ID   SYT_CERS4               Reviewed;         646 AA.
AC   Q3J0X4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 113.
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=RHOS4_19920; ORFNames=RSP_0385;
OS   Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG
OS   31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=272943;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC
RC   12203 / NCIMB 8253 / ATH 2.4.1.;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Richardson P., Mackenzie C.,
RA   Choudhary M., Larimer F., Hauser L.J., Land M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides 2.4.1.";
RL   Submitted (SEP-2005) 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=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; 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}.
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DR   EMBL; CP000143; ABA79560.1; -; Genomic_DNA.
DR   RefSeq; WP_011338194.1; NZ_CP030271.1.
DR   RefSeq; YP_353461.1; NC_007493.2.
DR   AlphaFoldDB; Q3J0X4; -.
DR   SMR; Q3J0X4; -.
DR   STRING; 272943.RSP_0385; -.
DR   EnsemblBacteria; ABA79560; ABA79560; RSP_0385.
DR   KEGG; rsp:RSP_0385; -.
DR   PATRIC; fig|272943.9.peg.2331; -.
DR   eggNOG; COG0441; Bacteria.
DR   OrthoDB; 9802304at2; -.
DR   PhylomeDB; Q3J0X4; -.
DR   Proteomes; UP000002703; Chromosome 1.
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; 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..646
FT                   /note="Threonine--tRNA ligase"
FT                   /id="PRO_1000020490"
FT   DOMAIN          1..63
FT                   /note="TGS"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT   REGION          247..544
FT                   /note="Catalytic"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         344
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         395
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT   BINDING         521
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ   SEQUENCE   646 AA;  73352 MW;  BEC094BCB08C81DD CRC64;
     MAQISLTFPD GKAREFPAGI TPAEVAASIS TSLGKKAISA SVDGRHYDLQ WPIETDAKIA
     IHTMADEAQA LELIRHDLAH IMARAVQELW PDVKVTIGPV VANGWYYDFD REETFTPEDL
     GAIEKRMKEI INAREAVKTE LWERARAIAY YEERGEPFKV ELVQAIPEDQ SIRMYWHGGW
     QDLCRGPHLQ HTGQVPADAF KLMSVAGAYW RGDSANKQLQ RIYGVAFKTR DELKAYLHML
     EEAAKRDHRK LGREMELFHL QEEAPGMVFW HPNGWQIYRT LEDYMRGRLR QAGYKEIRTP
     QVVDRKLWEA SGHWEAYKEN MFIVEVEEEH AKEKRINALK PMNCPCHVQV YNQGLKSYRD
     LPLRLAEFGS CHRYESSGSM HGLMRVRGFV QDDAHIFCTE DQIESECAAF IELLSSVYKD
     LGFDSFEIKL STRPEVRIGS DEAWDKVETA LENAIRKVGA AYEIDPGEGA FYGPKLDFKL
     TDAIGRKWQC GTFQVDPNLP TRLGAEYIGE DGAKHRPYML HRAILGSFER FIGILIENYA
     GKLPFWLAPR QVVVASIVSD ADPYVAEVVA ALRARGVRAE ADTRNEKINY KVREHSVGKV
     PVILAIGMQE VEARSVSVRR LGETRTESMG LDQVVDQLAA DARIPG
//