ID   SYL_CUPPJ               Reviewed;         873 AA.
AC   Q46XD8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 115.
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=Reut_A2834;
OS   Cupriavidus pinatubonensis (strain JMP 134 / LMG 1197) (Cupriavidus necator
OS   (strain JMP 134)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=264198;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JMP134 / LMG 1197;
RX   PubMed=20339589; DOI=10.1371/journal.pone.0009729;
RA   Lykidis A., Perez-Pantoja D., Ledger T., Mavromatis K., Anderson I.J.,
RA   Ivanova N.N., Hooper S.D., Lapidus A., Lucas S., Gonzalez B.,
RA   Kyrpides N.C.;
RT   "The complete multipartite genome sequence of Cupriavidus necator JMP134, a
RT   versatile pollutant degrader.";
RL   PLoS ONE 5:E9729-E9729(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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAZ62195.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000090; AAZ62195.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011298980.1; NC_007347.1.
DR   AlphaFoldDB; Q46XD8; -.
DR   SMR; Q46XD8; -.
DR   STRING; 264198.Reut_A2834; -.
DR   PRIDE; Q46XD8; -.
DR   EnsemblBacteria; AAZ62195; AAZ62195; Reut_A2834.
DR   KEGG; reu:Reut_A2834; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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.
FT   CHAIN           1..873
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334800"
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;  97066 MW;  64987B16A46F6342 CRC64;
     MQDKYLPSAV EQAAQQHWQA IDAYRVPEHA TGPDGKEKPK FYACSMLPYP SGKLHMGHVR
     NYTINDVMAR YLRMNGNNVL MPMGWDAFGM PAENAALNNG VAPAAWTYDN IAYMKKQMQS
     MGLAIDWSRE VATCSPDYYR WNQWLFLKML EKGIAYRKTG TVNWDPVDQT VLANEQVIDG
     RGWRSGAIVE KREIPMYYLR ITDYAEELLG DLDGLGWPER VKIMQQNWIG KSVGVRFAFK
     HDIEGDDGQL INDGKLYVFT TRADTIMGVT FCAVAAEHPL ATHAAANNPE LAAFIDECKH
     GSVMEADMAT MEKKGMPTGL QVTHPLTGEQ VDVWVGNYVL MSYGDGAVMG VPAHDERDFA
     FANKYKLPIR QVIDVKGQPY STEAWQEWYG DKENGVCIES GKYNGLGYLA AVEAIAADLG
     AMGLGEKKIT WRLRDWGISR QRYWGTPIPL IHCDSCGVVP VPEQDLPVVL PEDLVPDGTG
     NPLNKDPRFL QCSCPSCGKP ARRETDTMDT FIDSCWYYMR YTCPDAATMV DARNDYWMPM
     DQYIGGIEHA ILHLLYARFW TKVMRDLGLV KFDEPFTNLL TQGMVLNETF YREDAAGKKT
     WYNPADVDVQ TDDRGRPVGA TLKADGQPVV IGGVEKMSKS KNNGIDPQAL IDQHGADTAR
     LFVMFAAPPE QQLEWSGSGV EGASRFLRRV WNYGFANAAA VRDGAGAAPT ADDADLRREI
     HGVLKQANYD YQRIQYNTVV SATMKMLNAL EDAKNASPVA RRECFGILLR VLYPVVPHIT
     HGLWDALGYA TQYGDLLDAP WPQVDEGALV RTEIEMVLQI NGKVRGSVTV PADADRAAIE
     TAAAASETVA KFAEGKAPKK IVVVPGRLVN VVL