ID SYT_CLOTE Reviewed; 639 AA.
AC Q891T0;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE RecName: Full=Threonine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00184};
DE EC=6.1.1.3 {ECO:0000255|HAMAP-Rule:MF_00184};
DE AltName: Full=Threonyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00184};
DE Short=ThrRS {ECO:0000255|HAMAP-Rule:MF_00184};
GN Name=thrS {ECO:0000255|HAMAP-Rule:MF_00184}; OrderedLocusNames=CTC_02286;
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88;
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H.,
RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A.,
RA Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
CC -!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a two-
CC step reaction: L-threonine is first activated by ATP to form Thr-AMP
CC and then transferred to the acceptor end of tRNA(Thr). Also edits
CC incorrectly charged L-seryl-tRNA(Thr). {ECO:0000255|HAMAP-
CC Rule:MF_00184}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonine + tRNA(Thr) = AMP + diphosphate + H(+) + L-
CC threonyl-tRNA(Thr); Xref=Rhea:RHEA:24624, Rhea:RHEA-COMP:9670,
CC Rhea:RHEA-COMP:9704, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57926, ChEBI:CHEBI:78442,
CC ChEBI:CHEBI:78534, ChEBI:CHEBI:456215; EC=6.1.1.3;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-Rule:MF_00184};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00184}.
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DR EMBL; AE015927; AAO36765.1; -; Genomic_DNA.
DR RefSeq; WP_011100426.1; NC_004557.1.
DR AlphaFoldDB; Q891T0; -.
DR SMR; Q891T0; -.
DR STRING; 212717.CTC_02286; -.
DR GeneID; 24253800; -.
DR KEGG; ctc:CTC_02286; -.
DR HOGENOM; CLU_008554_0_1_9; -.
DR OrthoDB; 9802304at2; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016740; F:transferase activity; IEA:UniProt.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR CDD; cd01667; TGS_ThrRS; 1.
DR CDD; cd00860; ThrRS_anticodon; 1.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.10.20.30; -; 1.
DR Gene3D; 3.30.54.20; -; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1.
DR HAMAP; MF_00184; Thr_tRNA_synth; 1.
DR InterPro; IPR002314; aa-tRNA-synt_IIb.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004154; Anticodon-bd.
DR InterPro; IPR036621; Anticodon-bd_dom_sf.
DR InterPro; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
DR InterPro; IPR012676; TGS-like.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR InterPro; IPR047246; ThrRS_anticodon.
DR InterPro; IPR033728; ThrRS_core.
DR InterPro; IPR012947; tRNA_SAD.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF02824; TGS; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF07973; tRNA_SAD; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SMART; SM00863; tRNA_SAD; 1.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF81271; TGS-like; 1.
DR SUPFAM; SSF55186; ThrRS/AlaRS common domain; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
DR PROSITE; PS51880; TGS; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome; RNA-binding;
KW tRNA-binding; Zinc.
FT CHAIN 1..639
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000100967"
FT DOMAIN 1..61
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 242..532
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 333
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 384
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 509
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 639 AA; 73572 MW; 2E62F21DEB8A390B CRC64;
MINITLKDGK VIEVEKGVKV SDIVMKISPA LYKKAVGAKI NGEIAELMTE IKEDSELEIL
TFDDEEGRKT VRHTSSHILA QAVKRLYPEA KLAIGPAIDN GFYYDFDIDF TFTPEMLEKI
EKEMAKIVKE NLEIERFELP REEAIKLVKD ASEPYKVELI EDLPEGEVIS FYKQGDFVDL
CAGPHLPSTG KIKAIKLLSV AGAYWRGDEK NKMLQRIYGT AFLKKSELEA YLKMLEEAKR
RDHRKLGKEL DLFTINEEGP GFPFFHPKGM VVRNILENFW REKHTKAGYD EIRTPVILNE
ELWHRSGHWD HYKENMYFTK IDNENFAIKP MNCPGSILVY KSHLHSYKEF PMRLGELGLV
HRHELSGALH GLMRVRCFTQ DDAHIFMTKE QIKDEILNVI KLIDSFYKVF GFEYFVELST
RPEDSMGSDE DWEVATNGLK NALEGAGLEY KINEGDGAFY GPKIDFHLKD CIGRTWQCGT
IQLDFQMPER FDLTYVGQDG EKHRPVMVHR VVFGSIERFI GILIEHFAGA FPTWLAPVQV
KVMTITDSQK DYANKVVNDL KEKGIRVEFD DRNEKIGYKI REAQLQKVPY MIILGDKEVS
ENKVAVRSRK EGDLGAISLK EFVAKLNYEI DNRIVENSK
//
