THII_SULTO
ID THII_SULTO Reviewed; 368 AA.
AC Q96YE5;
DT 03-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Probable tRNA sulfurtransferase;
DE EC=2.8.1.4;
DE AltName: Full=Sulfur carrier protein ThiS sulfurtransferase;
DE AltName: Full=Thiamine biosynthesis protein ThiI;
DE AltName: Full=tRNA 4-thiouridine synthase;
GN Name=thiI; OrderedLocusNames=STK_22250;
OS Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
OS (Sulfolobus tokodaii).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfurisphaera.
OX NCBI_TaxID=273063;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16993 / JCM 10545 / NBRC 100140 / 7;
RX PubMed=11572479; DOI=10.1093/dnares/8.4.123;
RA Kawarabayasi Y., Hino Y., Horikawa H., Jin-no K., Takahashi M., Sekine M.,
RA Baba S., Ankai A., Kosugi H., Hosoyama A., Fukui S., Nagai Y.,
RA Nishijima K., Otsuka R., Nakazawa H., Takamiya M., Kato Y., Yoshizawa T.,
RA Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K.,
RA Masuda S., Yanagii M., Nishimura M., Yamagishi A., Oshima T., Kikuchi H.;
RT "Complete genome sequence of an aerobic thermoacidophilic Crenarchaeon,
RT Sulfolobus tokodaii strain7.";
RL DNA Res. 8:123-140(2001).
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 (By similarity).
CC {ECO:0000250}.
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 -!- 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;
CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000305}.
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DR EMBL; BA000023; BAB67332.1; -; Genomic_DNA.
DR RefSeq; WP_010980307.1; NC_003106.2.
DR AlphaFoldDB; Q96YE5; -.
DR SMR; Q96YE5; -.
DR STRING; 273063.STK_22250; -.
DR EnsemblBacteria; BAB67332; BAB67332; STK_22250.
DR GeneID; 1460303; -.
DR KEGG; sto:STK_22250; -.
DR PATRIC; fig|273063.9.peg.2523; -.
DR eggNOG; arCOG00038; Archaea.
DR OMA; VIPVHIY; -.
DR OrthoDB; 57901at2157; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000001015; 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:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
DR CDD; cd01712; ThiI; 1.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_00021; ThiI; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
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 TIGRFAMs; TIGR00342; TIGR00342; 1.
DR PROSITE; PS51165; THUMP; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; Nucleotide-binding; Reference proteome;
KW RNA-binding; Thiamine biosynthesis; Transferase; tRNA-binding.
FT CHAIN 1..368
FT /note="Probable tRNA sulfurtransferase"
FT /id="PRO_0000154901"
FT DOMAIN 51..153
FT /note="THUMP"
FT BINDING 171..172
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 196..197
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 251
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 273
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 282
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 368 AA; 41293 MW; 7FC71EF32DBE2286 CRC64;
MIIIVRLAGE IGIKSPRSRK NFEHALINNI KNVIDVEEVS IDQGYIILNT KGDFSKLSKV
FGIASFSPAD VISFSKLQDI VDFVKNKYAE KVKGKKFAIR VRRVGKHNFT SLDAAKVIGS
SLYPYSSGVD LENPEIEIHV DIRQDYAYVY DKVYEGARGL PIGTTGRTIV LFSGGFDSPI
ATWMMMKRGS SVTLLNFKLG GEVHKKIVLD EVKILSEWNS GHKIKVYFVN GIKVLSALAG
VKRYIRVVVL KRIMYKTAEL LAKKINAYSV TTGESLSQVS SQTMKNLFVT EYDINIPIFR
PLIGFDKEEI IELSRKVGTY EYSSKLPEYC AISSKSTTSA NLEEVLESEK QVNIEYEKLI
DEAEVVEV
