ID SYT_BORHD Reviewed; 583 AA. AC B2S162; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-2008, sequence version 1. DT 02-SEP-2026, entry version 97. 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=BH0720; OS Borrelia hermsii (strain HS1 / DAH). OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales; OC Borreliaceae; Borrelia. OX NCBI_TaxID=314723; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HS1 / DAH; RA Porcella S.F., Raffel S.J., Schrumpf M.E., Montgomery B., Smith T., RA Schwan T.G.; RT "The genome sequence of Borrelia hermsii and Borrelia turicatae: RT comparative analysis of two agents of endemic N. America relapsing fever."; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. 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=tRNA(Thr) + L-threonine + ATP = L-threonyl-tRNA(Thr) + AMP + CC diphosphate + H(+); 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; Evidence={ECO:0000255|HAMAP- CC 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}. 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; CP000048; AAX17218.1; -; Genomic_DNA. DR RefSeq; WP_012422468.1; NC_010673.1. DR AlphaFoldDB; B2S162; -. DR SMR; B2S162; -. DR KEGG; bhr:BH0720; -. DR HOGENOM; CLU_008554_0_1_12; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-UniRule. DR CDD; cd00860; ThrRS_anticodon; 1. DR CDD; cd00771; ThrRS_core; 1. DR FunFam; 3.30.930.10:FF:000002; Threonine--tRNA ligase; 1. DR FunFam; 3.40.50.800:FF:000001; Threonine--tRNA ligase; 1. DR FunFam; 3.30.980.10:FF:000005; Threonyl-tRNA synthetase, mitochondrial; 1. DR Gene3D; 3.30.54.20; -; 1. DR Gene3D; 3.40.50.800; Anticodon-binding domain; 1. DR Gene3D; 3.30.930.10; Bira Bifunctional Protein, Domain 2; 1. DR Gene3D; 3.30.980.10; Threonyl-trna Synthetase, Chain A, domain 2; 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; 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; 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; SSF55186; ThrRS/AlaRS common domain; 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..583 FT /note="Threonine--tRNA ligase" FT /id="PRO_1000098544" 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 583 AA; 68115 MW; F7759BCB7D0C2BF0 CRC64; MSEKLDRESI LYKKRHSIAH VMAEAVLELF PNTKIAIGPP IKDGFYYDFD FEKHITEDDL LLIEQKMREI LKTGSPFVKE VITKEQALML FKDEPYKMDL IRGLAITDEI SIYKSHNFTD LCKGPHVDNM GKIDPKAFKL TSIAGAYWRG DEKNKMLTRI YGTLWNNEKD LKAYLKLREE IKRRDHRKLG RELDLFSVHE DIGPGLIFFH PNGARIRAII EDFWREEHFK NGYDVLFTPH IGKSCLWETS GHLDFYKESM FEKMEMDKSN YYVKPMNCPF HIAIYNTGKH SYRDLPFRWA ELGTVYRYEK IGALHGTMRV RGFTQDDAHI ICAYEQVKSE VQEVLRFALY MWNQFGFADL KAYLSTKPEK AVGDKDDWEM SVKVLEEALI DLNIAYDIDE GGGAFYGPKI DLKIIDSLGR EWQMSTIQFD FNLPERFKMT YTAEDGKEKR PFMIHRALLG SIERFFGILV EHYGGAFPVW LAPLQVIIIP VNNVVEEYAL EILSLFKNEG IRIKLDNDCN MRMNAKIRQY QSKKVPYMFI IGEKEVVEGK ISIRTRTNDQ INGLELKEAL EFVRLKVKNK EIL //