ID A0A719X6I9_SALTI Unreviewed; 482 AA. AC A0A719X6I9; DT 02-DEC-2020, integrated into UniProtKB/TrEMBL. DT 02-DEC-2020, sequence version 1. DT 13-SEP-2023, entry version 11. DE RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021}; DE EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021}; 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:HAD7425589.1}; GN ORFNames=G1Y63_10060 {ECO:0000313|EMBL:HAD7425589.1}, G1Y70_10055 GN {ECO:0000313|EMBL:HAD7537039.1}; OS Salmonella enterica subsp. enterica serovar Typhi str. 404ty. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=497977 {ECO:0000313|EMBL:HAD7425589.1}; RN [1] {ECO:0000313|EMBL:HAD7425589.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=404ty {ECO:0000313|EMBL:HAD7425589.1}; RX PubMed=30286803; RA Souvorov A., Agarwala R., Lipman D.J.; RT "SKESA: strategic k-mer extension for scrupulous assemblies."; RL Genome Biol. 19:153-150(2018). RN [2] {ECO:0000313|EMBL:HAD7425589.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=404ty {ECO:0000313|EMBL:HAD7425589.1}; RG NCBI Pathogen Detection Project; RL Submitted (JAN-2019) 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:0000256|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:0000256|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:0000256|HAMAP- CC Rule:MF_00021}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00021}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP- CC Rule:MF_00021}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00021}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HAD7425589.1}. 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; DAAPRH010000006; HAD7425589.1; -; Genomic_DNA. DR EMBL; DAAPSJ010000006; HAD7537039.1; -; Genomic_DNA. DR AlphaFoldDB; A0A719X6I9; -. DR SMR; A0A719X6I9; -. DR UniPathway; UPA00060; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase 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; cd00158; RHOD; 1. DR CDD; cd01712; ThiI; 1. DR CDD; cd11716; THUMP_ThiI; 1. DR Gene3D; 3.30.2130.30; -; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 3.40.250.10; Rhodanese-like domain; 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 NCBIfam; TIGR04271; ThiI_C_thiazole; 1. DR NCBIfam; TIGR00342; tRNA 4-thiouridine(8) synthase ThiI; 1. DR PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1. DR PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 1. DR Pfam; PF02568; ThiI; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1. DR SUPFAM; SSF143437; THUMP domain-like; 1. DR PROSITE; PS50206; RHODANESE_3; 1. DR PROSITE; PS51165; THUMP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00021}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP- KW Rule:MF_00021}; Transferase {ECO:0000256|HAMAP-Rule:MF_00021}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00021}. FT DOMAIN 61..165 FT /note="THUMP" FT /evidence="ECO:0000259|PROSITE:PS51165" FT DOMAIN 404..480 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT ACT_SITE 456 FT /note="Cysteine persulfide intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 183..184 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 265 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 287 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 296 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT DISULFID 344..456 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" SQ SEQUENCE 482 AA; 54777 MW; 718C3AE5C3B1687B CRC64; MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALAQYRE QLEGKTFCVR VKRRGKHEFS SIEVERYVGG GLNQHIESAR VKLTNPDVTV 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 LDIRSVDEQD DKPLKVEGVD VVSLPFYKLS TKFGDLDQSK TWLLWCERGV MSRLQALYLR EQGFANVKVY RP //