ID   SYT_DEHMC               Reviewed;         582 AA.
AC   Q3ZXB5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
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=cbdbA726;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexi; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(2005).
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; AJ965256; CAI82888.1; -; Genomic_DNA.
DR   RefSeq; WP_011309239.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZXB5; -.
DR   SMR; Q3ZXB5; -.
DR   KEGG; deh:cbdbA726; -.
DR   HOGENOM; CLU_008554_0_1_0; -.
DR   OMA; FYYDFAY; -.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   CDD; cd00771; ThrRS_core; 1.
DR   Gene3D; 3.30.930.10; -; 1.
DR   Gene3D; 3.40.50.800; -; 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; IPR002320; Thr-tRNA-ligase_IIa.
DR   InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
DR   InterPro; IPR033728; ThrRS_core.
DR   InterPro; IPR012947; tRNA_SAD.
DR   PANTHER; PTHR11451; PTHR11451; 1.
DR   Pfam; PF03129; HGTP_anticodon; 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; SSF55186; SSF55186; 1.
DR   SUPFAM; SSF55681; SSF55681; 1.
DR   TIGRFAMs; TIGR00418; thrS; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW   Nucleotide-binding; Protein biosynthesis; RNA-binding; tRNA-binding; Zinc.
FT   CHAIN           1..582
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_1000020380"
FT   REGION          185..478
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         278
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         329
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         455
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   582 AA;  67061 MW;  6140080C5FC7FA20 CRC64;
     MANQIDESKP ISDLEIMRHS AAHIMAEAVL SMFPEAKLGI GPAIDTGFYY DFDLPRTLTP
     EDLPEIETRM NQLVKSNLPF RREEMSKDEA RKLFANQPYK LELLNDITDE TVSIYRQGNF
     CDLCRGPHVN YTSKVKAFKL LSIAGAYWRG DEKRPMLQRI YGAAFLDKAS LAEYLNMLEE
     AAKRDHRKLG KELELFSLHQ EIGGGLVNWL PNGAIVRHLI EEFWKKEHLK RGYDLVYTPH
     IAKVDLWKTS GHWGFYRENM YSPMDIDGEE YVLKPMNCVY HILMFKNRTR SYKELPIRMA
     ELGTVYRYER SGVLHGLSRV RGFTQDDAHI FCLYDQLEKE VVKVLDLAKF MIDTFGFTKY
     KVMLSTRPEK YVGELDKWEY ATDILAKALE ANQIPYQVDP GEGVFYGPKI DIKFEDALGR
     TWQGPTIQVD FQLPERFDVS VVGEDGKDQP VAMVHRTVLG SMERFMSCLT EQYGGAFPAW
     LSPKQVMVIP IADRHTEFAE KLACELREEE VRVEVDSRSE TMNQKIRQAQ LAKIPYMLVV
     GDKEIETQSV AVRTRTGSQQ VMPFAEFKSM LLAKIKTKST EI