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Protein

tRNA sulfurtransferase

Gene

thiI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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.3 Publications

Catalytic activityi

ATP + [ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-sulfur] cluster.1 Publication
[IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH + AMP.1 Publication

Kineticsi

  1. KM=0.24 mM for ATP1 Publication
  2. KM=0.84 mM for GTP1 Publication
  1. Vmax=1.9 nmol/min/mg enzyme with ATP as cosubstrate1 Publication
  2. Vmax=1.29 nmol/min/mg enzyme with GTP as cosubstrate1 Publication

Pathwayi: thiamine diphosphate biosynthesis

This protein is involved in the pathway thiamine diphosphate biosynthesis, which is part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the pathway thiamine diphosphate biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei265ATPBy similarity1
Binding sitei287ATP; via amide nitrogenBy similarity1
Binding sitei296ATPBy similarity1
Active sitei456Cysteine persulfide intermediate1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi183 – 184ATPBy similarity2

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • sulfurtransferase activity Source: InterPro
  • tRNA adenylyltransferase activity Source: InterPro
  • tRNA binding Source: EcoCyc

GO - Biological processi

  • thiamine biosynthetic process Source: EcoCyc
  • thiamine diphosphate biosynthetic process Source: UniProtKB-UniPathway
  • thiazole biosynthetic process Source: InterPro
  • tRNA 4-thiouridine biosynthesis Source: EcoCyc

Keywordsi

Molecular functionRNA-binding, Transferase, tRNA-binding
Biological processThiamine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:THII-MONOMER
MetaCyc:THII-MONOMER
UniPathwayiUPA00060

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:thiI
Synonyms:yajK
Ordered Locus Names:b0423, JW0413
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13273 thiI

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi108C → A: No effect. 1 Publication1
Mutagenesisi189D → A: No activity. 1 Publication1
Mutagenesisi202C → A: No effect. 1 Publication1
Mutagenesisi207C → A: Enables partial functional complementation in vivo. Four-fold reduction in activity. 1 Publication1
Mutagenesisi321K → M: No activity. 1 Publication1
Mutagenesisi321K → R: Approximately half of wild-type activity. 1 Publication1
Mutagenesisi344C → A: Cannot functionally complement for wild-type enzyme in vivo. 2700-fold reduction in activity. 1 Publication1
Mutagenesisi456C → A: No activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001548371 – 482tRNA sulfurtransferaseAdd BLAST482

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi344 ↔ 456Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP77718
PaxDbiP77718
PRIDEiP77718

Interactioni

Protein-protein interaction databases

BioGridi4263344, 4 interactors
DIPiDIP-10985N
IntActiP77718, 13 interactors
STRINGi316385.ECDH10B_0379

Structurei

3D structure databases

ProteinModelPortaliP77718
SMRiP77718
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini61 – 165THUMPAdd BLAST105
Domaini404 – 482RhodaneseAdd BLAST79

Sequence similaritiesi

Belongs to the ThiI family.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105D8I Bacteria
COG0301 LUCA
COG0607 LUCA
HOGENOMiHOG000227469
InParanoidiP77718
KOiK03151
OMAiKLFPEIM
PhylomeDBiP77718

Family and domain databases

CDDicd01712 ThiI, 1 hit
Gene3Di3.40.250.10, 1 hit
3.40.50.620, 1 hit
HAMAPiMF_00021 ThiI, 1 hit
InterProiView protein in InterPro
IPR001763 Rhodanese-like_dom
IPR036873 Rhodanese-like_dom_sf
IPR014729 Rossmann-like_a/b/a_fold
IPR026340 Thiazole_biosynth_dom
IPR020536 ThiI_AANH
IPR004114 THUMP_dom
IPR003720 tRNA_STrfase
PfamiView protein in Pfam
PF02568 ThiI, 1 hit
PF02926 THUMP, 1 hit
SMARTiView protein in SMART
SM00981 THUMP, 1 hit
SUPFAMiSSF52821 SSF52821, 1 hit
TIGRFAMsiTIGR04271 ThiI_C_thiazole, 1 hit
TIGR00342 TIGR00342, 1 hit
PROSITEiView protein in PROSITE
PS50206 RHODANESE_3, 1 hit
PS51165 THUMP, 1 hit

Sequencei

Sequence statusi: Complete.

P77718-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI
60 70 80 90 100
EVRAKDENQR LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALVQYRD
110 120 130 140 150
QLEGKTFCVR VKRRGKHDFS SIDVERYVGG GLNQHIESAR VKLTNPDVTV
160 170 180 190 200
HLEVEDDRLL LIKGRYEGIG GFPIGTQEDV LSLISGGFDS GVSSYMLMRR
210 220 230 240 250
GCRVHYCFFN LGGAAHEIGV RQVAHYLWNR FGSSHRVRFV AINFEPVVGE
260 270 280 290 300
ILEKIDDGQM GVILKRMMVR AASKVAERYG VQALVTGEAL GQVSSQTLTN
310 320 330 340 350
LRLIDNVSDT LILRPLISYD KEHIINLARQ IGTEDFARTM PEYCGVISKS
360 370 380 390 400
PTVKAVKSKI EAEEEKFDFS ILDKVVEEAN NVDIREIAQQ TEQEVVEVET
410 420 430 440 450
VNGFGPNDVI LDIRSIDEQE DKPLKVEGID VVSLPFYKLS TKFGDLDQNK
460 470 480
TWLLWCERGV MSRLQALYLR EQGFNNVKVY RP
Length:482
Mass (Da):54,973
Last modified:February 1, 1997 - v1
Checksum:i72AF449459E45762
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U82664 Genomic DNA Translation: AAB40179.1
U00096 Genomic DNA Translation: AAC73526.1
AP009048 Genomic DNA Translation: BAE76203.1
U34923 Genomic DNA No translation available.
PIRiG64771
RefSeqiNP_414957.1, NC_000913.3
WP_000668662.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC73526; AAC73526; b0423
BAE76203; BAE76203; BAE76203
GeneIDi945067
KEGGiecj:JW0413
eco:b0423
PATRICifig|1411691.4.peg.1854

Similar proteinsi

Entry informationi

Entry nameiTHII_ECOLI
AccessioniPrimary (citable) accession number: P77718
Secondary accession number(s): Q2MC03
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: March 28, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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