(data stored in ACNUC7421 zone)

SWISSPROT: THII_ECODH

ID   THII_ECODH              Reviewed;         482 AA.
AC   B1XF11;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   30-AUG-2017, entry version 66.
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=ECDH10B_0379;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
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   -!- 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; CP000948; ACB01551.1; -; Genomic_DNA.
DR   RefSeq; WP_000668662.1; NC_010473.1.
DR   ProteinModelPortal; B1XF11; -.
DR   SMR; B1XF11; -.
DR   EnsemblBacteria; ACB01551; ACB01551; ECDH10B_0379.
DR   KEGG; ecd:ECDH10B_0379; -.
DR   eggNOG; ENOG4105D8I; Bacteria.
DR   eggNOG; COG0301; LUCA.
DR   eggNOG; COG0607; LUCA.
DR   HOGENOM; HOG000227469; -.
DR   KO; K03151; -.
DR   OMA; KLFPEIM; -.
DR   UniPathway; UPA00060; -.
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   3: Inferred from homology;
DR   PRODOM; B1XF11.
DR   SWISS-2DPAGE; B1XF11.
KW   ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding;
KW   Redox-active center; RNA-binding; Thiamine biosynthesis; Transferase;
KW   tRNA-binding.
FT   CHAIN         1    482       tRNA sulfurtransferase.
FT                                /FTId=PRO_1000090012.
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;  54973 MW;  72AF449459E45762 CRC64;
     MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR
     LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALVQYRD QLEGKTFCVR 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 TEQEVVEVET VNGFGPNDVI LDIRSIDEQE
     DKPLKVEGID VVSLPFYKLS TKFGDLDQNK TWLLWCERGV MSRLQALYLR EQGFNNVKVY
     RP
//

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