SYT_TROW8
ID SYT_TROW8 Reviewed; 640 AA.
AC Q83HM3;
DT 30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=TW508;
OS Tropheryma whipplei (strain TW08/27) (Whipple's bacillus).
OC Bacteria; Actinobacteria; Micrococcales; Tropherymataceae; Tropheryma.
OX NCBI_TaxID=218496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TW08/27;
RX PubMed=12606174; DOI=10.1016/s0140-6736(03)12597-4;
RA Bentley S.D., Maiwald M., Murphy L.D., Pallen M.J., Yeats C.A., Dover L.G.,
RA Norbertczak H.T., Besra G.S., Quail M.A., Harris D.E., von Herbay A.,
RA Goble A., Rutter S., Squares R., Squares S., Barrell B.G., Parkhill J.,
RA Relman D.A.;
RT "Sequencing and analysis of the genome of the Whipple's disease bacterium
RT Tropheryma whipplei.";
RL Lancet 361:637-644(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; BX251411; CAD67175.1; -; Genomic_DNA.
DR RefSeq; WP_011096455.1; NC_004551.1.
DR AlphaFoldDB; Q83HM3; -.
DR SMR; Q83HM3; -.
DR GeneID; 67388287; -.
DR KEGG; tws:TW508; -.
DR HOGENOM; CLU_008554_0_1_11; -.
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..640
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101079"
FT REGION 224..525
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 323
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 374
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 502
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 640 AA; 73145 MW; C79DF797FE686678 CRC64;
MDGFEFFSGR SDVVAMICDD RLLDLSESIP SGKVPEPIEL DSPRGLDILR HSCAHVLAQA
VQSIYGDAKL GIGPFTENGF YYDFSVNEPF SSDSLRVIED KMREIVHSDQ KFVRKVVDRQ
SAHSQFRDEP FKLEIINATD DTLSIYYNID ADSGSVRWMD FCRGPHLPST RFIGDAFALT
HVSSVYWRGN SDNPQMQRVY GTAWGSAKDL KGYLDRVELA KLVDHRKLGK ELDLFSLPDE
IGPGLALFHV KGGIIRSEME QYARLRHLEE GYNFVYSPHI TKRDLFERSG HLQWYGQSMF
PPMRLDKDSC SQGFDYYLKP MNCPFHSLVF SSQPRSYRQL PLRLAEFGTV YRYEQSGAIH
GLARVRGLTQ DDAHIYATRE SFEDEVSKAL QFTISLLGDY GLDQFYIEIS TRDASGKFLG
SDEDWAYATH ILQKVAQDSG LQTRDDPGGA AFYGPKISVQ AKDAIGRYWQ MSTIQLDFNL
PERFGLFYTD RAGERKRPIM VHRALFGSFE RFFAVLTEHY AGAFPPWLSP EQVVALPVTS
AHIPYLEEFV SRFSSRLIRA RVDYMQDRLP KKIRSYVKEK IPFVLVAGDR DLTNRTVAIR
FRDGTQISDL PIQKCFDGIC ASIDRKKQIQ TRIDFDSVLE
