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Database: UniProt
Entry: A0A0F5VA47_9GAMM
LinkDB: A0A0F5VA47_9GAMM
Original site: A0A0F5VA47_9GAMM 
ID   A0A0F5VA47_9GAMM        Unreviewed;       482 AA.
AC   A0A0F5VA47;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021};
DE            EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000256|HAMAP-Rule:MF_00021};
DE   AltName: Full=tRNA 4-thiouridine synthase {ECO:0000256|HAMAP-Rule:MF_00021};
GN   Name=thiI {ECO:0000256|HAMAP-Rule:MF_00021};
GN   ORFNames=KY46_15295 {ECO:0000313|EMBL:KKC98967.1};
OS   Photobacterium halotolerans.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Photobacterium.
OX   NCBI_TaxID=265726 {ECO:0000313|EMBL:KKC98967.1, ECO:0000313|Proteomes:UP000033633};
RN   [1] {ECO:0000313|EMBL:KKC98967.1, ECO:0000313|Proteomes:UP000033633}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MELD1 {ECO:0000313|EMBL:KKC98967.1,
RC   ECO:0000313|Proteomes:UP000033633};
RA   Mathew D.C., Huang C.-C.;
RT   "Mercury Reductase activity and rhizosphere competence traits in the genome
RT   of root associated Photobacterium halotolerans MELD1.";
RL   Submitted (DEC-2014) 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:0000256|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:0000256|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:0000256|HAMAP-
CC         Rule:MF_00021};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00021}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC       ECO:0000256|HAMAP-Rule:MF_00021}.
CC   -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00021}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00021}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KKC98967.1}.
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DR   EMBL; JWYV01000014; KKC98967.1; -; Genomic_DNA.
DR   RefSeq; WP_046221509.1; NZ_JWYV01000014.1.
DR   AlphaFoldDB; A0A0F5VA47; -.
DR   STRING; 265726.KY46_15295; -.
DR   PATRIC; fig|265726.11.peg.1324; -.
DR   OrthoDB; 9773948at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000033633; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004810; F:CCA tRNA nucleotidyltransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140741; F:tRNA-uracil-4 sulfurtransferase activity; 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; cd00158; RHOD; 1.
DR   CDD; cd01712; ThiI; 1.
DR   CDD; cd11716; THUMP_ThiI; 1.
DR   Gene3D; 3.30.2130.30; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.250.10; Rhodanese-like domain; 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   NCBIfam; TIGR04271; ThiI_C_thiazole; 1.
DR   NCBIfam; TIGR00342; tRNA 4-thiouridine(8) synthase ThiI; 1.
DR   PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1.
DR   PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 1.
DR   Pfam; PF00581; Rhodanese; 1.
DR   Pfam; PF02568; ThiI; 1.
DR   Pfam; PF02926; THUMP; 1.
DR   SMART; SM00981; THUMP; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF52821; Rhodanese/Cell cycle control phosphatase; 1.
DR   SUPFAM; SSF143437; THUMP domain-like; 1.
DR   PROSITE; PS50206; RHODANESE_3; 1.
DR   PROSITE; PS51165; THUMP; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00021};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00021};
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|HAMAP-
KW   Rule:MF_00021};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00021};
KW   Redox-active center {ECO:0000256|ARBA:ARBA00023284, ECO:0000256|HAMAP-
KW   Rule:MF_00021}; Reference proteome {ECO:0000313|Proteomes:UP000033633};
KW   RNA-binding {ECO:0000256|ARBA:ARBA00022884, ECO:0000256|HAMAP-
KW   Rule:MF_00021};
KW   Thiamine biosynthesis {ECO:0000256|ARBA:ARBA00022977, ECO:0000256|HAMAP-
KW   Rule:MF_00021};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW   Rule:MF_00021};
KW   tRNA-binding {ECO:0000256|ARBA:ARBA00022555, ECO:0000256|HAMAP-
KW   Rule:MF_00021}.
FT   DOMAIN          61..165
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
FT   DOMAIN          404..480
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   ACT_SITE        456
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         183..184
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         265
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         287
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         296
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   DISULFID        344..456
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
SQ   SEQUENCE   482 AA;  54251 MW;  AE1499975CA64C3B CRC64;
     MKFIVKPHPE IFVKSESVRK RFTKILECNI RIILQRLSDQ VAVYNRRSYI DVTVKDDSLR
     DQVLTVLTQT PGIHHVLEVK QTDFTDMHDI FEQTLAHVGN ELDGKTFCVR AKRVGKHDFT
     SIELERYVGG GLNQAVESAK VQLKKPQVTV NLEVDGEKLN QVLARHKGLG GFPLGTQEDV
     LSLISGGFDS GVSSYLHIKR GSKVHYCFFN LGGPAHEIGV KQVSHYLWKK FGSSAKVKFI
     AIDFEPVVAE ILENVDDGQM GVVLKRMFMR AAGQVAERFG IQALVTGEAL GQVSSQTLTN
     LRHIDNVTDT LILRPLINWD KEDIINLARD IGTEDFAKTM PEFCGVISKS PTVKAVKEKL
     EAEEAKFDFA VLDRVVSEAR ILDIRDIEKE SQEQAPEIEL VDQIDGNSTV LDIRSPDEED
     ESPLHIEGVE IKHLPFYKLA TQFGDLPQDK TYLLYCARGV MSRLQALYLK ENGFDNVKVY
     RP
//
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