQVVAE ILEKVDNGQM GVVLKRMMVR AASKVAQRFG IQAIVTGEAL GQVSSQTLTN 

       310        320        330        340        350        360 
LRLIDEAAES LVLRPLITHD KEQIIAKAKE IGTEDIAKSM PEFCGVISKS PTVKAVKEKI 

       370        380        390        400        410        420 
EQEESYFDFS VLESAVQNAQ YLDIRQIAEQ TKKEVFEVDE ITVLSANDVI LDIRSPEEVD 

       430        440        450        460        470        480 
DKPLEISGQN IILMPFYKLS SHFAELDQSK NYVLYCERGV MSKLQALYLR EKGFDNVKVL 


NKIS 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25177.1.
RefSeqYP_719112.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I3G4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_0902.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI25177; ABI25177; HS_0902.
GeneID4240394.
KEGGhso:HS_0902.
PATRIC20281817. VBIHaeSom53361_0945.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0301.
HOGENOMHOG000227469.
KOK03151.
OMAKLFPEIM.
OrthoDBEOG6TBHGR.
ProtClustDBPRK01269.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-935-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_HISS1
AccessionPrimary (citable) accession number: Q0I3G4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: October 3, 2006
Last modified: February 19, 2014
This is version 61 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