ID   A0A0Q0I0Q2_9GAMM        Unreviewed;       485 AA.
AC   A0A0Q0I0Q2;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   28-FEB-2018, entry version 17.
DE   RecName: Full=tRNA sulfurtransferase {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00898278};
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
CC       to produce 4-thiouridine in position 8 of tRNAs, which functions
CC       as a near-UV photosensor. Also catalyzes the transfer of sulfur to
CC       the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate.
CC       This is a step in the synthesis of thiazole, in the thiamine
CC       biosynthesis pathway. The sulfur is donated as persulfide by IscS.
CC       {ECO:0000256|HAMAP-Rule:MF_00021, ECO:0000256|SAAS:SAAS00848766}.
CC   -!- CATALYTIC ACTIVITY: ATP + [ThiI sulfur-carrier protein]-S-
CC       sulfanyl-L-cysteine + uracil in tRNA + 2 reduced ferredoxin [iron-
CC       sulfur] cluster = AMP + diphosphate + 4-thiouracil in tRNA + [ThiI
CC       sulfur-carrier protein]-L-cysteine + 2 oxidized ferredoxin [iron-
CC       sulfur] cluster. {ECO:0000256|HAMAP-Rule:MF_00021,
CC       ECO:0000256|SAAS:SAAS00860091}.
CC   -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH +
CC       [ThiS]-COSH + AMP. {ECO:0000256|HAMAP-Rule:MF_00021,
CC       ECO:0000256|SAAS:SAAS00848762}.
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
CC       of feature annotation. {ECO:0000256|HAMAP-Rule:MF_00021}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KPZ70775.1}.
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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:SAAS00023005};
KW   Complete proteome {ECO:0000313|Proteomes:UP000050391};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848768};
KW   Disulfide bond {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00898280};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00022982};
KW   Redox-active center {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00898282};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00529,
KW   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       THUMP. {ECO:0000259|PROSITE:PS51165}.
FT   DOMAIN      407    485       Rhodanese. {ECO:0000259|PROSITE:PS50206}.
FT   NP_BIND     186    187       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   ACT_SITE    459    459       Cysteine persulfide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     268    268       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     290    290       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     299    299       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   DISULFID    347    459       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                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
//