ID   SYL_CORDI               Reviewed;         960 AA.
AC   Q6NEF5;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=DIP2320;
OS   Corynebacterium diphtheriae (strain ATCC 700971 / NCTC 13129 / Biotype
OS   gravis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=257309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700971 / NCTC 13129 / Biotype gravis;
RX   PubMed=14602910; DOI=10.1093/nar/gkg874;
RA   Cerdeno-Tarraga A.-M., Efstratiou A., Dover L.G., Holden M.T.G.,
RA   Pallen M.J., Bentley S.D., Besra G.S., Churcher C.M., James K.D.,
RA   De Zoysa A., Chillingworth T., Cronin A., Dowd L., Feltwell T., Hamlin N.,
RA   Holroyd S., Jagels K., Moule S., Quail M.A., Rabbinowitsch E.,
RA   Rutherford K.M., Thomson N.R., Unwin L., Whitehead S., Barrell B.G.,
RA   Parkhill J.;
RT   "The complete genome sequence and analysis of Corynebacterium diphtheriae
RT   NCTC13129.";
RL   Nucleic Acids Res. 31:6516-6523(2003).
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; BX248360; CAE50842.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q6NEF5; -.
DR   SMR; Q6NEF5; -.
DR   STRING; 257309.DIP2320; -.
DR   PRIDE; Q6NEF5; -.
DR   EnsemblBacteria; CAE50842; CAE50842; DIP2320.
DR   KEGG; cdi:DIP2320; -.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000002198; 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; Reference proteome.
FT   CHAIN           1..960
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152005"
FT   MOTIF           71..82
FT                   /note="'HIGH' region"
FT   MOTIF           729..733
FT                   /note="'KMSKS' region"
FT   BINDING         732
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   960 AA;  107162 MW;  51819FA7BEB071F8 CRC64;
     MTMTNPSGNT PDTSAGPAFR YTAELAGEIE RSWQQYWIDN GTFNAPNPVG DLAVSGDKLP
     EDKLFVQDMF PYPSGAGLHV GHPLGYIATD VFARFNRMLG KNVLHTLGYD AFGLPAEQYA
     IQTGTHPRTT TMANIANMQR QLGALGLGHD PRRSVATTDP EFYKWTQWIF LQIFNAWFDT
     KQQKARPISE LIPLLESGEV ALPEGFEGSA DSYSELDAVE KAKVVDEFRL VYRSHSMVNW
     CPGLGTVLAN EEVTADGRSE RGNFPVFRKK LSQWMMRITA YSDRLIDDLD LLDWPDKVKS
     MQRNWIGRSR GAEVDFDALG HTITVFTTRP DTLFGASYMV LAPEHELVDA LVAAGTNSYE
     GIDPRWTFGQ ATPAEAVKAY RASIAAKSDL ERQENKEKTG VYLGVNAVNP VNGESIPVFI
     GDYVLTGYGT GAIMAVPAHD TRDYEFATEF GLPIREVVAG GNIAEAAYTE SGAAVNSAND
     QGLDINGLDK QEAIAQVIEW LVDKQKGSEK IQYKLRDWLF ARQRYWGEPF PVVYDENGLA
     HALPESMLPV ELPEVEDYKP VSFDPDDADS EPHPPLAKAT EWTQVELDLG DGLKKYTRDT
     NVMPQWAGSS WYQLRYIDPT NSEAFCDIEN ERYWTGPRSA EDSGGVDLYV GGVEHAVLHL
     LYSRFWHKVL FDLGFVTSRE PYRRLFNQGY IQAFAYTDSR GVYVPAEEVE EKDGKFYYQG
     EEVNQEYGKM GKSLKNAVAP DDICRDFGAD TLRVYEMAMG PLDTSRPWST KDVIGAHRFL
     QRLWRLVVSE DDGSIVVTDA ALTDDDLKQL HRTIAGMRDD YEGLRINTVV AKAIEYVNYL
     TKAYGSTGAP RAAVEPLVIM VAAVAPHIAE ELWKRLGHND TITFVPFPEY EDKWLVDDEV
     EMPVQINGKV RARIMVPADA SQDQISEIAL ASEAVATHIE GKNVIKKIVV SGRMVNLVVK