ID A0A0Q0I0Q2_9GAMM Unreviewed; 485 AA. AC A0A0Q0I0Q2; DT 20-JAN-2016, integrated into UniProtKB/TrEMBL. DT 20-JAN-2016, sequence version 1. DT 12-AUG-2020, entry version 24. DE RecName: Full=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 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|Proteomes:UP000050391} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1-26 {ECO:0000313|Proteomes:UP000050391}; RA Klassen J.L., Wolf T., Rischer M., Guo H., Shelest E., Clardy J., RA Beemelmanns C.; RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA to CC produce 4-thiouridine in position 8 of tRNAs, which functions as a CC near-UV photosensor. Also catalyzes the transfer of sulfur to the CC sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a CC step in the synthesis of thiazole, in the thiamine biosynthesis CC pathway. The sulfur is donated as persulfide by IscS. CC {ECO:0000256|HAMAP-Rule:MF_00021}. 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 tRNA + CC AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]; CC Xref=Rhea:RHEA:24176, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001, CC Rhea:RHEA-COMP:13337, Rhea:RHEA-COMP:13338, Rhea:RHEA-COMP:13339, CC Rhea:RHEA-COMP:13340, ChEBI:CHEBI:15378, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:33737, CC ChEBI:CHEBI:33738, ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, CC ChEBI:CHEBI:136798, ChEBI:CHEBI:456215; EC=2.8.1.4; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00021}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + AH2 + CC S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur-carrier CC protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + H(+) + L- CC cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:43340, Rhea:RHEA- CC COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-COMP:12908, Rhea:RHEA- CC COMP:12910, ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, CC ChEBI:CHEBI:90619, ChEBI:CHEBI:456215; Evidence={ECO:0000256|HAMAP- CC Rule:MF_00021}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496, CC ECO:0000256|HAMAP-Rule:MF_00021}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP- CC Rule:MF_00021}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00021}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 PATRIC; fig|1723759.3.peg.2289; -. 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-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|ARBA:ARBA00022840, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00021}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP- KW Rule:MF_00021}; Reference proteome {ECO:0000313|Proteomes:UP000050391}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|PROSITE- KW ProRule:PRU00529}; KW Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000313|EMBL:KPZ70775.1}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00021}. FT DOMAIN 64..168 FT /note="THUMP" FT /evidence="ECO:0000259|PROSITE:PS51165" FT DOMAIN 407..485 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT NP_BIND 186..187 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT ACT_SITE 459 FT /note="Cysteine persulfide intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 268 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 290 FT /note="ATP; via amide nitrogen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 299 FT /note="ATP" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT DISULFID 347..459 FT /note="Redox-active" FT /evidence="ECO:0000256|HAMAP-Rule: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 //