SYTC_SACS2
ID SYTC_SACS2 Reviewed; 545 AA.
AC Q97VW8;
DT 30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Threonine--tRNA ligase catalytic subunit;
DE EC=6.1.1.3;
DE AltName: Full=Threonyl-tRNA synthetase catalytic subunit {ECO:0000303|PubMed:15240874};
DE Short=ThrRS-cat {ECO:0000303|PubMed:15240874};
GN Name=thrS-cat {ECO:0000303|PubMed:15240874}; OrderedLocusNames=SSO2486;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=15240874; DOI=10.1073/pnas.0403926101;
RA Korencic D., Ahel I., Schelert J., Sacher M., Ruan B., Stathopoulos C.,
RA Blum P., Ibba M., Soell D.;
RT "A freestanding proofreading domain is required for protein synthesis
RT quality control in Archaea.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:10260-10265(2004).
RN [3]
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:15240874). Also activates L-serine and transfers it to
CC tRNA(Thr); unlike most archaea the editing function is found in a
CC freestanding protein (ACQ980D1) (PubMed:15240874). In vitro when both
CC subunits are present, or if the 2 subunits are fused, L-seryl-tRNA(Thr)
CC is no longer produced, the 2 subunits edit incorrectly charged L-seryl-
CC tRNA(Thr) (PubMed:15240874). Has no activity on correctly acylated L-
CC seryl-tRNA(Ser) or L-threonyl-tRNA(Thr). {ECO:0000269|PubMed:15240874}.
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: Inhibited by 1 uM borrelidin (BN).
CC {ECO:0000269|PubMed:15507440}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=55 mM for L-serine activation {ECO:0000269|PubMed:15240874};
CC KM=0.11 mM for L-threonine activation {ECO:0000269|PubMed:15240874};
CC KM=100 uM for L-threonine activation {ECO:0000269|PubMed:15507440};
CC Note=kcat is 1.3 sec(-1) for L-serine, 1.9 for L-threonine at 60
CC degrees Celsius (PubMed:15240874). {ECO:0000269|PubMed:15240874};
CC -!- SUBUNIT: Homodimer (By similarity). Probably interacts with its editing
CC subunit (AC Q980D1); a subunit fusion (in the order edit-catalytic) is
CC fully functional. {ECO:0000250|UniProtKB:Q9YDW0,
CC ECO:0000305|PubMed:15240874}.
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; AE006641; AAK42622.1; -; Genomic_DNA.
DR PIR; G90420; G90420.
DR RefSeq; WP_010923890.1; NC_002754.1.
DR AlphaFoldDB; Q97VW8; -.
DR SMR; Q97VW8; -.
DR STRING; 273057.SSO2486; -.
DR EnsemblBacteria; AAK42622; AAK42622; SSO2486.
DR GeneID; 7808880; -.
DR KEGG; sso:SSO2486; -.
DR PATRIC; fig|273057.12.peg.2567; -.
DR eggNOG; arCOG00401; Archaea.
DR HOGENOM; CLU_008554_0_1_2; -.
DR InParanoid; Q97VW8; -.
DR OMA; FYYDFAY; -.
DR PhylomeDB; Q97VW8; -.
DR Proteomes; UP000001974; 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; IDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IDA:UniProtKB.
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 PANTHER; PTHR11451; PTHR11451; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF55186; SSF55186; 1.
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..545
FT /note="Threonine--tRNA ligase catalytic subunit"
FT /id="PRO_0000101113"
FT REGION 139..433
FT /note="Catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 231
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 282
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
FT BINDING 410
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00184"
SQ SEQUENCE 545 AA; 63231 MW; D9CEA476A1A192B1 CRC64;
MESYKPVWLK GAVILAINLI DKGYKPVAVG LGERDFYIDV KSDTSITLDE VKKAINENVL
ANVSIENNQI VYKGNKVSII EDKVSISTNL NPKYFEILNI STHHPNPNEQ YVRIRGVAFE
TEEQLKDYLS WLEKAEETDH RLIGEKLDLF SFHEEAGSGL VLFHPKGQTI RNELIAFMRE
INDSMGYQEV YTSHVFKTDI WKISGHYTLY RDKLIVFNME GDEYGVKPMN CPAHILIYKS
KPRTYRDLPI RFSEFGHVYR WEKKGELYGL LRVRGFVQDD GHIFLREDQL REEIKMLISK
TVEVWHKFGF KDDDIKPYLS TRPDESIGSD ELWEKATNAL ISALQESGLK FGIKEKEGAF
YGPKIDFEIR DSLGRWWQLS TIQVDFNLPE RFKLEYIDKD GIKKRPVMVH RAIYGSIDRF
VAILLEHFKG KLPTWLSSVQ VRVLPITDEV NEYAEKVLND MRKRRIRAEI DYAGETLSKR
IKNAYDQGVP YILIVGKKEA SEGTVTVRAR GNIEVRNVKF EKFLELLITE IAQRDVEQTT
VKALK
