ID A0A5X8YHR5_SALET Unreviewed; 482 AA. AC A0A5X8YHR5; DT 22-APR-2020, integrated into UniProtKB/TrEMBL. DT 22-APR-2020, sequence version 1. DT 17-JUN-2020, entry version 2. DE RecName: Full=tRNA sulfurtransferase {ECO:0000256|SAAS:SAAS01082725}; DE EC=2.8.1.4 {ECO:0000256|SAAS:SAAS00848765}; GN Name=thiI {ECO:0000313|EMBL:ECB1985243.1}; GN ORFNames=EVG56_02110 {ECO:0000313|EMBL:ECB1985243.1}; OS Salmonella enterica subsp. enterica serovar Kisarawe. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=2517242 {ECO:0000313|EMBL:ECB1985243.1}; RN [1] {ECO:0000313|EMBL:ECB1985243.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=508285 {ECO:0000313|EMBL:ECB1985243.1}; RA Ashton P.M., Dallman T., Nair S., De Pinna E., Peters T., Grant K.; 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|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 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|SAAS:SAAS01118926}; 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; CC Evidence={ECO:0000256|SAAS:SAAS01118903}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|SAAS:SAAS00848764}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|SAAS:SAAS00848759}. CC -!- SIMILARITY: Belongs to the ThiI family. CC {ECO:0000256|SAAS:SAAS00848754}. 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:ECB1985243.1}. 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; AAHWUP010000002; ECB1985243.1; -; Genomic_DNA. DR UniPathway; UPA00060; -. DR CDD; cd01712; ThiI; 1. DR Gene3D; 3.40.250.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. 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. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|SAAS:SAAS00426880}; KW Cytoplasm {ECO:0000256|SAAS:SAAS00848768}; KW Disulfide bond {ECO:0000256|SAAS:SAAS01082722}; KW Nucleotide-binding {ECO:0000256|SAAS:SAAS00426907}; KW Redox-active center {ECO:0000256|SAAS:SAAS01082719}; KW RNA-binding {ECO:0000256|SAAS:SAAS00848760}; KW Thiamine biosynthesis {ECO:0000256|SAAS:SAAS00848763}; KW Transferase {ECO:0000256|SAAS:SAAS00848758}; KW tRNA-binding {ECO:0000256|SAAS:SAAS00848757}. FT DOMAIN 75..165 FT /note="THUMP" FT /evidence="ECO:0000259|SMART:SM00981" 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 //