ID   A0A389M7Z0_9GAMM        Unreviewed;       482 AA.
AC   A0A389M7Z0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   08-MAY-2019, entry version 4.
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:GBU12141.1};
GN   ORFNames=AwEntero_07420 {ECO:0000313|EMBL:GBU12141.1};
OS   Enterobacterales bacterium.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   unclassified Enterobacterales.
OX   NCBI_TaxID=1993870 {ECO:0000313|EMBL:GBU12141.1, ECO:0000313|Proteomes:UP000282082};
RN   [1] {ECO:0000313|EMBL:GBU12141.1, ECO:0000313|Proteomes:UP000282082}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AwEntero {ECO:0000313|EMBL:GBU12141.1};
RX   PubMed=30246365; DOI=10.1111/1462-2920.14420;
RA   Murakami T., Segawa T., Takeuchi N., Sepulveda G.B., Labarca P.,
RA   Kohshima S., Hongoh Y.;
RT   "Metagenomic analyses highlight the symbiotic association between the
RT   glacier stonefly Andiperla willinki and its bacterial gut community.";
RL   Environ. Microbiol. 20:4170-4183(2018).
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:
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
CC         tRNA + AMP + diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:24176, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC         COMP:10001, Rhea:RHEA-COMP:13337, Rhea:RHEA-COMP:13338,
CC         Rhea:RHEA-COMP:13339, Rhea:RHEA-COMP:13340, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:61963,
CC         ChEBI:CHEBI:65315, ChEBI:CHEBI:136798, ChEBI:CHEBI:456215;
CC         EC=2.8.1.4; 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 +
CC         AH2 + S-sulfanyl-L-cysteinyl-[cysteine desulfurase] = [sulfur-
CC         carrier protein ThiS]-C-terminal Gly-NH-CH2-C(O)SH + A + AMP +
CC         H(+) + L-cysteinyl-[cysteine desulfurase]; Xref=Rhea:RHEA:43340,
CC         Rhea:RHEA-COMP:12157, Rhea:RHEA-COMP:12158, Rhea:RHEA-
CC         COMP:12908, Rhea:RHEA-COMP:12910, ChEBI:CHEBI:13193,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17499, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:90618, ChEBI:CHEBI:90619,
CC         ChEBI:CHEBI:456215; Evidence={ECO:0000256|HAMAP-Rule:MF_00021,
CC         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
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:GBU12141.1}.
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DR   EMBL; BHES01000015; GBU12141.1; -; Genomic_DNA.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000282082; 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   Complete proteome {ECO:0000313|Proteomes:UP000282082};
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: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:GBU12141.1};
KW   tRNA-binding {ECO:0000256|HAMAP-Rule:MF_00021,
KW   ECO:0000256|SAAS:SAAS00848757}.
FT   DOMAIN       61    165       THUMP. {ECO:0000259|PROSITE:PS51165}.
FT   DOMAIN      404    482       Rhodanese. {ECO:0000259|PROSITE:PS50206}.
FT   NP_BIND     183    184       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   ACT_SITE    456    456       Cysteine persulfide intermediate.
FT                                {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     265    265       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     287    287       ATP; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   BINDING     296    296       ATP. {ECO:0000256|HAMAP-Rule:MF_00021}.
FT   DISULFID    344    456       Redox-active. {ECO:0000256|HAMAP-Rule:
FT                                MF_00021}.
SQ   SEQUENCE   482 AA;  54643 MW;  5AFCBF2018432B56 CRC64;
     MKFIIKLFPE ITIKSQSVRL RFIKILASSI RNIVKPHDET LAVVRHWDHI EVRSKDESKH
     DLIIELLCRI PGIRHVEEVE DRPYTDVHHI FEQVLEAYRS EVEGKTFCVR VKRRGKHTFS
     SGDVERYVGG GLNQHIESAK VNLTSPEVTV KLEINDDQLV LIKSRHEGQG GYPIGTQEDV
     LSLISGGFDS GVSSYMLMRR GCRVHYCFFN LGGSAHEIGV KQVAYYLWNR FGSSHKVRFI
     AIDFEPVVGE ILEKIEDGQM GVVLKRMMVR AASQIAERYG VQALVTGEAL GQVSSQTLTN
     LRLIDNATDT LILRPLISHD KEHIIKVARE IGTEDFAKTM PEYCGVISKS PTVKAVKAKI
     EAEEQMFDFS VLDKVVSEAQ NYDIRHIAEE TSKEVAEVET VAEFASTDIL LDIRAPDEAD
     DKPLELDNVQ VKTLPFYKLS AQFADLDQTK TYLLYCERGV MSRLQALYLI EQGFNNVKVY
     RP
//