ID A0A0Q0I0Q2_9GAMM Unreviewed; 485 AA. AC A0A0Q0I0Q2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 15-FEB-2017, entry version 10. DE RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00635850}; DE EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00498919}; 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:KPZ70775.1}; GN ORFNames=AN394_02272 {ECO:0000313|EMBL:KPZ70775.1}; OS Pseudoalteromonas sp. P1-26. OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales; OC Pseudoalteromonadaceae; Pseudoalteromonas. OX NCBI_TaxID=1723759 {ECO:0000313|EMBL:KPZ70775.1, ECO:0000313|Proteomes:UP000050391}; RN [1] {ECO:0000313|EMBL:KPZ70775.1, ECO:0000313|Proteomes:UP000050391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1-26 {ECO:0000313|EMBL:KPZ70775.1, RC ECO:0000313|Proteomes:UP000050391}; RA Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E., RA Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M., RA Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.; RL Submitted (SEP-2015) 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:SAAS00498907}. CC -!- CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine + CC tRNA containing a thionucleotide. {ECO:0000256|HAMAP- CC Rule:MF_00021, ECO:0000256|SAAS:SAAS00498918}. CC -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + CC [ThiS]-COSH + AMP. {ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS00498909}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00498911}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS00498906}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP- CC Rule:MF_00021, ECO:0000256|SAAS:SAAS00543539}. 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:KPZ70775.1}. 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; LKDX01000020; KPZ70775.1; -; Genomic_DNA. DR RefSeq; WP_054560932.1; NZ_LKDX01000020.1. DR EnsemblBacteria; KPZ70775; KPZ70775; AN394_02272. DR UniPathway; UPA00060; -. DR Proteomes; UP000050391; 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 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; 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:SAAS00023005}; KW Complete proteome {ECO:0000313|Proteomes:UP000050391}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00498917}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00635856}; KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00022982}; KW Redox-active center {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00635846}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00498916}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00498910}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00498913, ECO:0000313|EMBL:KPZ70775.1}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00498905}. FT DOMAIN 64 168 THUMP. {ECO:0000259|PROSITE:PS51165}. FT DOMAIN 407 485 Rhodanese. {ECO:0000259|PROSITE:PS50206}. FT NP_BIND 186 187 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT ACT_SITE 459 459 Cysteine persulfide intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 268 268 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 290 290 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 299 299 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT DISULFID 347 459 Redox-active. {ECO:0000256|HAMAP-Rule: FT MF_00021}. SQ SEQUENCE 485 AA; 54392 MW; C85C2F33319F6D18 CRC64; MLKFIVKLHP EIAIKSKSVR KRFTKLLENN IKIVLRRVDE KVQVRNNWDN ISVVSLLESE QVRLDIIDGL KRIPGIVQFI EVTETDFDSI DDIYQKALEL IGHTIAGKTF CVRCKRSGKH DFTSSDVERY VGGGLNQHVE GARVKLSHPE VTVRLEVRDD KAYIVTQTHL GMAGFPLPTQ EDVLSLMSGG FDSGVASYQM IRKGARTHFL FFNLGGAAHE IGVKQASYYI WKQFSSTHKV KFVTVDFEPV VAEILENVEN SQMGVVLKRM MMRAGSQVAE KLGVQALVTG ESIGQVSSQT LANLSVIDRV TETLIIRPLI QHDKQDIINI ARQIGTAEMA ESMPEYCGVI SKKPTVKAKI KTILAEEAKF DFDVLNTVVE NARVMDIRDI DTEAKEEVKE AESVSDLPEG AVVVDIRSPD EEDANPLELE GIEVVHLPFF RLATKFGDLP KDKEYYLYCA KGVMSQLQAL ILHEEGFSNV KVYRP //