ID THII_SALAR Reviewed; 482 AA. AC A9MM39; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 14-DEC-2022, entry version 85. 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}; OrderedLocusNames=SARI_02502; OS Salmonella arizonae (strain ATCC BAA-731 / CDC346-86 / RSK2980). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=41514; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-731 / CDC346-86 / RSK2980; RG The Salmonella enterica serovar Arizonae Genome Sequencing Project; RA McClelland M., Sanderson E.K., Porwollik S., Spieth J., Clifton W.S., RA Fulton R., Chunyan W., Wollam A., Shah N., Pepin K., Bhonagiri V., Nash W., RA Johnson M., Thiruvilangam P., Wilson R.; RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to CC produce 4-thiouridine in position 8 of tRNAs, which functions as a CC near-UV photosensor. Also catalyzes the transfer of sulfur to the CC sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a CC step in the synthesis of thiazole, in the thiamine biosynthesis CC pathway. The sulfur is donated as persulfide by IscS. CC {ECO:0000255|HAMAP-Rule:MF_00021}. 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 tRNA + CC AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]; CC Xref=Rhea:RHEA:24176, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, CC Rhea:RHEA-COMP:13337, Rhea:RHEA-COMP:13338, Rhea:RHEA-COMP:13339, CC Rhea:RHEA-COMP:13340, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33737, CC ChEBI:CHEBI:33738, ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, CC ChEBI:CHEBI:136798, ChEBI:CHEBI:456215; EC=2.8.1.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00021}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + AH2 + CC S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur-carrier CC protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L- CC cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:43340, Rhea:RHEA- CC COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12908, Rhea:RHEA- CC COMP:12910, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, CC ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; Evidence={ECO:0000255|HAMAP- CC 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000880; ABX22361.1; -; Genomic_DNA. DR RefSeq; WP_000668639.1; NC_010067.1. DR AlphaFoldDB; A9MM39; -. DR SMR; A9MM39; -. DR STRING; 41514.SARI_02502; -. DR EnsemblBacteria; ABX22361; ABX22361; SARI_02502. DR KEGG; ses:SARI_02502; -. DR HOGENOM; CLU_037952_4_1_6; -. DR OMA; SMPEFCG; -. DR OrthoDB; 773697at2; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000002084; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; 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:0140741; F:tRNA U4 sulfurtransferase; IEA:UniProtKB-EC. 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; Rhodanese/Cell cycle control phosphatase; 1. DR TIGRFAMs; TIGR04271; ThiI_C_thiazole; 1. DR TIGRFAMs; TIGR00342; tRNA sulfurtransferase ThiI; 1. DR PROSITE; PS50206; RHODANESE_3; 1. DR PROSITE; PS51165; THUMP; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding; KW Redox-active center; Reference proteome; RNA-binding; KW Thiamine biosynthesis; Transferase; tRNA-binding. FT CHAIN 1..482 FT /note="tRNA sulfurtransferase" FT /id="PRO_1000074257" FT DOMAIN 61..165 FT /note="THUMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT DOMAIN 404..482 FT /note="Rhodanese" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT ACT_SITE 456 FT /note="Cysteine persulfide intermediate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 183..184 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 265 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 287 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 296 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT DISULFID 344..456 FT /note="Redox-active" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" SQ SEQUENCE 482 AA; 54745 MW; DD22EE603796F147 CRC64; MKFIIKLFPE ITIKSQSVRL RFIKILAGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALAQYRE QLEGKTFCVR VKRRGKHEFS SIEVERYVGG GLNQHIESAR VKLANPDVTV HLEVEDDRLL LIKGRYEGIG GFPIGTQEDV LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGAAHEIGV RQVAHYLWNR FGSSHRVRFV AINFEPVVGE ILEKVDDGQM GVVLKRMMVR AASKVAERYG VQALVTGEAL GQVSSQTLTN LRLIDNVSDT LILRPLISYD KEHIINLARQ IGTEDFARTM PEYCGVISKS PTVKAIKAKI EAEEENFDFS ILDKVVEEAN NVDIREIAQQ TQQEVVEVET VSGFGANDVI LDIRSIDEQD DKPLKVEGID VVSLPFYKLS TKFGDLDQSK TWLLWCERGV MSRLQALYLR EQGFANVKVY RP //