Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

tRNA sulfurtransferase

Gene

thiI

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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

L-cysteine + 'activated' tRNA = L-serine + tRNA containing a thionucleotide.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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei265 – 2651ATPBy similarity
Binding sitei287 – 2871ATP; via amide nitrogenBy similarity
Binding sitei296 – 2961ATPBy similarity
Active sitei456 – 4561Cysteine persulfide intermediate

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi183 – 1842ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-HAMAP
  • sulfurtransferase activity Source: UniProtKB-HAMAP
  • 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: GO_Central
  • tRNA 4-thiouridine biosynthesis Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

Thiamine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding, RNA-binding, tRNA-binding

Enzyme and pathway databases

BioCyciEcoCyc:THII-MONOMER.
ECOL316407:JW0413-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG13273. thiI.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi108 – 1081C → A: No effect. 1 Publication
Mutagenesisi189 – 1891D → A: No activity. 1 Publication
Mutagenesisi202 – 2021C → A: No effect. 1 Publication
Mutagenesisi207 – 2071C → A: Enables partial functional complementation in vivo. Four-fold reduction in activity. 1 Publication
Mutagenesisi321 – 3211K → M: No activity. 1 Publication
Mutagenesisi321 – 3211K → R: Approximately half of wild-type activity. 1 Publication
Mutagenesisi344 – 3441C → A: Cannot functionally complement for wild-type enzyme in vivo. 2700-fold reduction in activity. 1 Publication
Mutagenesisi456 – 4561C → A: No activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 482482tRNA sulfurtransferasePRO_0000154837Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi344 ↔ 456Redox-active1 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

EPDiP77718.
PaxDbiP77718.
PRIDEiP77718.

Interactioni

Protein-protein interaction databases

DIPiDIP-10985N.
IntActiP77718. 12 interactions.
STRINGi511145.b0423.

Structurei

3D structure databases

ProteinModelPortaliP77718.
SMRiP77718. Positions 19-376.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 165105THUMPAdd
BLAST
Domaini404 – 48279RhodaneseAdd
BLAST

Sequence similaritiesi

Belongs to the ThiI family.Curated
Contains 1 rhodanese domain.Curated
Contains 1 THUMP domain.Curated

Keywords - Domaini

Redox-active center

Phylogenomic databases

eggNOGiENOG4105D8I. Bacteria.
COG0301. LUCA.
COG0607. LUCA.
HOGENOMiHOG000227469.
InParanoidiP77718.
KOiK03151.
OMAiKLFPEIM.
PhylomeDBiP77718.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00021. ThiI. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR026340. Thiazole_biosynth_dom.
IPR020536. ThiI_AANH.
IPR004114. THUMP_dom.
IPR003720. tRNA_STrfase.
[Graphical view]
PfamiPF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view]
SMARTiSM00981. THUMP. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
TIGRFAMsiTIGR04271. ThiI_C_thiazole. 1 hit.
TIGR00342. TIGR00342. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS51165. THUMP. 1 hit.
[Graphical view]

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.
PATRICi32115997. VBIEscCol129921_0440.

Cross-referencesi

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.

3D structure databases

ProteinModelPortaliP77718.
SMRiP77718. Positions 19-376.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10985N.
IntActiP77718. 12 interactions.
STRINGi511145.b0423.

Proteomic databases

EPDiP77718.
PaxDbiP77718.
PRIDEiP77718.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC73526; AAC73526; b0423.
BAE76203; BAE76203; BAE76203.
GeneIDi945067.
KEGGiecj:JW0413.
eco:b0423.
PATRICi32115997. VBIEscCol129921_0440.

Organism-specific databases

EchoBASEiEB3058.
EcoGeneiEG13273. thiI.

Phylogenomic databases

eggNOGiENOG4105D8I. Bacteria.
COG0301. LUCA.
COG0607. LUCA.
HOGENOMiHOG000227469.
InParanoidiP77718.
KOiK03151.
OMAiKLFPEIM.
PhylomeDBiP77718.

Enzyme and pathway databases

UniPathwayiUPA00060.
BioCyciEcoCyc:THII-MONOMER.
ECOL316407:JW0413-MONOMER.
MetaCyc:THII-MONOMER.

Miscellaneous databases

PROiP77718.

Family and domain databases

Gene3Di3.40.250.10. 1 hit.
3.40.50.620. 1 hit.
HAMAPiMF_00021. ThiI. 1 hit.
InterProiIPR001763. Rhodanese-like_dom.
IPR014729. Rossmann-like_a/b/a_fold.
IPR026340. Thiazole_biosynth_dom.
IPR020536. ThiI_AANH.
IPR004114. THUMP_dom.
IPR003720. tRNA_STrfase.
[Graphical view]
PfamiPF02568. ThiI. 1 hit.
PF02926. THUMP. 1 hit.
[Graphical view]
SMARTiSM00981. THUMP. 1 hit.
[Graphical view]
SUPFAMiSSF52821. SSF52821. 1 hit.
TIGRFAMsiTIGR04271. ThiI_C_thiazole. 1 hit.
TIGR00342. TIGR00342. 1 hit.
PROSITEiPS50206. RHODANESE_3. 1 hit.
PS51165. THUMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiTHII_ECOLI
AccessioniPrimary (citable) accession number: P77718
Secondary accession number(s): Q2MC03
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 129 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.