THII_ECO8A
ID THII_ECO8A Reviewed; 482 AA.
AC B7M3R2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=ECIAI1_0423;
OS Escherichia coli O8 (strain IAI1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585034;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IAI1;
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
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; CU928160; CAQ97295.1; -; Genomic_DNA.
DR RefSeq; WP_000668691.1; NC_011741.1.
DR AlphaFoldDB; B7M3R2; -.
DR SMR; B7M3R2; -.
DR KEGG; ecr:ECIAI1_0423; -.
DR HOGENOM; CLU_037952_4_1_6; -.
DR OMA; SMPEFCG; -.
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: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; RNA-binding; Thiamine biosynthesis; Transferase;
KW tRNA-binding.
FT CHAIN 1..482
FT /note="tRNA sulfurtransferase"
FT /id="PRO_1000116402"
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; 55043 MW; 6564E8EEA025BDB7 CRC64;
MKFIIKLFPE ITIKSQSVRL RFIKILTGNI RNVLKHYDET LAVVRHWDNI EVRAKDENQR
LAIRDALTRI PGIHHILEVE DVPFTDMHDI FEKALVQYRD QLEGKTFCVR VKRRGKHDFS
SIDVERYVGG GLNQHIESAR VKLTNPEVTV HLEVEDDRLL LIKGRYEGIG GFPIGTQEDV
LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGAAHEIGV RQVAHYLWNR FGSSHRVRFV
AINFEPVVGE ILEKIDDGQM GVILKRMMVR AASKVAERYG VQALVTGEAL GQVSSQTLTN
LRLIDNVSDT LILRPLISYD KEHIINLARQ IGTEDFARTM PEYCGVISKS PTVKAVKSKI
EAEEEKFDFS ILDKVVEEVN NVDIREIAQQ TEQEVVEVET VNGFGPNDVI LDIRSIDEQE
DKPLKVEGID VVSLPFYKLS TKFGDLDQNR TWLLWCERGV MSRLQALYLR EQGFNNVKVY
RP
