ID   A0A389M7Z0_9GAMM        Unreviewed;       482 AA.
AC   A0A389M7Z0;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   29-MAY-2024, entry version 22.
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   ECO:0000313|EMBL:GBU12141.1};
GN   ORFNames=AwEntero_07420 {ECO:0000313|EMBL:GBU12141.1};
OS   Enterobacterales bacterium.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; 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 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:GBU12141.1}.
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; BHES01000015; GBU12141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A389M7Z0; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000282082; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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:0002937; P:tRNA 4-thiouridine biosynthesis; IEA:TreeGrafter.
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 uracil 4-sulfurtransferase ThiI; 1.
DR   PANTHER; PTHR43209; TRNA SULFURTRANSFERASE; 1.
DR   PANTHER; PTHR43209:SF1; TRNA SULFURTRANSFERASE; 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};
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          434..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;  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
//