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Database: UniProt
Entry: A0A2N7TTX3_9GAMM
LinkDB: A0A2N7TTX3_9GAMM
Original site: A0A2N7TTX3_9GAMM 
ID   A0A2N7TTX3_9GAMM        Unreviewed;       490 AA.
AC   A0A2N7TTX3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=Probable 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=C1H66_01845 {ECO:0000313|EMBL:PMR71598.1};
OS   Halomonas heilongjiangensis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Halomonadaceae; Halomonas.
OX   NCBI_TaxID=1387883 {ECO:0000313|EMBL:PMR71598.1, ECO:0000313|Proteomes:UP000235346};
RN   [1] {ECO:0000313|EMBL:PMR71598.1, ECO:0000313|Proteomes:UP000235346}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 26881 {ECO:0000313|EMBL:PMR71598.1,
RC   ECO:0000313|Proteomes:UP000235346};
RA   Chen C.;
RT   "Halomonas endophytica sp. nov., isolated from storage liquid in the stems
RT   of Populus euphratica.";
RL   Submitted (JAN-2018) 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:PMR71598.1}.
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DR   EMBL; PNRE01000012; PMR71598.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N7TTX3; -.
DR   OrthoDB; 9773948at2; -.
DR   UniPathway; UPA00060; -.
DR   Proteomes; UP000235346; 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; 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; 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; 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   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00021}; Reference proteome {ECO:0000313|Proteomes:UP000235346};
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          64..168
FT                   /note="THUMP"
FT                   /evidence="ECO:0000259|PROSITE:PS51165"
FT   BINDING         186..187
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         268
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         290
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT   BINDING         299
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
SQ   SEQUENCE   490 AA;  55275 MW;  E74A819F52E9A794 CRC64;
     MHYLLKLFPE ITIKSRSVRR HMTRCLAGNV RTILRRLDEG VSVKDTWDAL HVTLPEALPE
     ALTREMEERL TRIPGIHEVL AIREAPFSDL TDIADQVVPL WQHTIAGRRF RVSAKRRGDH
     DFSSEHIERL IGRRLLEASP DARVDLTRAD VNVSVEVVHQ RLRLIQARWP GLGGYPLGLQ
     GQALTLISGG FDSPVAAWRM MRRGIKTHFL FFNLGGPAHE AGVREVTHHL WQRYGSSHRV
     NFLSVPFEGV VAEILRSVPD GLMGVVLKRM MVRAASRIAH RERIPALVTG DAIAQVSSQT
     LTNLALIDEA SELPILRPLL TEDKQDIIAQ ARRLDTARFA ETMPEYCGVI SRRPHTRARA
     HDVEQAEAGF DFAVLEAAIR AVETTRSDRL MERRHPPGEV PTVDSPQALA QLGDASVIDI
     RAPEEREASP LRLPDVPRLE IPFYELQGRA PDLPDDRCYL LYCDQGVMSR MQALHLHDRG
     LTHFGVYRTT
//
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