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THII_EDWI9
ID   THII_EDWI9              Reviewed;         482 AA.
AC   C5BCI2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=tRNA sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021};
DE            EC=2.8.1.4 {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000255|HAMAP-Rule:MF_00021};
DE   AltName: Full=tRNA 4-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_00021};
GN   Name=thiI {ECO:0000255|HAMAP-Rule:MF_00021}; OrderedLocusNames=NT01EI_1065;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) 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:0000255|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:0000255|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:0000255|HAMAP-
CC         Rule:MF_00021};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00021}.
CC   -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000255|HAMAP-
CC       Rule:MF_00021}.
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DR   EMBL; CP001600; ACR68277.1; -; Genomic_DNA.
DR   RefSeq; WP_015870457.1; NC_012779.2.
DR   AlphaFoldDB; C5BCI2; -.
DR   SMR; C5BCI2; -.
DR   STRING; 67780.B6E78_15690; -.
DR   PRIDE; C5BCI2; -.
DR   EnsemblBacteria; ACR68277; ACR68277; NT01EI_1065.
DR   GeneID; 7960650; -.
DR   KEGG; eic:NT01EI_1065; -.
DR   PATRIC; fig|634503.3.peg.964; -.
DR   HOGENOM; CLU_037952_4_1_6; -.
DR   OMA; SMPEFCG; -.
DR   OrthoDB; 773697at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000001485; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; 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: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   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; Cytoplasm; Disulfide bond; Nucleotide-binding;
KW   Redox-active center; Reference proteome; RNA-binding;
KW   Thiamine biosynthesis; Transferase; tRNA-binding.
FT   CHAIN           1..482
FT                   /note="tRNA sulfurtransferase"
FT                   /id="PRO_1000201912"
FT   DOMAIN          61..165
FT                   /note="THUMP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   DOMAIN          404..482
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   ACT_SITE        456
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         183..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT   DISULFID        344..456
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
SQ   SEQUENCE   482 AA;  54871 MW;  71664979C6F2685F CRC64;
     MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKPLVED VAVTRHWDHI EVRAKEESRR
     DLVRDALTRI PGIHHILEVE DHPYTDMHDI FEQTLAMYRE QLEEKTFCVR VKRRGKHTFT
     SIEVERYVGG GLNQNIPSAR VRLNHPEVTV NLEIEDDRLL LVRGRFEGQG GYPIGTQEDV
     LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGSAHEIGV KQVAHYLWNR FGSSHRVRFV
     AIDFAPVVGE ILEKVDDGQM GVVLKRMMVR AASRVAERYG IQALVTGEAL GQVSSQTLTN
     LRLIDGVSDT LVLRPLIAHD KEHIIRLARN IGTEDFAKTM PEFCGVISKS PTVKAVKARI
     EAEEEHFDFA ILDRVVDEAQ TMDIRDIARQ SEADVVEVET IESLAEGDVV LDIRAPDEQE
     AKPLQLADSE VICLPFYKLA NAFGDLDQVR RYVLYCDRGV MSRLQALYLR EQGYDNVRVY
     RP
 
 
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