SYT_ARCFU
ID SYT_ARCFU Reviewed; 619 AA.
AC O29703;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 138.
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=AF_0548;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP FUNCTION, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=15507440; DOI=10.1074/jbc.m411039200;
RA Ruan B., Bovee M.L., Sacher M., Stathopoulos C., Poralla K.,
RA Francklyn C.S., Soell D.;
RT "A unique hydrophobic cluster near the active site contributes to
RT differences in borrelidin inhibition among threonyl-tRNA synthetases.";
RL J. Biol. Chem. 280:571-577(2005).
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)
CC (PubMed:15507440). Also edits incorrectly charged L-seryl-tRNA(Thr) (By
CC similarity). {ECO:0000255|HAMAP-Rule:MF_00184,
CC ECO:0000269|PubMed:15507440}.
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 -!- ACTIVITY REGULATION: Not inhibited by 1 uM borrelidin (BN); probably
CC does not bind BN. {ECO:0000269|PubMed:15507440}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for L-threonine activation {ECO:0000269|PubMed:15507440};
CC Note=kcat is 3.8 sec(-1). {ECO:0000269|PubMed:15507440};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
CC -!- DOMAIN: The N-terminal domain is an archaea-specific tRNA-editing
CC domain that hydrolyzes incorrectly charged L-seryl-tRNA(Thr). Catalysis
CC of tRNA editing is performed by the charged tRNA itself.
CC {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; AE000782; AAB90685.1; -; Genomic_DNA.
DR PIR; D69318; D69318.
DR RefSeq; WP_010878055.1; NC_000917.1.
DR AlphaFoldDB; O29703; -.
DR SMR; O29703; -.
DR STRING; 224325.AF_0548; -.
DR PRIDE; O29703; -.
DR EnsemblBacteria; AAB90685; AAB90685; AF_0548.
DR GeneID; 1483764; -.
DR KEGG; afu:AF_0548; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_029833_0_0_2; -.
DR OMA; DAHIFML; -.
DR OrthoDB; 11656at2157; -.
DR PhylomeDB; O29703; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:UniProt.
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:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
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 Gene3D; 3.50.80.10; -; 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; IPR023509; DTD-like_sf.
DR InterPro; IPR002320; Thr-tRNA-ligase_IIa.
DR InterPro; IPR015011; Threonyl-tRNA_syn_edit_dom_arc.
DR InterPro; IPR033728; ThrRS_core.
DR PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR Pfam; PF08915; tRNA-Thr_ED; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF55681; SSF55681; 1.
DR TIGRFAMs; TIGR00418; thrS; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
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..619
FT /note="Threonine--tRNA ligase"
FT /id="PRO_0000101097"
FT REGION 1..133
FT /note="Editing domain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT REGION 196..495
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 288
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 340
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 464
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 619 AA; 72150 MW; 839AB5D2EE545A02 CRC64;
MKLLLIHADY MEYEVKKKTK LAEPFDGKGE RVEEVLVAFT SVEKGDDENV VRKAAEAIRE
VAEKVNAERI MIYPYAHLSS NLADAETAVK LLKQLEAELS DFEVHRSPFG WYKAFRISCK
GHPLSELSRE IGGEAEAEVT QALKDEEEKV VSYWYILTPE KELVEVEKFD FTGYEKLRKF
VNYEIAKRRA VDVTPPHVEY MRRLELADYE PASDSGHIRY YPKGRLVKTL LEQFITRKCI
DYGAMEVETP IMYDRNHPTL RRYLERFPAR QYIIKGDKRE FFLRFAACFG QFLMLSSSTI
TYRNLPLKIY ELTRYSFRKE QRGELVGLRR LRAFTMPDMH TVAKDMEQAK EEFFNQYRLS
VEVLREIGLE PEDYEVAVRI TKDFYEENRE FVHSLVDILK KPILIEMWDH RFFYFVLKFE
FNFVDALDKA SALSTVQIDV ENAERYGITF VDSDGKEKHP YILHCSVSGA VERVMYALLE
KAKFMLDEGR LPMLPVWLSP TQVRVIPVSE RFVDAAIKIA DDIARNGIRV DVDDRNETLG
KKIRDAQTEW IPYIAVVGEK EIESGKLAVT VRAESTQKEQ KRVEMSAEEL AERVRSECEG
KPFMPLPLPK LLSLRPSFR
