(data stored in ACNUC10821 zone)

SWISSPROT: C8U2A7_ECO10

ID   C8U2A7_ECO10            Unreviewed;       482 AA.
AC   C8U2A7;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 77.
DE   RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS01082725};
DE            EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848765};
DE   AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=tRNA 4-thiouridine synthase {ECO:0000256|HAMAP-Rule:MF_00021};
GN   Name=thiI {ECO:0000256|HAMAP-Rule:MF_00021,
GN   ECO:0000313|EMBL:BAI29265.1};
GN   OrderedLocusNames=ECO103_0397 {ECO:0000313|EMBL:BAI29265.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI29265.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI29265.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
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:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848766}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[ThiI sulfur-carrier protein]-S-sulfanyl-L-cysteine + a
CC         uridine in tRNA + ATP + H(+) + 2 reduced [2Fe-2S]-[ferredoxin] =
CC         [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in
CC         tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:24176, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, Rhea:RHEA-COMP:13337, Rhea:RHEA-COMP:13338,
CC         Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13340, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:61963,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:136798, ChEBI:CHEBI:456215;
CC         EC=2.8.1.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00021,
CC         ECO:0000256|SAAS:SAAS01118926};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP +
CC         AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP +
CC         H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:43340,
CC         Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-
CC         COMP:12908, Rhea:RHEA-COMP:12910, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|HAMAP-Rule:MF_00021,
CC         ECO:0000256|SAAS:SAAS01118903};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848764}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021,
CC       ECO:0000256|SAAS:SAAS00848759}.
CC   -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00021, ECO:0000256|SAAS:SAAS00848754}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00021}.
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DR   EMBL; AP010958; BAI29265.1; -; Genomic_DNA.
DR   RefSeq; WP_000668685.1; NC_013353.1.
DR   SMR; C8U2A7; -.
DR   EnsemblBacteria; BAI29265; BAI29265; ECO103_0397.
DR   KEGG; eoh:ECO103_0397; -.
DR   HOGENOM; HOG000227469; -.
DR   KO; K03151; -.
DR   OMA; KLFPEIM; -.
DR   BioCyc; ECOL585395:ECO103_RS02080-MONOMER; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000000959; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-UniRule.
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:UniProtKB-UniRule.
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; IPR036873; Rhodanese-like_dom_sf.
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; C8U2A7.
DR   SWISS-2DPAGE; C8U2A7.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00426880};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848768};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS01082722};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00426907};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS01082719};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|PROSITE-
KW   ProRule:PRU00529, ECO:0000256|SAAS:SAAS00848760};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848763};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848758, ECO:0000313|EMBL:BAI29265.1};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848757}.
FT   DOMAIN       61    165       THUMP. {ECO:0000259|PROSITE:PS51165}.
FT   DOMAIN      404    482       Rhodanese. {ECO:0000259|PROSITE:PS50206}.
FT   NP_BIND     183    184       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   ACT_SITE    456    456       Cysteine persulfide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     265    265       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     287    287       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     296    296       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   DISULFID    344    456       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00021}.
SQ   SEQUENCE   482 AA;  55015 MW;  F44C4A64889486A9 CRC64;
     MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR
     LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALVQYRD QLEGKTFCVR VKRRGKHDFS
     SIDVERYVGG GLNQHIESAR VKLTNPEVTV 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 TKFGDLDQNR TWLLWCERGV MSRLQALYLR EQGFNNVKVY
     RP
//

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