SYT_BUCAP
ID SYT_BUCAP Reviewed; 642 AA.
AC P46244;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 30-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=BUsg_117;
OS Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=198804;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7766160; DOI=10.1007/bf00295507;
RA Kolibachuk D., Rouhbakhsh D., Baumann P.;
RT "Aromatic amino acid biosynthesis in Buchnera aphidicola (endosymbiont of
RT aphids): cloning and sequencing of a DNA fragment containing aroH-thrS-
RT infC-rpmI-rplT.";
RL Curr. Microbiol. 30:313-316(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sg;
RX PubMed=12089438; DOI=10.1126/science.1071278;
RA Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT "50 million years of genomic stasis in endosymbiotic bacteria.";
RL Science 296:2376-2379(2002).
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; U11066; AAC43605.1; -; Genomic_DNA.
DR EMBL; AE013218; AAM67686.1; -; Genomic_DNA.
DR PIR; I40071; I40071.
DR RefSeq; WP_011053652.1; NC_004061.1.
DR AlphaFoldDB; P46244; -.
DR SMR; P46244; -.
DR STRING; 198804.BUsg_117; -.
DR PRIDE; P46244; -.
DR EnsemblBacteria; AAM67686; AAM67686; BUsg_117.
DR KEGG; bas:BUsg_117; -.
DR eggNOG; COG0441; Bacteria.
DR HOGENOM; CLU_008554_0_1_6; -.
DR OMA; FYYDFAY; -.
DR OrthoDB; 900765at2; -.
DR Proteomes; UP000000416; Chromosome.
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; 3.10.20.30; -; 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; IPR012675; Beta-grasp_dom_sf.
DR InterPro; IPR004095; TGS.
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.
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..642
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000100951"
FT DOMAIN 1..61
FT /note="TGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01228"
FT REGION 243..534
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 334
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 385
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 511
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT CONFLICT 19..22
FT /note="SLRE -> LIER (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 26
FT /note="N -> I (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 49
FT /note="T -> S (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 86
FT /note="T -> R (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="C -> S (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 100..116
FT /note="SGFYCDIDFENSITEED -> VVFIVILILKIVLQKKI (in Ref. 1;
FT AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 191
FT /note="K -> R (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 197..199
FT /note="KLQ -> NY (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..289
FT /note="EYK -> GIIN (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 300
FT /note="D -> H (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 316
FT /note="A -> R (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 530..533
FT /note="SGKL -> QEI (in Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
FT CONFLICT 584..603
FT /note="EHTLRQIPYILICGEKEIKS -> ATYIASNSIYINLWRKEKLNL (in
FT Ref. 1; AAC43605)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 642 AA; 76227 MW; BC0AF5338B09EBF6 CRC64;
MPVIRFCDGS QQVYKHSVSL REIIENKKPN IIRSLIAISV NNSFSNFNTL ITEDSSISFI
SKKDCEALNI IRYSCIQLLN YAAKKTWPSC KIGESEITKS GFYCDIDFEN SITEEDFFIL
ENNMKTLIKR EYFISHQNIS FDHAYEMFKK KSEIYKIHLI KKYINKKNKI SLYYHENYFD
IDMGMQVFNI KFCKYFKLQK IGGIYWKGDH KNKMLQRIYG TAWSTKKELD KHLSYINELK
KRDHRKIGKL LNLYHMQKES PGMIFWHNNG WIIFNELEIF VREKLKEYKY KEVKTPLLID
KSIWQKSGHW DNYQDAIFTT SSENREYCIK PMNCPGHVQI FNCGLKSYRD LPIRMAEFGS
CHRNESSGSL HGLMRIRNFT QDDAHIFCTQ EQLRYEINNC IKMIYDLYST FNFKKILVKF
STRPKKRIGD ESVWDQAEKD LSDVLIENNL KFEHQEGEGA FYGPKIEFVL QDSLDRNWQC
GTIQLDFYLP IRLRSFYIDE HNHQKIPIII HRAILGSIER FIGILIEEFS GKLPTWLSPI
QVVILSITDS HINYVKKIVQ HFSDINIRVE SDLRNEKIGF KIREHTLRQI PYILICGEKE
IKSKKISVRT RNGYNLGIID IDCFIKKLQK EIFTRSFYQM EE
