ID J3BIN2_9PSED Unreviewed; 484 AA. AC J3BIN2; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 28-NOV-2012, entry version 3. DE RecName: Full=tRNA sulfurtransferase; DE EC=2.8.1.4; DE AltName: Full=Sulfur carrier protein ThiS sulfurtransferase; DE AltName: Full=Thiamine biosynthesis protein ThiI; DE AltName: Full=tRNA 4-thiouridine synthase; GN Name=thiI; OS Pseudomonas sp. GM67. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=1144335; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=GM67; RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L., RA Land M.L., Lu T.-Y.S., Schadt C.W., Pelletier D.A., Doktycz M.J.; RT "Sequencing of Twenty One Pseudomonas Genomes and Twenty Two Genomes RT from Diverse Bacteria isolated from Populus deltoides endosphere RT communities."; RL Submitted (MAY-2012) 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 (By similarity). CC -!- CATALYTIC ACTIVITY: -SSH + [ThiS]-COAMP = [IscS]-SH + [ThiS]-COSH CC + AMP. CC -!- CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine + CC tRNA containing a thionucleotide. CC -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + CC [ThiS]-COSH + AMP. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the ThiI family. CC -!- SIMILARITY: Contains 1 THUMP domain. CC -!- SIMILARITY: Contains 1 rhodanese domain. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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 UniPathway; UPA00060; -. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR GO; GO:0052837; P:thiazole biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.250.10; Rhodanese-like; 1. DR Gene3D; 3.40.50.620; Rossmann-like_a/b/a_fold; 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; IPR003720; ThiI. DR InterPro; IPR020536; ThiI_C_dom. DR InterPro; IPR004114; THUMP. DR Pfam; PF02568; ThiI; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF52821; Rhodanese-like; 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; Cytoplasm; Disulfide bond; Nucleotide-binding; KW Redox-active center; RNA-binding; Thiamine biosynthesis; Transferase; KW tRNA-binding. FT DOMAIN 63 167 THUMP (By similarity). FT DOMAIN 405 483 Rhodanese (By similarity). FT NP_BIND 185 186 ATP (By similarity). FT ACT_SITE 457 457 Cysteine persulfide intermediate (By FT similarity). FT BINDING 267 267 ATP (By similarity). FT BINDING 289 289 ATP; via amide nitrogen (By similarity). FT BINDING 298 298 ATP (By similarity). FT DISULFID 346 457 Redox-active (By similarity). 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 //