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A9QZR9 (THII_YERPG) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 53. 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:YpAngola_A3070
OrganismYersinia pestis bv. Antiqua (strain Angola) [Complete proteome] [HAMAP]
Taxonomic identifier349746 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeYersinia

Protein attributes

Sequence length483 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 – 483483tRNA sulfurtransferase HAMAP-Rule MF_00021
PRO_1000090047

Regions

Domain62 – 166105THUMP
Domain405 – 48379Rhodanese
Nucleotide binding184 – 1852ATP By similarity

Sites

Active site4571Cysteine persulfide intermediate By similarity
Binding site2661ATP By similarity
Binding site2881ATP; via amide nitrogen By similarity
Binding site2971ATP By similarity

Amino acid modifications

Disulfide bond345 ↔ 457Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
A9QZR9 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: B773AAF42D9895BD

FASTA48354,894
        10         20         30         40         50         60 
MKFIIKLFPE ITIKSQSVRL RFIKILTTNI RNVLKHLEDD TLAIVRHWDH IELRTKDDNL 

        70         80         90        100        110        120 
GPEICDALTR IPGIHHILEV EDRSYSDMHN IFEQTLEAYR ETLVGKTFCV RVKRRGKHEF 

       130        140        150        160        170        180 
SSGDVERYVG GGLNQHIESA KVNLTRPQVT VNLEVDQDKL ILVKARHEGL GGFPIGTQED 

       190        200        210        220        230        240 
VLSLISGGFD SGVSSYMLMR RGCRVHYCFF NLGGSAHEIG VKQVAHYLWN RFGSSHRVRF 

       250        260        270        280        290        300 
IAIDFEPVVG EILEKVEDGQ MGVVLKRMMV RAASQVAERY GVQALVTGEA LGQVSSQTLT 

       310        320        330        340        350        360 
NLRLIDNASD TLILRPLISH DKEHIINLAR QIGTEDFAKT MPEYCGVISK SPTVKAVKAK 

       370        380        390        400        410        420 
IEEEESHFDF SILDRVVSEA KNVDIREIAQ QSREQVVEVE TVAELADTDV LLDIRAPDEQ 

       430        440        450        460        470        480 
EEKPLKLDQV EVRSLPFYKL SSQFADLDQS KTYLLYCDRG VMSRLQALYL REQGYTNVKV 


YRP 

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References

[1]"Genome sequence of the deep-rooted Yersinia pestis strain Angola reveals new insights into the evolution and pangenome of the plague bacterium."
Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y., Mou S., Achtman M., Lindler L.E., Ravel J.
J. Bacteriol. 192:1685-1699(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Angola.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000901 Genomic DNA. Translation: ABX88049.1.
RefSeqYP_001607436.1. NC_010159.1.

3D structure databases

ProteinModelPortalA9QZR9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING349746.YpAngola_A3070.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX88049; ABX88049; YpAngola_A3070.
GeneID5801543.
KEGGypg:YpAngola_A3070.
PATRIC18575696. VBIYerPes97331_3611.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0301.
HOGENOMHOG000227469.
KOK03151.
OMAKLFPEIM.
OrthoDBEOG6TBHGR.

Enzyme and pathway databases

BioCycYPES349746:GHPB-3077-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_YERPG
AccessionPrimary (citable) accession number: A9QZR9
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 5, 2008
Last modified: July 9, 2014
This is version 53 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