THII_THEMA
ID THII_THEMA Reviewed; 388 AA.
AC Q9X220;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Probable 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=TM_1694;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
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; AE000512; AAD36761.1; -; Genomic_DNA.
DR PIR; H72223; H72223.
DR RefSeq; NP_229494.1; NC_000853.1.
DR PDB; 4KR6; X-ray; 2.85 A; A/B=1-388.
DR PDB; 4KR7; X-ray; 3.42 A; A/B=1-388.
DR PDB; 4KR9; X-ray; 3.50 A; A/B=1-388.
DR PDBsum; 4KR6; -.
DR PDBsum; 4KR7; -.
DR PDBsum; 4KR9; -.
DR AlphaFoldDB; Q9X220; -.
DR SMR; Q9X220; -.
DR STRING; 243274.THEMA_05770; -.
DR EnsemblBacteria; AAD36761; AAD36761; TM_1694.
DR KEGG; tma:TM1694; -.
DR PATRIC; fig|243274.18.peg.1115; -.
DR eggNOG; COG0301; Bacteria.
DR InParanoid; Q9X220; -.
DR OMA; SMPEFCG; -.
DR BRENDA; 2.8.1.B3; 6331.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0002937; P:tRNA 4-thiouridine biosynthesis; IBA:GO_Central.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Nucleotide-binding;
KW Reference proteome; RNA-binding; Thiamine biosynthesis; Transferase;
KW tRNA-binding.
FT CHAIN 1..388
FT /note="Probable tRNA sulfurtransferase"
FT /id="PRO_0000154880"
FT DOMAIN 55..162
FT /note="THUMP"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 180..181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 205..206
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 264
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 286
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT BINDING 295
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00021"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 12..14
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 21..36
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 46..50
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 58..61
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 69..76
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 80..95
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 102..111
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:4KR7"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 140..142
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 144..152
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 155..162
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 176..180
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 186..196
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:4KR6"
FT TURN 209..211
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 216..227
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 228..230
FT /evidence="ECO:0007829|PDB:4KR6"
FT TURN 231..233
FT /evidence="ECO:0007829|PDB:4KR7"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 256..258
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 259..278
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 282..284
FT /evidence="ECO:0007829|PDB:4KR7"
FT STRAND 289..292
FT /evidence="ECO:0007829|PDB:4KR7"
FT HELIX 293..295
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 297..304
FT /evidence="ECO:0007829|PDB:4KR6"
FT TURN 314..317
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:4KR6"
FT TURN 333..335
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 346..348
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 365..367
FT /evidence="ECO:0007829|PDB:4KR6"
FT HELIX 371..380
FT /evidence="ECO:0007829|PDB:4KR6"
FT STRAND 383..387
FT /evidence="ECO:0007829|PDB:4KR6"
SQ SEQUENCE 388 AA; 44126 MW; D8BE03E3EFEEB856 CRC64;
MKELRVYIVR YSEIGLKGKN RKDFEEALRR NIERVTGMKV KRQWGRFLIP IDENVTLDDK
LKKIFGIQNF SKGFLVSHDF EEVKKYSLIA VKEKLEKGNY RTFKVQAKKA YKEYKKGVYE
INSELGALIL KNFKELSVDV RNPDFVLGVE VRPEGVLIFT DRVECYGGLP VGTGGKAVLL
LSGGIDSPVA GWYALKRGVL IESVTFVSPP FTSEGAVEKV RDILRVLREF SGGHPLRLHI
VNLTKLQLEV KKRVPDKYSL IMYRRSMFRI AEKIAEETGA VAFYTGENIG QVASQTLENL
WSIESVTTRP VIRPLSGFDK TEIVEKAKEI GTYEISIKPY QDSCVFFAPK NPATRSHPSI
LEKLEQQVPD LPVLEEEAFT SRKVEVIE
