ID A0A0R2CTA0_9LACO Unreviewed; 399 AA.
AC A0A0R2CTA0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=FC80_GL000861 {ECO:0000313|EMBL:KRM90867.1};
OS Liquorilactobacillus cacaonum DSM 21116.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423729 {ECO:0000313|EMBL:KRM90867.1, ECO:0000313|Proteomes:UP000051131};
RN [1] {ECO:0000313|EMBL:KRM90867.1, ECO:0000313|Proteomes:UP000051131}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21116 {ECO:0000313|EMBL:KRM90867.1,
RC ECO:0000313|Proteomes:UP000051131};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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: 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:KRM90867.1}.
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DR EMBL; AYZE01000014; KRM90867.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0R2CTA0; -.
DR STRING; 1423729.FC80_GL000861; -.
DR PATRIC; fig|1423729.3.peg.871; -.
DR UniPathway; UPA00060; -.
DR Proteomes; UP000051131; 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:0034227; P:tRNA thio-modification; IEA:UniProtKB-UniRule.
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 HAMAP; MF_00021; ThiI; 1.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR020536; ThiI_AANH.
DR InterPro; IPR004114; THUMP_dom.
DR InterPro; IPR003720; tRNA_STrfase.
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; 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:UP000051131};
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 54..159
FT /note="THUMP"
FT /evidence="ECO:0000259|PROSITE:PS51165"
FT BINDING 177..178
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT BINDING 202..203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT BINDING 259
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00021"
FT BINDING 281
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"
SQ SEQUENCE 399 AA; 44702 MW; DBD3850BF81DF9F3 CRC64;
MVRYGELSTK GKNRKSFIDR LGFNVRESLH SFSKLVIKAN RDRMHIQLNG EDSTSVMKRL
EQVFGIQNFS PSIKVARDVD SVKQRAVELL REQFFEGMTF KINTRRSDHD FKLDTNEMND
LLGGYILDNI PNIKVKMKNP DVILRVEIRS NGIFLSSKTI EGAGGLPVGT AGKGMLMLSG
GIDSPVAGYL AMKRGVAIEM VHFYSPPYTS EQALNKAKEL TAKLAPFVGN IKFIQVPFTE
IQETVKHDVP SGYLMTVQRR FMLRLATLIA KKREGLAIFN GEALGQVASQ TLESMVAIND
VTTLPVLRPV VSMDKNEIIE IAQKIDTFNL SIMPFEDCCT IFAPPAPKTK PRLDKARLYE
ARLDIEGLIK RALDGITITE IKSDDRFLTE TSDSFAEFL
//
