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Q3KJG6 (THII_PSEPF) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 68. 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:Pfl01_0346
OrganismPseudomonas fluorescens (strain Pf0-1) [Complete proteome] [HAMAP]
Taxonomic identifier205922 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

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_1000074253

Regions

Domain63 – 167105THUMP
Domain405 – 48379Rhodanese
Nucleotide binding185 – 1862ATP By similarity

Sites

Active site4571Cysteine persulfide intermediate By similarity
Binding site2671ATP By similarity
Binding site2891ATP; via amide nitrogen By similarity
Binding site2981ATP By similarity

Amino acid modifications

Disulfide bond346 ↔ 457Redox-active By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3KJG6 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: ABD3F5C83DDE633C

FASTA48454,193
        10         20         30         40         50         60 
MKLIVKVFPE ITIKSRPVRT KFIRQLAKNI RTVLRDLDPA VVVNGVWDNL ELETRVTDPK 

        70         80         90        100        110        120 
ALKEMGERLT CMPGIAHFLQ IDEYPLGDFD DITEKCKQHY GDALAGKIFS VRCKRAGKHA 

       130        140        150        160        170        180 
FSSMDVEKYV GSKLRRECGA AGIDLKQPEI EVRIEVRDKR LFVIHSQHNG IGGYPLGALE 

       190        200        210        220        230        240 
QTLVLMSGGF DSTVAAYQIL RRGLMTHFCF FNLGGRAHEL GVMEVAHFIW KKYGSSQRVL 

       250        260        270        280        290        300 
FVSVPFEEVL GEILGKVDDS HMGVVLKRMM LRAASSIAER LHIDALVTGE AISQVSSQTL 

       310        320        330        340        350        360 
PNLSVIDCVT DKLVLRPLIV AHKQDIIDTA DQIGTGDFAR HMPEYCGVIS VNPKTAAKRG 

       370        380        390        400        410        420 
RVEHEEQEFD MAVLERALAN ARLVPIDRVI DELGQDLQIE EVSEALAGQI VIDIRHPDAA 

       430        440        450        460        470        480 
EDDPLELAGI EVQTMPFYAV NARFKELDPT RQYLLYCDKG VMSRLHAHHL LSEGHANVRV 


YRPS 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000094 Genomic DNA. Translation: ABA72090.1.
RefSeqYP_346079.1. NC_007492.2.

3D structure databases

ProteinModelPortalQ3KJG6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205922.Pfl01_0346.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABA72090; ABA72090; Pfl01_0346.
GeneID3713374.
KEGGpfo:Pfl01_0346.
PATRIC19882720. VBIPseFlu44242_0347.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0301.
HOGENOMHOG000227469.
KOK03151.
OMAKLFPEIM.
OrthoDBEOG6TBHGR.

Enzyme and pathway databases

BioCycPFLU205922:GJBD-354-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_PSEPF
AccessionPrimary (citable) accession number: Q3KJG6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: November 8, 2005
Last modified: July 9, 2014
This is version 68 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