ID A0A158GEC1_9BURK Unreviewed; 410 AA.
AC A0A158GEC1;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=threonine--tRNA ligase {ECO:0000256|ARBA:ARBA00013163};
DE EC=6.1.1.3 {ECO:0000256|ARBA:ARBA00013163};
GN ORFNames=AWB69_02387 {ECO:0000313|EMBL:SAL29730.1};
OS Caballeronia udeis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=1232866 {ECO:0000313|EMBL:SAL29730.1, ECO:0000313|Proteomes:UP000054683};
RN [1] {ECO:0000313|EMBL:SAL29730.1, ECO:0000313|Proteomes:UP000054683}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 27134 {ECO:0000313|EMBL:SAL29730.1};
RA Oliw E.H.;
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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:0000256|ARBA:ARBA00000070};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FCOK02000012; SAL29730.1; -; Genomic_DNA.
DR RefSeq; WP_062085049.1; NZ_FCOK02000012.1.
DR AlphaFoldDB; A0A158GEC1; -.
DR OrthoDB; 9802304at2; -.
DR Proteomes; UP000054683; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:InterPro.
DR CDD; cd00771; ThrRS_core; 1.
DR Gene3D; 3.40.50.800; Anticodon-binding domain; 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; IPR033728; ThrRS_core.
DR NCBIfam; TIGR00418; thrS; 1.
DR PANTHER; PTHR11451:SF44; THREONINE--TRNA LIGASE, CHLOROPLASTIC_MITOCHONDRIAL 2; 1.
DR PANTHER; PTHR11451; THREONINE-TRNA LIGASE; 1.
DR Pfam; PF03129; HGTP_anticodon; 1.
DR Pfam; PF00587; tRNA-synt_2b; 1.
DR PRINTS; PR01047; TRNASYNTHTHR.
DR SUPFAM; SSF52954; Class II aaRS ABD-related; 1.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW ECO:0000313|EMBL:SAL29730.1}; ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917}.
FT DOMAIN 5..306
FT /note="Aminoacyl-transfer RNA synthetases class-II family
FT profile"
FT /evidence="ECO:0000259|PROSITE:PS50862"
SQ SEQUENCE 410 AA; 47094 MW; 1B5BA9345012B610 CRC64;
MGNIDHRQLG NKLNLFHQQD EGPGMVFWHP RGWELYRVVE DYIRRRMRGA GFREVRTPQL
LARSLWERSG HWDKFQAAMY SVNGSQDEAR DEAHESQPYC LKPMSCPCHV QIFNQRIRSY
RDLPIRYSEF GACHRDEPSG SLEGLKRTRA FTQDDAHVFC TEDQVKAELG QFCDLLRVVY
ADLGFSTFRV QLATRPEQRA GDDAVWDRAE EALAKAAVSA GLTFDVRPGE GAFYGPKLEF
HLTDSRDRSW QCGTIQLDFV LPDRLDASFV SFENEHVRPV MIHHAVLGSM ERFIAMLLEH
HEGWLPLWLA PDQVTVATVS DASAAYGQRV MDLLDEAGLR AVFDDRPERL ERKIVDAREQ
RIPVFITVGA RDQRDETVSL RFRDGTQDTF PIHEGVAHLR ERGRTPAKAR
//
