ID A0A389M7Z0_9GAMM Unreviewed; 482 AA. AC A0A389M7Z0; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 27-NOV-2024, entry version 25. 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:GBU12141.1}; GN ORFNames=AwEntero_07420 {ECO:0000313|EMBL:GBU12141.1}; OS Enterobacterales bacterium. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales. OX NCBI_TaxID=1993870 {ECO:0000313|EMBL:GBU12141.1, ECO:0000313|Proteomes:UP000282082}; RN [1] {ECO:0000313|EMBL:GBU12141.1, ECO:0000313|Proteomes:UP000282082} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=AwEntero {ECO:0000313|EMBL:GBU12141.1}; RX PubMed=30246365; DOI=10.1111/1462-2920.14420; RA Murakami T., Segawa T., Takeuchi N., Sepulveda G.B., Labarca P., RA Kohshima S., Hongoh Y.; RT "Metagenomic analyses highlight the symbiotic association between the RT glacier stonefly Andiperla willinki and its bacterial gut community."; RL Environ. Microbiol. 20:4170-4183(2018). 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 + 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:0000256|HAMAP-Rule:MF_00021}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + S- CC sulfanyl-L-cysteinyl-[cysteine desulfurase] + AH2 = [sulfur-carrier CC protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + L-cysteinyl-[cysteine CC desulfurase] + A + AMP + H(+); 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:GBU12141.1}. 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; BHES01000015; GBU12141.1; -; Genomic_DNA. DR AlphaFoldDB; A0A389M7Z0; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000282082; Unassembled WGS sequence. 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:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:InterPro. DR GO; GO:0002937; P:tRNA 4-thiouridine biosynthesis; IEA:TreeGrafter. DR CDD; cd00158; RHOD; 1. DR CDD; cd01712; ThiI; 1. DR CDD; cd11716; THUMP_ThiI; 1. DR FunFam; 3.30.2130.30:FF:000002; tRNA sulfurtransferase; 1. DR FunFam; 3.40.250.10:FF:000003; tRNA sulfurtransferase; 1. DR FunFam; 3.40.50.620:FF:000029; tRNA sulfurtransferase; 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; IPR020536; ThiI_AANH. DR InterPro; IPR054173; ThiI_fer. DR InterPro; IPR049961; ThiI_N. DR InterPro; IPR026340; THII_Thiazole_biosynth_dom. DR InterPro; IPR004114; THUMP_dom. DR InterPro; IPR049962; THUMP_ThiI. DR InterPro; IPR003720; tRNA_STrfase. DR InterPro; IPR050102; tRNA_sulfurtransferase_ThiI. 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; 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; 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}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW 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 434..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; 54643 MW; 5AFCBF2018432B56 CRC64; MKFIIKLFPE ITIKSQSVRL RFIKILASSI RNIVKPHDET LAVVRHWDHI EVRSKDESKH DLIIELLCRI PGIRHVEEVE DRPYTDVHHI FEQVLEAYRS EVEGKTFCVR VKRRGKHTFS SGDVERYVGG GLNQHIESAK VNLTSPEVTV KLEINDDQLV LIKSRHEGQG GYPIGTQEDV LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGSAHEIGV KQVAYYLWNR FGSSHKVRFI AIDFEPVVGE ILEKIEDGQM GVVLKRMMVR AASQIAERYG VQALVTGEAL GQVSSQTLTN LRLIDNATDT LILRPLISHD KEHIIKVARE IGTEDFAKTM PEYCGVISKS PTVKAVKAKI EAEEQMFDFS VLDKVVSEAQ NYDIRHIAEE TSKEVAEVET VAEFASTDIL LDIRAPDEAD DKPLELDNVQ VKTLPFYKLS AQFADLDQTK TYLLYCERGV MSRLQALYLI EQGFNNVKVY RP //