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Threonine--tRNA ligase catalytic subunit (EC 6.1.1.3) (Threonyl-tRNA synthetase catalytic subunit) (ThrRS-cat)

 SYTC_SULSO              Reviewed;         545 AA.
Q97VW8;
30-AUG-2002, integrated into UniProtKB/Swiss-Prot.
01-OCT-2001, sequence version 1.
28-FEB-2018, entry version 100.
RecName: Full=Threonine--tRNA ligase catalytic subunit;
EC=6.1.1.3;
AltName: Full=Threonyl-tRNA synthetase catalytic subunit {ECO:0000303|PubMed:15240874};
Short=ThrRS-cat {ECO:0000303|PubMed:15240874};
Name=thrS-cat {ECO:0000303|PubMed:15240874};
OrderedLocusNames=SSO2486;
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 /
P2).
Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
Sulfolobus.
NCBI_TaxID=273057;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=11427726; DOI=10.1073/pnas.141222098;
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G.,
Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A.,
De Moors A., Erauso G., Fletcher C., Gordon P.M.K.,
Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X.,
Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N.,
Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
"The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
[2]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT.
STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
PubMed=15240874; DOI=10.1073/pnas.0403926101;
Korencic D., Ahel I., Schelert J., Sacher M., Ruan B.,
Stathopoulos C., Blum P., Ibba M., Soell D.;
"A freestanding proofreading domain is required for protein synthesis
quality control in Archaea.";
Proc. Natl. Acad. Sci. U.S.A. 101:10260-10265(2004).
[3]
FUNCTION, ENZYME REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=15507440; DOI=10.1074/jbc.M411039200;
Ruan B., Bovee M.L., Sacher M., Stathopoulos C., Poralla K.,
Francklyn C.S., Soell D.;
"A unique hydrophobic cluster near the active site contributes to
differences in borrelidin inhibition among threonyl-tRNA
synthetases.";
J. Biol. Chem. 280:571-577(2005).
-!- FUNCTION: Catalyzes the attachment of threonine to tRNA(Thr) in a
two-step reaction: L-threonine is first activated by ATP to form
Thr-AMP and then transferred to the acceptor end of tRNA(Thr)
(PubMed:15240874). Also activates L-serine and transfers it to
tRNA(Thr); unlike most archaea the editing function is found in a
freestanding protein (ACQ980D1) (PubMed:15240874). In vitro when
both subunits are present, or if the 2 subunits are fused, L-
seryl-tRNA(Thr) is no longer produced, the 2 subunits edit
incorrectly charged L-seryl-tRNA(Thr) (PubMed:15240874). Has no
activity on correctly acylated L-seryl-tRNA(Ser) or L-threonyl-
tRNA(Thr). {ECO:0000269|PubMed:15240874}.
-!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP +
diphosphate + L-threonyl-tRNA(Thr). {ECO:0000255|HAMAP-
Rule:MF_00184}.
-!- COFACTOR:
Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
Evidence={ECO:0000255|HAMAP-Rule:MF_00184};
Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
Rule:MF_00184};
-!- ENZYME REGULATION: Inhibited by 1 uM borrelidin (BN).
{ECO:0000269|PubMed:15507440}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=55 mM for L-serine activation {ECO:0000269|PubMed:15240874};
KM=0.11 mM for L-threonine activation
{ECO:0000269|PubMed:15240874};
KM=100 uM for L-threonine activation
{ECO:0000269|PubMed:15507440};
Note=kcat is 1.3 s(-1) for L-serine, 1.9 for L-threonine at 60
degrees Celsius (PubMed:15240874).
{ECO:0000269|PubMed:15240874};
-!- SUBUNIT: Homodimer (By similarity). Probably interacts with its
editing subunit (AC Q980D1); a subunit fusion (in the order edit-
catalytic) is fully functional. {ECO:0000250|UniProtKB:Q9YDW0,
ECO:0000305|PubMed:15240874}.
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00184}.
-!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
family. {ECO:0000255|HAMAP-Rule:MF_00184}.
-----------------------------------------------------------------------
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-----------------------------------------------------------------------
EMBL; AE006641; AAK42622.1; -; Genomic_DNA.
PIR; G90420; G90420.
RefSeq; WP_010923890.1; NC_002754.1.
ProteinModelPortal; Q97VW8; -.
SMR; Q97VW8; -.
STRING; 273057.SSO2486; -.
EnsemblBacteria; AAK42622; AAK42622; SSO2486.
GeneID; 7808880; -.
KEGG; sso:SSO2486; -.
PATRIC; fig|273057.12.peg.2567; -.
eggNOG; arCOG00401; Archaea.
eggNOG; COG0441; LUCA.
HOGENOM; HOG000003878; -.
InParanoid; Q97VW8; -.
KO; K01868; -.
OMA; FYYDFAY; -.
OrthoDB; POG093Z01GO; -.
Proteomes; UP000001974; Chromosome.
GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0004829; F:threonine-tRNA ligase activity; IDA:UniProtKB.
GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
GO; GO:0006435; P:threonyl-tRNA aminoacylation; IDA:UniProtKB.
CDD; cd00771; ThrRS_core; 1.
Gene3D; 3.40.50.800; -; 1.
HAMAP; MF_00184; Thr_tRNA_synth; 1.
InterPro; IPR002314; aa-tRNA-synt_IIb.
InterPro; IPR006195; aa-tRNA-synth_II.
InterPro; IPR004154; Anticodon-bd.
InterPro; IPR036621; Anticodon-bd_dom_sf.
InterPro; IPR002320; Thr-tRNA-ligase_IIa.
InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit.
InterPro; IPR033728; ThrRS_core.
PANTHER; PTHR11451; PTHR11451; 1.
Pfam; PF03129; HGTP_anticodon; 1.
Pfam; PF00587; tRNA-synt_2b; 1.
PRINTS; PR01047; TRNASYNTHTHR.
SUPFAM; SSF55186; SSF55186; 1.
TIGRFAMs; TIGR00418; thrS; 1.
PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
1: Evidence at protein level;
Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis;
Reference proteome; RNA-binding; tRNA-binding; Zinc.
CHAIN 1 545 Threonine--tRNA ligase catalytic subunit.
/FTId=PRO_0000101113.
REGION 139 433 Catalytic. {ECO:0000255|HAMAP-
Rule:MF_00184}.
METAL 231 231 Zinc. {ECO:0000255|HAMAP-Rule:MF_00184}.
METAL 282 282 Zinc; via tele nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00184}.
METAL 410 410 Zinc; via pros nitrogen.
{ECO:0000255|HAMAP-Rule:MF_00184}.
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


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