ID SYT_STRZP Reviewed; 647 AA. AC C1CLX1; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 02-SEP-2026, entry version 84. 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}; GN OrderedLocusNames=SPP_1650; OS Streptococcus pneumoniae (strain P1031). OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Streptococcaceae; OC Streptococcus. OX NCBI_TaxID=488223; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=P1031; RX PubMed=21034474; DOI=10.1186/gb-2010-11-10-r107; RA Donati C., Hiller N.L., Tettelin H., Muzzi A., Croucher N.J., RA Angiuoli S.V., Oggioni M., Dunning Hotopp J.C., Hu F.Z., Riley D.R., RA Covacci A., Mitchell T.J., Bentley S.D., Kilian M., Ehrlich G.D., RA Rappuoli R., Moxon E.R., Masignani V.; RT "Structure and dynamics of the pan-genome of Streptococcus pneumoniae and RT closely related species."; RL Genome Biol. 11:R107.1-R107.19(2010). 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; CP000920; ACO21023.1; -; Genomic_DNA. DR RefSeq; WP_000608339.1; NC_012467.1. DR AlphaFoldDB; C1CLX1; -. DR SMR; C1CLX1; -. DR KEGG; spp:SPP_1650; -. DR HOGENOM; CLU_008554_3_2_9; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0140096; F:catalytic activity, acting on a protein; IEA:UniProtKB-ARBA. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-ARBA. 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 FunFam; 3.10.20.30:FF:000005; Threonine--tRNA ligase; 1. DR FunFam; 3.30.54.20:FF:000002; Threonine--tRNA ligase; 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; 3.10.20.30; -; 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; 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:SF56; THREONINE--TRNA LIGASE 1; 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; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1..647 FT /note="Threonine--tRNA ligase" FT /id="PRO_1000199572" FT DOMAIN 1..61 FT /note="TGS" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228" FT REGION 242..540 FT /note="Catalytic" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184" FT BINDING 336 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184" FT BINDING 387 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184" FT BINDING 517 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184" SQ SEQUENCE 647 AA; 74664 MW; 311E63158C457877 CRC64; MINITFPDGA VREFESGVTT FEIAQSISNS LAKKALAGKF NGKLIDTTRA ITEDGSIEIV TPDHEDALPI LRHSAAHLFA QAARRLFPDI HLGVGPAIED GFYYDTDNTA GQISNEDLPR IEEEMQKIVK ENFPSIREEV TKDEAREIFK NDPYKLELIE EHSEDEGGLT IYRQGEYVDL CRGPHVPSTG RIQIFHLLHV AGAYWRGNSD NAMMQRIYGT AWFDKKDLKN YLQMREEAKE RDHRKLGKEL DLFIISQEVG QGLPFWLPNG ATIRRELERY IVNKELASGY QHVYTPPLAS VELYKTSGHW DHYQEDMFPT MDMGDGEEFV LRPMNCPHHI QVFKHHVHSY RELPIRIAEI GMMHRYEKSG ALTGLQRVRE MSLNDGHLFV TPEQIQEEFQ RALQLIIDVY EDFNLTDYRF RLSLRDPQDT HKYFDNDEMW ENAQTMLRAA LDEMGVNYFE AEGEAAFYGP KLDIQIKTAL GKEETLSTIQ LDFLLPERFD LKYIGADGED HRPVMIHRGV ISTMERFTAI LIENYKGAFP TWLAPHQVTL IPVSNEKHVD YAWEVAKKLR DRGVRADVDE RNEKMQFKIR ASQTSKIPYQ LIVGDKEMED ETVNVRRYGQ KETQTVSVDN FVQAILADIA NKSRVEK //