THII_PSESM
ID THII_PSESM Reviewed; 484 AA.
AC Q88AM9;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
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=PSPTO_0360;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(2003).
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; AE016853; AAO53904.1; -; Genomic_DNA.
DR RefSeq; NP_790209.1; NC_004578.1.
DR RefSeq; WP_003380207.1; NC_004578.1.
DR AlphaFoldDB; Q88AM9; -.
DR SMR; Q88AM9; -.
DR STRING; 223283.PSPTO_0360; -.
DR DNASU; 1181969; -.
DR EnsemblBacteria; AAO53904; AAO53904; PSPTO_0360.
DR GeneID; 1181969; -.
DR KEGG; pst:PSPTO_0360; -.
DR PATRIC; fig|223283.9.peg.377; -.
DR eggNOG; COG0301; Bacteria.
DR eggNOG; COG0607; Bacteria.
DR HOGENOM; CLU_037952_4_1_6; -.
DR OMA; SMPEFCG; -.
DR OrthoDB; 773697at2; -.
DR PhylomeDB; Q88AM9; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000002515; 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..484
FT /note="tRNA sulfurtransferase"
FT /id="PRO_0000154858"
FT DOMAIN 63..167
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT DOMAIN 405..483
FT /note="Rhodanese"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT ACT_SITE 457
FT /note="Cysteine persulfide intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 185..186
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 267
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 289
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 298
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT DISULFID 346..457
FT /note="Redox-active"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
SQ SEQUENCE 484 AA; 54340 MW; C857ABE5AE7EC1F6 CRC64;
MKLIVKVFPE ITIKSPPVRK KFIRQLGKNI RTVLRELDAD IVVGGVWDNL EVETRLTDPK
VLQGIRDRLS CMPGIANFLQ VAEYPLGDMD DVVAKCKLHY ADLLPGTMFS VRCKRAGRHD
FSSMDVEKYV GSQLRMQCGA AGIELKKPDL VVRMEIRDQR LFVVHDQHKG MGGYPLGALE
QTLVLMSGGF DSTVAAYQIM RRGLMAHFCF FNLGGRAHEL GVMEVAHFIW KKYGSSQRVL
FVSVPFEEVL GEILQKVDNS HMGVVLKRMM LRAASAVADR LEIDVLVTGE AISQVASQTL
PNLSLIDAAT DKLVLRPLVA THKQDIVDLA TEIGTADFAR HMPEYCGVIS VNPKTNAKRN
RVEYEEQQFD MAILEQALER AKLVSIDRVI DDLSRNIDIE EVSQALAGQV IIDIRHPDAQ
EDQPLQVPGV EIQTLPFYAL NSRFKALDDT RQYLLYCDKG VMSRLHAHHL LSEGHANVRV
YRPS
