ID THII_MOOTA Reviewed; 390 AA. AC Q2RM06; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2006, sequence version 1. DT 02-SEP-2026, entry version 108. DE RecName: Full=Probable 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=Moth_0198; OS Moorella thermoacetica (strain ATCC 39073 / JCM 9320). OC Bacteria; Bacillati; Bacillota; Clostridia; Neomoorellales; OC Neomoorellaceae; Neomoorella. OX NCBI_TaxID=264732; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 39073 / JCM 9320; RX PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x; RA Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C., RA Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.; RT "The complete genome sequence of Moorella thermoacetica (f. Clostridium RT thermoaceticum)."; RL Environ. Microbiol. 10:2550-2573(2008). 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 + 2 reduced [2Fe-2S]-[ferredoxin] + ATP + H(+) = CC [ThiI sulfur-carrier protein]-L-cysteine + a 4-thiouridine in tRNA + CC 2 oxidized [2Fe-2S]-[ferredoxin] + AMP + diphosphate; 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=[ThiS sulfur-carrier protein]-C-terminal Gly-Gly-AMP + S- CC sulfanyl-L-cysteinyl-[cysteine desulfurase] + AH2 = [ThiS sulfur- CC carrier protein]-C-terminal-Gly-aminoethanethioate + L-cysteinyl- CC [cysteine desulfurase] + A + AMP + 2 H(+); Xref=Rhea:RHEA:43340, CC Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12910, CC Rhea:RHEA-COMP:19908, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, CC ChEBI:CHEBI:90618, ChEBI:CHEBI:232372, ChEBI:CHEBI:456215; CC 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; CP000232; ABC18533.1; -; Genomic_DNA. DR AlphaFoldDB; Q2RM06; -. DR SMR; Q2RM06; -. DR STRING; 264732.Moth_0198; -. DR EnsemblBacteria; ABC18533; ABC18533; Moth_0198. DR KEGG; mta:Moth_0198; -. DR PATRIC; fig|264732.11.peg.210; -. DR eggNOG; COG0301; Bacteria. DR HOGENOM; CLU_037952_4_0_9; -. DR OrthoDB; 9773948at2; -. DR UniPathway; UPA00060; -. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. 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:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:TreeGrafter. DR GO; GO:0002937; P:tRNA 4-thiouridine biosynthesis; IEA:TreeGrafter. DR CDD; cd01712; PPase_ThiI; 1. DR CDD; cd11716; THUMP_ThiI; 1. DR FunFam; 3.40.50.620:FF:000053; Probable tRNA sulfurtransferase; 1. DR Gene3D; 3.30.2130.30; -; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR HAMAP; MF_00021; ThiI; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR020536; ThiI_AANH. DR InterPro; IPR054173; ThiI_fer. DR InterPro; IPR049961; ThiI_N. DR InterPro; IPR004114; THUMP_dom. DR InterPro; IPR049962; THUMP_ThiI. DR InterPro; IPR003720; tRNA_STrfase. DR NCBIfam; TIGR00342; tRNA uracil 4-sulfurtransferase ThiI; 1. DR PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1. DR PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 1. DR Pfam; PF02568; ThiI; 1. DR Pfam; PF22025; ThiI_fer; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF143437; THUMP domain-like; 1. DR PROSITE; PS51165; THUMP; 1. PE 3: Inferred from homology; KW ATP-binding; Cytoplasm; Nucleotide-binding; RNA-binding; KW Thiamine biosynthesis; Transferase; tRNA-binding. FT CHAIN 1..390 FT /note="Probable tRNA sulfurtransferase" FT /id="PRO_1000074245" FT DOMAIN 58..161 FT /note="THUMP" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 179..180 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 204..205 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 261 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 283 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" FT BINDING 292 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021" SQ SEQUENCE 390 AA; 43237 MW; 035FB245B58B5538 CRC64; MYTSLLVRYG EISLKGNNRP YFEDKLLANM RRALAGLPPR RMRKTFGRVF VELHDDLEAV ARRLQRVFGI VSMSPVATAP LELEAIKKAA LAVLKDSPGS TFKVQAQRPN KRFPLTSPEV NQELGAYLLT HSQGQRVDVH HPDRVIHVEI RDEGAYIYSR IIPGPGGLPV GVTGRGLLLI SGGIDSPVAG YMGMKRGLEL TALHFHSFPF TSERSKEKVI DLCRVLAGYS GPLRLVVAPF TNIQKAIRQN CPQEFYVTIM RRMMFRIARA VAAKEEAPAI LTGESLGQVA SQTLQSMAVI NKVVDLPVLR PLVAWDKSEI IEVARRIGTY DISIRPYEDC CTLFVPKHPA TKPPLARVEA AEKNLAVVEL VAECLENLEI LTVEPEADVV //