THII_VIBC1
ID THII_VIBC1 Reviewed; 482 AA.
AC A7MYC5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 90.
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};
GN OrderedLocusNames=VIBHAR_01178;
OS Vibrio campbellii (strain ATCC BAA-1116).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=2902295;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1116 / BB120;
RG The Vibrio harveyi Genome Sequencing Project;
RA Bassler B., Clifton S.W., Fulton L., Delehaunty K., Fronick C.,
RA Harrison M., Markivic C., Fulton R., Tin-Wollam A.-M., Shah N., Pepin K.,
RA Nash W., Thiruvilangam P., Bhonagiri V., Waters C., Tu K.C., Irgon J.,
RA Wilson R.K.;
RL Submitted (AUG-2007) 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; CP000789; ABU70168.1; -; Genomic_DNA.
DR RefSeq; WP_012127164.1; NC_022269.1.
DR AlphaFoldDB; A7MYC5; -.
DR SMR; A7MYC5; -.
DR EnsemblBacteria; ABU70168; ABU70168; VIBHAR_01178.
DR KEGG; vha:VIBHAR_01178; -.
DR PATRIC; fig|338187.25.peg.1451; -.
DR OMA; SMPEFCG; -.
DR OrthoDB; 773697at2; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000008152; Chromosome I.
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_1000074307"
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; 54386 MW; BD1E3F604B829C27 CRC64;
MKFIVKPHPE IFVKSESVRK RFTKILECNI RNIVKSRTES VAVFNRRDHI EVTSESDEFH
AEVLEILTHT PGIRHVLEVK QTEFKDLHDI YEQVLELSGS LIEGKTFAVR AKRRGKHDFT
SIELERYVGG GLNQAVESAR VKLSKPDVTI NVEVTNDRLN QVLASHKGLG GFPLGTQEDV
LSLISGGFDS GVSSYLHIKR GSKVHYCFFN LGGPAHEIGV KQVSHYLWNK YGSSAKVRFI
SVDFEPVVAE ILEKVDDGQM GVILKRMFMR AAGMIAQKMK IEALVTGEAL GQVSSQTLTN
LRHIDNVTDT LILRPLINWD KEDIVNLARE IGTEDFAKTM PEYCGVISKK PTVKAVKGKL
EAEEQKFDFS ILEQVVQDAR MTDIRDIAKE SKQAAPEVEQ VQAVEEHAIV LDIRSPEEED
DNSLEIDGVE VKHIPFYKLG TQFGDLDQAK TYLLYCDRGV MSRLQALYLQ EQGFNNVKVY
RP
