(data stored in ACNUC7421 zone)

SWISSPROT: THII_ECO57

ID   THII_ECO57              Reviewed;         482 AA.
AC   Q8XE74;
DT   03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   30-AUG-2017, entry version 106.
DE   RecName: Full=tRNA sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021};
DE            EC=2.8.1.4 {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=tRNA 4-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_00021};
GN   Name=thiI {ECO:0000255|HAMAP-Rule:MF_00021};
GN   OrderedLocusNames=Z0526, ECs0477;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
RN   [3]
RP   INTERACTION WITH ISCS, AND SUBUNIT.
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=20404999; DOI=10.1371/journal.pbio.1000354;
RA   Shi R., Proteau A., Villarroya M., Moukadiri I., Zhang L.,
RA   Trempe J.F., Matte A., Armengod M.E., Cygler M.;
RT   "Structural basis for Fe-S cluster assembly and tRNA thiolation
RT   mediated by IscS protein-protein interactions.";
RL   PLoS Biol. 8:E1000354-E1000354(2010).
CC   -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA
CC       to produce 4-thiouridine in position 8 of tRNAs, which functions
CC       as a near-UV photosensor. Also catalyzes the transfer of sulfur to
CC       the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate.
CC       This is a step in the synthesis of thiazole, in the thiamine
CC       biosynthesis pathway. The sulfur is donated as persulfide by IscS.
CC       {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- CATALYTIC ACTIVITY: ATP + [ThiI sulfur-carrier protein]-S-
CC       sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-
CC       sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI
CC       sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-
CC       sulfur] cluster. {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH +
CC       [ThiS]-COSH + AMP. {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- SUBUNIT: Interacts with IscS. {ECO:0000269|PubMed:20404999}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00021}.
DR   EMBL; AE005174; AAG54773.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33900.1; -; Genomic_DNA.
DR   PIR; A85539; A85539.
DR   PIR; E90688; E90688.
DR   RefSeq; NP_308504.1; NC_002695.1.
DR   RefSeq; WP_000668700.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; Q8XE74; -.
DR   SMR; Q8XE74; -.
DR   DIP; DIP-58576N; -.
DR   STRING; 155864.Z0526; -.
DR   EnsemblBacteria; AAG54773; AAG54773; Z0526.
DR   EnsemblBacteria; BAB33900; BAB33900; BAB33900.
DR   GeneID; 914579; -.
DR   KEGG; ece:Z0526; -.
DR   KEGG; ecs:ECs0477; -.
DR   PATRIC; fig|386585.9.peg.578; -.
DR   eggNOG; ENOG4105D8I; Bacteria.
DR   eggNOG; COG0301; LUCA.
DR   eggNOG; COG0607; LUCA.
DR   HOGENOM; HOG000227469; -.
DR   KO; K03151; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0052837; P:thiazole biosynthetic process; IEA:InterPro.
DR   GO; GO:0034227; P:tRNA thio-modification; IEA:InterPro.
DR   CDD; cd01712; ThiI; 1.
DR   Gene3D; 3.40.250.10; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00021; ThiI; 1.
DR   InterPro; IPR001763; Rhodanese-like_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR026340; Thiazole_biosynth_dom.
DR   InterPro; IPR020536; ThiI_AANH.
DR   InterPro; IPR004114; THUMP_dom.
DR   InterPro; IPR003720; tRNA_STrfase.
DR   Pfam; PF02568; ThiI; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF52821; SSF52821; 1.
DR   TIGRFAMs; TIGR04271; ThiI_C_thiazole; 1.
DR   TIGRFAMs; TIGR00342; TIGR00342; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS51165; THUMP; 1.
PE   1: Evidence at protein level;
DR   PRODOM; Q8XE74.
DR   SWISS-2DPAGE; Q8XE74.
KW   ATP-binding; Complete proteome; Cytoplasm; Disulfide bond;
KW   Nucleotide-binding; Redox-active center; RNA-binding;
KW   Thiamine biosynthesis; Transferase; tRNA-binding.
FT   CHAIN         1    482       tRNA sulfurtransferase.
FT                                /FTId=PRO_0000154838.
FT   DOMAIN       61    165       THUMP. {ECO:0000255|HAMAP-Rule:MF_00021}.
FT   DOMAIN      404    482       Rhodanese. {ECO:0000255|HAMAP-
FT                                Rule:MF_00021}.
FT   NP_BIND     183    184       ATP. {ECO:0000255|HAMAP-Rule:MF_00021}.
FT   ACT_SITE    456    456       Cysteine persulfide intermediate.
FT                                {ECO:0000255|HAMAP-Rule:MF_00021}.
FT   BINDING     265    265       ATP. {ECO:0000255|HAMAP-Rule:MF_00021}.
FT   BINDING     287    287       ATP; via amide nitrogen.
FT                                {ECO:0000255|HAMAP-Rule:MF_00021}.
FT   BINDING     296    296       ATP. {ECO:0000255|HAMAP-Rule:MF_00021}.
FT   DISULFID    344    456       Redox-active. {ECO:0000255|HAMAP-
FT                                Rule:MF_00021}.
SQ   SEQUENCE   482 AA;  55003 MW;  896E83BA0E2A352C CRC64;
     MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR
     LTIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALVQYRD QLDGKTFCVR VKRRGKHDFS
     SIDVERYVGG GLNQHIESAR VKLTNPDVTV HLEVEDDRLL LIKGRYEGIG GFPIGTQEDV
     LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGAAHEIGV RQVAHYLWNR FGSSHRVRFV
     AINFEPVVGE ILEKIDDGQM GVILKRMMVR AASKVAERYG VQALVTGEAL GQVSSQTLTN
     LRLIDNVSDT LILRPLISYD KEHIINLARQ IGTEDFARTM PEYCGVISKS PTVKAVKSKI
     EAEEEKFDFS ILDKVVEEAN NVDIREIAQQ TGQEVVEVET VNDFGPNDVI LDIRSVDEQE
     DKPLKVEGID VVSLPFYKLS TKFGDLDQNR TWLLWCERGV MSRLQALYLR EQGFKNVKVY
     RP
//

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