ID J3BIN2_9PSED Unreviewed; 484 AA. AC J3BIN2; DT 03-OCT-2012, integrated into UniProtKB/TrEMBL. DT 03-OCT-2012, sequence version 1. DT 22-FEB-2023, entry version 57. 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 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 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: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 AlphaFoldDB; J3BIN2; -. DR EnsemblBacteria; EJM86188; EJM86188; PMI33_03420. DR PATRIC; fig|1144335.3.peg.3328; -. DR OrthoDB; 9773948at2; -. 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-UniRule. DR GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule. DR GO; GO:0140741; F:tRNA U4 sulfurtransferase; IEA:UniProtKB-EC. 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 CDD; cd11716; THUMP_ThiI; 1. DR Gene3D; 3.30.2130.30; -; 1. DR Gene3D; 3.40.50.620; HUPs; 1. DR Gene3D; 3.40.250.10; Rhodanese-like domain; 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 PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1. DR PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 1. DR Pfam; PF02568; ThiI; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1. DR SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1. DR SUPFAM; SSF143437; THUMP domain-like; 1. DR TIGRFAMs; TIGR04271; ThiI_C_thiazole; 1. DR TIGRFAMs; TIGR00342; tRNA sulfurtransferase ThiI; 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}; KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP- KW Rule:MF_00021}; Redox-active center {ECO:0000256|ARBA:ARBA00023284}; 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|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00021}; KW tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP- KW Rule:MF_00021}. FT DOMAIN 63..167 FT /note="THUMP" FT /evidence="ECO:0000259|PROSITE:PS51165" FT DOMAIN 405..481 FT /note="Rhodanese" FT /evidence="ECO:0000259|PROSITE:PS50206" FT ACT_SITE 457 FT /note="Cysteine persulfide intermediate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 185..186 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 267 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 289 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021" FT BINDING 298 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="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 //