ID   SYL_CUPMC               Reviewed;         873 AA.
AC   Q1LJ30;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
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=Rmet_2973;
OS   Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS   CH34) (Ralstonia metallidurans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=266264;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX   PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA   Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA   Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA   Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT   "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT   master survivalist in harsh and anthropogenic environments.";
RL   PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF09846.1; -; Genomic_DNA.
DR   RefSeq; WP_011517508.1; NC_007973.1.
DR   AlphaFoldDB; Q1LJ30; -.
DR   SMR; Q1LJ30; -.
DR   STRING; 266264.Rmet_2973; -.
DR   EnsemblBacteria; ABF09846; ABF09846; Rmet_2973.
DR   KEGG; rme:Rmet_2973; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002429; 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   Gene3D; 3.90.740.10; -; 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; 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; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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; Reference proteome.
FT   CHAIN           1..873
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009406"
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   873 AA;  96869 MW;  5641A1642E217597 CRC64;
     MQDKYLPSAV EQAAQQHWKA IDAYKVSEHA VGPDGKEKSK FYACSMLPYP SGKLHMGHVR
     NYTINDVMAR YLRMNGRNVL MPMGWDAFGM PAENAALNNG VAPAAWTYDN IAYMKKQMQS
     MGLAIDWSRE VATCSPEYYR WNQWLFLKML EKGIAYRKTG TVNWDPVDQT VLANEQVIDG
     RGWRSGAVVE KREIPMYYLR ITDYAQELLG DLEGLGWPER VKIMQQNWIG RSEGVRFAFP
     HEIKGADGKL INDGKLYVFT TRADTIMGVT FCAVAAEHPL ATHAAESNPA LAAFIEECKH
     GSVMEADMAT MEKKGMPTGL KVTHPLTGEQ VDVWVGNYVL MTYGDGAVMG VPAHDERDFA
     FALKYNLPIK QVIDVKGQAY STDAWLEWYG DKEHGLCIHS GKYDGLGYKA AVDAIAADLA
     AKGLGEKKVT WRLRDWGISR QRYWGTPIPL IHCDSCGVVP VPEKDLPVVL PEDLVPDGTG
     NPLAKDPRFL ECTCPSCGKP ARRETDTMDT FIDSCWYYMR YTCPDAGTMV DARNDYWMPM
     DQYIGGIEHA ILHLLYARFW TKVMRDMGLV KFDEPFTNLL TQGMVLNETF YREDASGKKT
     WYNPADVDVQ TDERGRPAGA TAKADGQPVV IGGIEKMSKS KNNGIDPQAL IDQYGADTAR
     LFVMFAAPPE QQLEWSGSGV EGASRFLRRV WNYGYANAQA IRDGAGTAPT ADDAALRREI
     HTVLKQANYD YERIQYNTVV SATMKMLNAL EDAKTASPAG RREGFSVLLR VLYPVVPHIA
     HGLWQELGYA AETVDILDAA WPQVDEAALV RSEIELVLQV NGKVRGSLTV PADADRAAIE
     ATAAASEIVA KFAAGAAPKK IVVVPGRLVN VVL