SYL_THEP1
ID SYL_THEP1 Reviewed; 824 AA.
AC A5IKQ3;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=Tpet_0757;
OS Thermotoga petrophila (strain ATCC BAA-488 / DSM 13995 / JCM 10881 /
OS RKU-1).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=390874;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-488 / DSM 13995 / JCM 10881 / RKU-1;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Mikhailova N., Nelson K., Gogarten J.P., Noll K., Richardson P.;
RT "Complete sequence of Thermotoga petrophila RKU-1.";
RL Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-leucine + tRNA(Leu) = AMP + diphosphate + L-leucyl-
CC tRNA(Leu); Xref=Rhea:RHEA:11688, Rhea:RHEA-COMP:9613, Rhea:RHEA-
CC COMP:9622, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:57427,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78494, ChEBI:CHEBI:456215; EC=6.1.1.4;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; CP000702; ABQ46776.1; -; Genomic_DNA.
DR RefSeq; WP_011943352.1; NC_009486.1.
DR AlphaFoldDB; A5IKQ3; -.
DR SMR; A5IKQ3; -.
DR STRING; 390874.Tpet_0757; -.
DR EnsemblBacteria; ABQ46776; ABQ46776; Tpet_0757.
DR KEGG; tpt:Tpet_0757; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_0; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000006558; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004823; F:leucine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 2.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR InterPro; IPR002300; aa-tRNA-synth_Ia.
DR InterPro; IPR002302; Leu-tRNA-ligase.
DR InterPro; IPR025709; Leu_tRNA-synth_edit.
DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd.
DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR PANTHER; PTHR43740; PTHR43740; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 1.
DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..824
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000071116"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 824 AA; 95623 MW; 12A34BAB6683EB3E CRC64;
MKEYRPQEIE KKWQEVWEEK KVFYTPQRSE KPKYYALVMF PYPSGTLHVG HVKNYVIGDI
VARYKRMRGY NVLHPFGYDA FGLPAENAAI EKGIHPEEWT RKNINTIRGQ VKKLGISYDW
SREIATCDEE YYKWTQWIFL QLYKNGLAYK KKAAVNWCPK CKTVLANEQV KDGKCERCGT
SVTIRHLEQW FFKITDYAER LLNDLDKLTG WPEHVKTMQR NWIGKSTGAE IDFPVEGSDT
KIRVFTTRPD TLWGVTFMAL APESPLVEEL VLEEKKEDLQ EFLERVKQQD RFRRTSVEAE
KEGFFLGRYA INPVTGERIP IYVANYILME YGTGAIMGVP AHDQRDFSFA KKYGIPIKVV
IKPADRDLDP EKMEEAYEGE GIMVNSGPFD GTPSSEGIEK VINWLEEKGI GKRSVQYKLR
DWLISRQRYW GAPIPIIYCE KCGVVPVPEE DLPVRLPKDV EFLPTGQSPL SFHEGFKRTK
CPICGGEAQR ETDTMDTFVD SSWYFLRYVN PHLEDKPFEP DDVNYWLPVD QYIGGVEHAV
LHLLYSRFVT KVLHDLGYLN FDEPFTNLFT QGMIYKDGAK MSKSKGNVVS PDEMIEKYGA
DTLRMYILFM APPEKDAEWS DAGIEGVHRF IKRLWNTFYT VLPFVKEENT ENLVLKNSTE
KELRRKLHSI IKKITEDIEG GFKFNTAISG LMELVNHLSQ YLNSVPQEEW NRKLLREIVE
KLTLALSPFA PHLAEEFWHD LGNDSLVVQQ AWPSYDPKAL EVEEVEIAIQ INGKVRDKVV
VPVDISEEAL KRIVLERERV KEYVDGKPIR KFIYVKGRIV NIVV