ID A0A2X2G1J1_RAOPL Unreviewed; 482 AA. AC A0A2X2G1J1; DT 07-NOV-2018, integrated into UniProtKB/TrEMBL. DT 07-NOV-2018, sequence version 1. DT 08-MAY-2019, entry version 6. DE RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS01082725}; DE EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848765}; 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:SPZ26929.1}; GN ORFNames=DN603_16565 {ECO:0000313|EMBL:RWT21571.1}, NCTC9528_00984 GN {ECO:0000313|EMBL:SPZ26929.1}; OS Raoultella planticola (Klebsiella planticola). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Raoultella. OX NCBI_TaxID=575 {ECO:0000313|EMBL:SPZ26929.1, ECO:0000313|Proteomes:UP000250543}; RN [1] {ECO:0000313|EMBL:RWT21571.1, ECO:0000313|Proteomes:UP000288843} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GEO_47_Down_B {ECO:0000313|EMBL:RWT21571.1, RC ECO:0000313|Proteomes:UP000288843}; RA Mathys D.A., Mollenkopf D.F., Feicht S.M., Adams R.J., Albers A.L., RA Stuever D.M., Daniels J.B., Wittum T.E.; RT "Carbapenemase-producing Enterobacteriaceae present in wastewater RT treatment plant effluent and nearby surface waters in the US."; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:SPZ26929.1, ECO:0000313|Proteomes:UP000250543} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC9528 {ECO:0000313|EMBL:SPZ26929.1, RC ECO:0000313|Proteomes:UP000250543}; RG Pathogen Informatics; RA Doyle S.; RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA CC to produce 4-thiouridine in position 8 of tRNAs, which functions CC as a near-UV photosensor. Also catalyzes the transfer of sulfur to CC the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. CC This is a step in the synthesis of thiazole, in the thiamine CC biosynthesis pathway. The sulfur is donated as persulfide by IscS. CC {ECO:0000256|HAMAP-Rule:MF_00021, 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 CC tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]; CC Xref=Rhea:RHEA:24176, Rhea:RHEA-COMP:10000, Rhea:RHEA- CC COMP:10001, Rhea:RHEA-COMP:13337, Rhea:RHEA-COMP:13338, CC Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13340, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:61963, CC ChEBI:CHEBI:65315, ChEBI:CHEBI:136798, ChEBI:CHEBI:456215; CC EC=2.8.1.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS01118926}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + CC AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur- CC carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + CC H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:43340, CC Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA- CC COMP:12908, Rhea:RHEA-COMP:12910, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS01118903}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848764}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS00848759}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP- CC Rule:MF_00021, ECO:0000256|SAAS:SAAS00848754}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation CC of feature annotation. {ECO:0000256|HAMAP-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; QKOX01000016; RWT21571.1; -; Genomic_DNA. DR EMBL; UAUJ01000001; SPZ26929.1; -; Genomic_DNA. DR RefSeq; WP_032689256.1; NZ_UAUJ01000001.1. DR KEGG; rpln:B1209_21295; -. DR KO; K03151; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000250543; Unassembled WGS sequence. DR Proteomes; UP000288843; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-UniRule. DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. 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; cd01712; ThiI; 1. DR Gene3D; 3.40.250.10; -; 1. DR Gene3D; 3.40.50.620; -; 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 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. DR PROSITE; PS50206; RHODANESE_3; 1. DR PROSITE; PS51165; THUMP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00426880}; KW Complete proteome {ECO:0000313|Proteomes:UP000250543, KW ECO:0000313|Proteomes:UP000288843}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848768}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS01082722}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00426907}; KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS01082719}; KW Reference proteome {ECO:0000313|Proteomes:UP000250543}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|PROSITE- KW ProRule:PRU00529, ECO:0000256|SAAS:SAAS00848760}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848763}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848758, ECO:0000313|EMBL:SPZ26929.1}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848757}. FT DOMAIN 61 165 THUMP. {ECO:0000259|PROSITE:PS51165}. FT DOMAIN 404 482 Rhodanese. {ECO:0000259|PROSITE:PS50206}. FT NP_BIND 183 184 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT ACT_SITE 456 456 Cysteine persulfide intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 265 265 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 287 287 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 296 296 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT DISULFID 344 456 Redox-active. {ECO:0000256|HAMAP-Rule: FT MF_00021}. SQ SEQUENCE 482 AA; 54828 MW; A6FEFAD112FE7412 CRC64; MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKNYDET LAVVRHWDHI EVRAKDENQR PIIRDALTRI PGIHHILEVE DVPFTSLHDI FEKTLPLWRE ALEGKTFCVR VKRRGKHEFT SIEVERYVGG GLNQHIETAR VKLTDPDITV NLEIENDRLL LVKGRYEGIG GFPIGTQEDV LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGAAHEIGV RQVAHYLWNR FGSSHRVRFV AINFEPVVGE ILEKVDDGQM GVVLKRMMIR AASKVAERYG VQALVTGEAL GQVSSQTLTN LRLIDNVSDT LILRPLISHD KEHIIDLARE IGTEDFARTM PEYCGVISKS PTVKAVKAKI EAEEENFDFS ILDKVVAEAN NVDIRDIAQQ TQQEVVEVET VTGFSPNDVI LDIRSVDEQD EKPLKVEGVD VVSLPFYKLS TQFGNLDQSK TWLLWCERGV MSRLQALYLR EQGFENVKVY RP //