ID THII_HISS1 Reviewed; 484 AA. AC Q0I3G4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 1. DT 27-MAR-2024, entry version 100. 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=HS_0902; OS Histophilus somni (strain 129Pt) (Haemophilus somnus). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Histophilus. OX NCBI_TaxID=205914; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=129Pt; RX PubMed=17172329; DOI=10.1128/jb.01422-06; RA Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., RA Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., RA Xie G., Inzana T.J.; RT "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain RT 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus RT influenzae Rd."; RL J. Bacteriol. 189:1890-1898(2007). 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; CP000436; ABI25177.1; -; Genomic_DNA. DR AlphaFoldDB; Q0I3G4; -. DR SMR; Q0I3G4; -. DR KEGG; hso:HS_0902; -. DR eggNOG; COG0301; Bacteria. DR eggNOG; COG0607; Bacteria. DR HOGENOM; CLU_037952_4_1_6; -. 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-uracil-4 sulfurtransferase activity; 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 uracil 4-sulfurtransferase ThiI; 1. DR PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1. DR PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 1. DR Pfam; PF00581; Rhodanese; 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; Cytoplasm; Disulfide bond; Nucleotide-binding; KW Redox-active center; RNA-binding; Thiamine biosynthesis; Transferase; KW tRNA-binding. FT CHAIN 1..484 FT /note="tRNA sulfurtransferase" FT /id="PRO_1000074229" FT DOMAIN 61..165 FT /note="THUMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT DOMAIN 404..484 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 484 AA; 54756 MW; 8D24364396FA415B CRC64; MKFIIKLFPE IMIKSESVRK RFVKILTGNI RNVLNKYDDT VAVVKHWDYI EVRSKNIENR ILLVELLGRI PGIHHFLEVE EKPFVTLHDI FEQTLSDVAT QIENKTFCVR VKRKGKHDFS SLDAERYIGG GLNQAVASAK VQLSKPDVTV RIDIENDKMM LIKARHQGIG GYPIGTQEDV LSLISGGFDS GVSSYMLIRR GSRVHYCFFN LGGATHEIGV KQMAYHIWKR FSGSHKVRFV AINFEQVVAE ILEKVDNGQM GVVLKRMMVR AASKVAQRFG IQAIVTGEAL GQVSSQTLTN LRLIDEAAES LVLRPLITHD KEQIIAKAKE IGTEDIAKSM PEFCGVISKS PTVKAVKEKI EQEESYFDFS VLESAVQNAQ YLDIRQIAEQ TKKEVFEVDE ITVLSANDVI LDIRSPEEVD DKPLEISGQN IILMPFYKLS SHFAELDQSK NYVLYCERGV MSKLQALYLR EKGFDNVKVL NKIS //