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 08-MAY-2019, entry version 75. 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=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., RA Nash W., 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 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: 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:0000255|HAMAP-Rule:MF_00021}; 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: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}. 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 SMR; A9MM39; -. DR EnsemblBacteria; ABX22361; ABX22361; SARI_02502. DR KEGG; ses:SARI_02502; -. DR eggNOG; ENOG4105D8I; Bacteria. DR eggNOG; COG0301; LUCA. DR eggNOG; COG0607; LUCA. DR HOGENOM; HOG000227469; -. DR KO; K03151; -. DR OMA; KLFPEIM; -. DR OrthoDB; 773697at2; -. DR BioCyc; SENT882884:G1GAH-2459-MONOMER; -. 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: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; KW ATP-binding; Complete proteome; Cytoplasm; Disulfide bond; KW Nucleotide-binding; Redox-active center; Reference proteome; KW RNA-binding; Thiamine biosynthesis; Transferase; tRNA-binding. FT CHAIN 1 482 tRNA sulfurtransferase. FT /FTId=PRO_1000074257. 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; 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 //