ID   SYL_CORGB               Reviewed;         952 AA.
AC   A4QI59;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=cgR_2905;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
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; AP009044; BAF55925.1; -; Genomic_DNA.
DR   RefSeq; WP_006286817.1; NC_009342.1.
DR   AlphaFoldDB; A4QI59; -.
DR   SMR; A4QI59; -.
DR   EnsemblBacteria; BAF55925; BAF55925; cgR_2905.
DR   GeneID; 58309678; -.
DR   KEGG; cgt:cgR_2905; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; A4QI59; -.
DR   Proteomes; UP000006698; 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; -; 3.
DR   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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..952
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009333"
FT   MOTIF           66..77
FT                   /note="'HIGH' region"
FT   MOTIF           722..726
FT                   /note="'KMSKS' region"
FT   BINDING         725
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   952 AA;  106747 MW;  CA1A789CF8EAE151 CRC64;
     MTNPSEGTTP LAFRYTPELA NKIEGEWQNY WTDNGTFNAP NPVGDLAPAD GKALPEDKLF
     VQDMFPYPSG AGLHVGHPLG YIATDVFARY NRMLGKNVLH TLGYDAFGLP AEQYAIQTGT
     HPRTTTMANI ENMKRQLGAL GLGHDSRRAV ATTDPEFYKW TQWIFLQIFN SWFDAEQQKA
     RPISELIPLL ESGELKTKDG ADYNALGDVE KQKAVDDYRL VYRSNSTVNW CPGLGTVLAN
     EEVTADGRSE RGNFPVFRKN LSQWMMRITA YSDRLIDDLE LLDWTEKVKS MQRNWIGRSR
     GAEVDFSAEG ETVTVFTTRP DTLFGATYMV LAPEHELVDV LLEKAGSYEG VDARWTNGQA
     SPAEAVAAYR ASIAAKSDLE RQENKEKTGV FLGVYATNPV NGDQIPVFIA DYVLTGYGTG
     AIMAVPAHDE RDYEFATVLG LPIKEVVAGG NIEEAAFTES GEAVNSANDN GLDINGLAKD
     EAVAKTIEWL EEKELGRGTI QYKLRDWLFA RQRYWGEPFP IVYDENGQAH ALPDSMLPVE
     LPEVEDYKPV SFDPEDADSE PSPPLAKARE WVEVELDLGD GKKKYTRDTN VMPQWAGSSW
     YQLRYVDPSN DEQFCNIENE RYWTGPRPET HGPNDPGGVD LYVGGVEHAV LHLLYARFWH
     KVLFDLGHVS SKEPYRRLYN QGYIQAFAYT DSRGVYVPAD DVEEKDGKFF YQGEEVNQEY
     GKMGKSLKNA VAPDDICNNF GADTLRVYEM AMGPLDTSRP WATKDVVGAQ RFLQRLWRLV
     VDENTGEVLT RDEVLTDDDN KQLHRTIAGV RDDYTNLRVN TVVAKLIEYV NYLTKTYPDT
     IPAGAVLPLI VMVSPVAPHI AEELWKKLGH DDTVTYEPFP TFEEKWLTDD EIELPVQVNG
     KVRGRITVAA DASQEQVIEA ALADEKVQEQ ISGKNLIKQI VVPGRMVNLV VK