ID   A0A0Q0I0Q2_9GAMM        Unreviewed;       485 AA.
AC   A0A0Q0I0Q2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   11-DEC-2019, entry version 23.
DE   RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS01082725};
DE            EC=2.8.1.4 {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848765};
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   ECO:0000313|EMBL:KPZ70775.1};
GN   ORFNames=AN394_02272 {ECO:0000313|EMBL:KPZ70775.1};
OS   Pseudoalteromonas sp. P1-26.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=1723759 {ECO:0000313|EMBL:KPZ70775.1, ECO:0000313|Proteomes:UP000050391};
RN   [1] {ECO:0000313|EMBL:KPZ70775.1, ECO:0000313|Proteomes:UP000050391}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=P1-26 {ECO:0000313|EMBL:KPZ70775.1,
RC   ECO:0000313|Proteomes:UP000050391};
RA   Jackson K.R., Lunt B.L., Fisher J.N.B., Gardner A.V., Bailey M.E.,
RA   Deus L.M., Earl A.S., Gibby P.D., Hartmann K.A., Liu J.E., Manci A.M.,
RA   Nielsen D.A., Solomon M.B., Breakwell D.P., Burnett S.H., Grose J.H.;
RL   Submitted (SEP-2015) 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, ECO:0000256|SAAS:SAAS00848766}.
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         ECO:0000256|SAAS:SAAS01118926};
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, ECO:0000256|SAAS:SAAS01118903};
CC   -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848764}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021,
CC       ECO:0000256|SAAS:SAAS00848759}.
CC   -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000256|HAMAP-
CC       Rule:MF_00021, ECO:0000256|SAAS:SAAS00848754}.
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:KPZ70775.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; LKDX01000020; KPZ70775.1; -; Genomic_DNA.
DR   RefSeq; WP_054560932.1; NZ_LKDX01000020.1.
DR   EnsemblBacteria; KPZ70775; KPZ70775; AN394_02272.
DR   PATRIC; fig|1723759.3.peg.2289; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000050391; 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:0016783; F:sulfurtransferase activity; 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: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 {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00426880};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848768};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS01082722};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00426907};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS01082719};
KW   RNA-binding {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|PROSITE-
KW   ProRule:PRU00529, ECO:0000256|SAAS:SAAS00848760};
KW   Thiamine biosynthesis {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848763};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848758, ECO:0000313|EMBL:KPZ70775.1};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848757}.
FT   DOMAIN          64..168
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
FT   DOMAIN          407..485
FT                   /note="Rhodanese"
FT                   /evidence="ECO:0000259|PROSITE:PS50206"
FT   NP_BIND         186..187
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   ACT_SITE        459
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         268
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         290
FT                   /note="ATP; via amide nitrogen"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         299
FT                   /note="ATP"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   DISULFID        347..459
FT                   /note="Redox-active"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
SQ   SEQUENCE   485 AA;  54392 MW;  C85C2F33319F6D18 CRC64;
     MLKFIVKLHP EIAIKSKSVR KRFTKLLENN IKIVLRRVDE KVQVRNNWDN ISVVSLLESE
     QVRLDIIDGL KRIPGIVQFI EVTETDFDSI DDIYQKALEL IGHTIAGKTF CVRCKRSGKH
     DFTSSDVERY VGGGLNQHVE GARVKLSHPE VTVRLEVRDD KAYIVTQTHL GMAGFPLPTQ
     EDVLSLMSGG FDSGVASYQM IRKGARTHFL FFNLGGAAHE IGVKQASYYI WKQFSSTHKV
     KFVTVDFEPV VAEILENVEN SQMGVVLKRM MMRAGSQVAE KLGVQALVTG ESIGQVSSQT
     LANLSVIDRV TETLIIRPLI QHDKQDIINI ARQIGTAEMA ESMPEYCGVI SKKPTVKAKI
     KTILAEEAKF DFDVLNTVVE NARVMDIRDI DTEAKEEVKE AESVSDLPEG AVVVDIRSPD
     EEDANPLELE GIEVVHLPFF RLATKFGDLP KDKEYYLYCA KGVMSQLQAL ILHEEGFSNV
     KVYRP
//