ID J3BIN2_9PSED Unreviewed; 484 AA. AC J3BIN2; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 30-AUG-2017, entry version 36. DE RecName: Full=Probable 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 ORFNames=PMI33_03420 {ECO:0000313|EMBL:EJM86188.1}; OS Pseudomonas sp. GM67. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144335 {ECO:0000313|EMBL:EJM86188.1, ECO:0000313|Proteomes:UP000007281}; RN [1] {ECO:0000313|EMBL:EJM86188.1, ECO:0000313|Proteomes:UP000007281} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=GM67 {ECO:0000313|EMBL:EJM86188.1, RC ECO:0000313|Proteomes:UP000007281}; RX PubMed=23045501; DOI=10.1128/JB.01243-12; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.; RT "Twenty-one genome sequences from Pseudomonas species and 19 genome RT sequences from diverse bacteria isolated from the rhizosphere and RT endosphere of Populus deltoides."; RL J. Bacteriol. 194:5991-5993(2012). 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: L-cysteine + 'activated' tRNA = L-serine + CC tRNA containing a thionucleotide. {ECO:0000256|HAMAP- CC Rule:MF_00021, ECO:0000256|SAAS:SAAS00848755}. CC -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + CC [ThiS]-COSH + AMP. {ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS00848762}. 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 -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EJM86188.1}. 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; AKJH01000066; EJM86188.1; -; Genomic_DNA. DR RefSeq; WP_008040995.1; NZ_AKJH01000066.1. DR EnsemblBacteria; EJM86188; EJM86188; PMI33_03420. DR PATRIC; fig|1144335.3.peg.3328; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000007281; Unassembled WGS sequence. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. 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-HAMAP. 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; 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; PS51165; THUMP; 1. PE 3: Inferred from homology; KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00023005}; KW Complete proteome {ECO:0000313|Proteomes:UP000007281}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848768}; KW Disulfide bond {ECO:0000256|SAAS:SAAS00848756}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00022982}; KW Redox-active center {ECO:0000256|SAAS:SAAS00848761}; 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}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848757}. FT DOMAIN 63 167 THUMP. {ECO:0000259|PROSITE:PS51165}. FT NP_BIND 185 186 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 267 267 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 289 289 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 298 298 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. SQ SEQUENCE 484 AA; 54424 MW; 989C3CB4F81796F6 CRC64; MKLIVKVFPE ITIKSRPVRM RFIRQLAKNI RAVLRDLDPA VVVNGVWDNL ELETRVSDPK ALKEMGERLS CMPGVAHFLQ IDEYPLGDFD DIVEKCKQHY GDALAGKIFS VRCKRAGKHP FSSIDIEKYV GSQLRRQCGA AGIDLKKPEI EVRIEVRDQR LFVIHSQHNG IGGYPLGALE QTLVLMSGGF DSTVAAYQIM RRGLMAHFCF FNLGGRAHEL GVMEVAHFIW KKYGSSQRVL FVSVPFEEVL GEILGKVDNS HMGVVLKRMM LRAATQIADR LQIEALVTGE AISQVSSQTL PNLNVIDCVT EKLVLRPLIA SHKQDIIDLA NEIGTADFAR HMPEYCGVIS VNPKTAAKRH RVEHEEKEFD MAVLERALEN AKLVPIDRVI DELGQDLQIE EVSEALAGQI IIDIRHPDAA EDEPLELGGI EVQTMPFYAL NARFKELDPT RQYLLYCDKG VMSRLHAHHL LSEGHANVRV YRPS //