ID A0A389M7Z0_9GAMM Unreviewed; 482 AA. AC A0A389M7Z0; DT 05-DEC-2018, integrated into UniProtKB/TrEMBL. DT 05-DEC-2018, sequence version 1. DT 13-FEB-2019, entry version 3. DE RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS01082725}; DE EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848765}; 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:GBU12141.1}; GN ORFNames=AwEntero_07420 {ECO:0000313|EMBL:GBU12141.1}; OS Enterobacterales bacterium. OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales; OC unclassified Enterobacterales. OX NCBI_TaxID=1993870 {ECO:0000313|EMBL:GBU12141.1}; RN [1] {ECO:0000313|EMBL:GBU12141.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=AwEntero {ECO:0000313|EMBL:GBU12141.1}; RA Murakami T., Segawa T., Takeuchi N., Sepulveda G.B., Labarca P., RA Kohshima S., Hongoh Y.; RT "Metagenomic analyses highlight the symbiotic association between the RT glacier stonefly Andiperla willinki and its bacterial gut community."; RL Environ. Microbiol. 0:0-0(2018). 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:SAAS00848766}. 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 CC tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin]; CC Xref=Rhea:RHEA:24176, Rhea:RHEA-COMP:10000, Rhea:RHEA- CC COMP:10001, Rhea:RHEA-COMP:13337, Rhea:RHEA-COMP:13338, CC Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13340, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:61963, CC ChEBI:CHEBI:65315, ChEBI:CHEBI:136798, ChEBI:CHEBI:456215; CC EC=2.8.1.4; Evidence={ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS01118926}; CC -!- CATALYTIC ACTIVITY: CC Reaction=[sulfur-carrier protein ThiS]-C-terminal Gly-Gly-AMP + CC AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur- CC carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP + CC H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:43340, CC Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA- CC COMP:12908, Rhea:RHEA-COMP:12910, ChEBI:CHEBI:13193, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950, CC ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619, CC ChEBI:CHEBI:456215; Evidence={ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS01118903}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848764}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, CC ECO:0000256|SAAS:SAAS00848759}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP- CC Rule:MF_00021, ECO:0000256|SAAS:SAAS00848754}. 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:GBU12141.1}. 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; BHES01000015; GBU12141.1; -; Genomic_DNA. DR UniPathway; UPA00060; -. 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|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00023005}; KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848768}; KW Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS01082722}; 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:SAAS01082719}; KW RNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|PROSITE- KW ProRule:PRU00529, ECO:0000256|SAAS:SAAS00848760}; KW Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848763}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848758, ECO:0000313|EMBL:GBU12141.1}; KW tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, KW ECO:0000256|SAAS:SAAS00848757}. FT DOMAIN 61 165 THUMP. {ECO:0000259|PROSITE:PS51165}. FT DOMAIN 404 482 Rhodanese. {ECO:0000259|PROSITE:PS50206}. FT NP_BIND 183 184 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT ACT_SITE 456 456 Cysteine persulfide intermediate. FT {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 265 265 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 287 287 ATP; via amide nitrogen. FT {ECO:0000256|HAMAP-Rule:MF_00021}. FT BINDING 296 296 ATP. {ECO:0000256|HAMAP-Rule:MF_00021}. FT DISULFID 344 456 Redox-active. {ECO:0000256|HAMAP-Rule: FT MF_00021}. SQ SEQUENCE 482 AA; 54643 MW; 5AFCBF2018432B56 CRC64; MKFIIKLFPE ITIKSQSVRL RFIKILASSI RNIVKPHDET LAVVRHWDHI EVRSKDESKH DLIIELLCRI PGIRHVEEVE DRPYTDVHHI FEQVLEAYRS EVEGKTFCVR VKRRGKHTFS SGDVERYVGG GLNQHIESAK VNLTSPEVTV KLEINDDQLV LIKSRHEGQG GYPIGTQEDV LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGSAHEIGV KQVAYYLWNR FGSSHKVRFI AIDFEPVVGE ILEKIEDGQM GVVLKRMMVR AASQIAERYG VQALVTGEAL GQVSSQTLTN LRLIDNATDT LILRPLISHD KEHIIKVARE IGTEDFAKTM PEYCGVISKS PTVKAVKAKI EAEEQMFDFS VLDKVVSEAQ NYDIRHIAEE TSKEVAEVET VAEFASTDIL LDIRAPDEAD DKPLELDNVQ VKTLPFYKLS AQFADLDQTK TYLLYCERGV MSRLQALYLI EQGFNNVKVY RP //