ID   SYL_RALN1               Reviewed;         877 AA.
AC   Q8XVT3;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   27-MAR-2024, entry version 123.
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};
GN   OrderedLocusNames=RSc2744; ORFNames=RS00110;
OS   Ralstonia nicotianae (strain GMI1000) (Ralstonia solanacearum).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Ralstonia.
OX   NCBI_TaxID=267608;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GMI1000;
RX   PubMed=11823852; DOI=10.1038/415497a;
RA   Salanoubat M., Genin S., Artiguenave F., Gouzy J., Mangenot S., Arlat M.,
RA   Billault A., Brottier P., Camus J.-C., Cattolico L., Chandler M.,
RA   Choisne N., Claudel-Renard C., Cunnac S., Demange N., Gaspin C., Lavie M.,
RA   Moisan A., Robert C., Saurin W., Schiex T., Siguier P., Thebault P.,
RA   Whalen M., Wincker P., Levy M., Weissenbach J., Boucher C.A.;
RT   "Genome sequence of the plant pathogen Ralstonia solanacearum.";
RL   Nature 415:497-502(2002).
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}.
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; AL646052; CAD16451.1; -; Genomic_DNA.
DR   RefSeq; WP_011002651.1; NC_003295.1.
DR   AlphaFoldDB; Q8XVT3; -.
DR   SMR; Q8XVT3; -.
DR   STRING; 267608.RSc2744; -.
DR   EnsemblBacteria; CAD16451; CAD16451; RSc2744.
DR   GeneID; 60502246; -.
DR   KEGG; rso:RSc2744; -.
DR   PATRIC; fig|267608.8.peg.2791; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   Proteomes; UP000001436; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit.
DR   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..877
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152069"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           636..640
FT                   /note="'KMSKS' region"
FT   BINDING         639
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   877 AA;  97368 MW;  16DAD3713614475F CRC64;
     MQDKYSPSEV EQQAQQHWQA QDAYRVTEHA RAADGSDKPK FYACSMLPYP SGKLHMGHVR
     NYTINDVMMR QLRMKGYNVL MPMGWDAFGM PAENAALNNG VAPAAWTYDN IAYMKKQMQS
     MGLAIDWSRE VATCSPDYYK WNQWLFLKML EKGIAYRKTG TVNWDPIDQT VLANEQVIDG
     RGWRSGAVVE KREIPMYYLR ITDYAQELLS DLDPLGWPER VKLMQQNWIG KSEGVRFAFP
     HGIPGDDGKV IGDGKLYVFT TRADTIMGVT FCAVAAEHPI AAHAAQGNPA LAAFIDECKH
     GSVMEADMAT MEKKGMPTGL TVTHPLTGEA VPVWVGNYVL MTYGDGAVMG VPAHDERDFA
     FANKYGLAIK QVIDVKGQPF GTEAWQEWYA DKERGVLVHS GKYDGLDYRQ AVDAVAADLA
     AQGLGEKKTT WRLRDWGISR QRYWGTPIPL IHCDSCGVVP VPEQDLPVRL PEDLVPDGSG
     NPLAKDARFL ECTCPSCGKP ARRETDTMDT FIDSCWYYMR YTCPDGATMV DGRNDYWMPM
     DQYIGGIEHA ILHLLYARFW TKVMRDLGLV KFDEPFTKLL TQGMVLNETY YREDAAGKKQ
     WINPADVDVQ TDDRGRPIGA TLKADGQPVV IGGVEKMSKS KNNGIDPQAL IDQYGADTAR
     LFTMFAAPPE QQLEWSDAGV EGASRFLRRA WNFGVAHAES IRAGHGNGVV NGATDADRAL
     RRELHTVLKQ ANYDYERLQY NTVVSAAMKM LNALEGAKDA GADARREGLG ILLRVLYPVV
     PHITHVLWQE LGYAGAYGGL LDAPWPQVDE GALVQSEIEL VLQVNGKVRG SIVVPADADR
     AAIEAIAAKD EAVHRFAEGK PPKKIIVVPG RLVNVVA
//