ID J3BIN2_9PSED Unreviewed; 484 AA. AC J3BIN2; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 31-OCT-2012, entry version 2. DE SubName: Full=Thiazole biosynthesis/tRNA modification protein 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: 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: 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 Gene3D; G3DSA:3.40.250.10; Rhodanese-like; 1. DR Gene3D; G3DSA: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. 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 //