ID   SYL_CLONN               Reviewed;         812 AA.
AC   A0PYK3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=NT01CX_1372;
OS   Clostridium novyi (strain NT).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=386415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NT;
RX   PubMed=17115055; DOI=10.1038/nbt1256;
RA   Bettegowda C., Huang X., Lin J., Cheong I., Kohli M., Szabo S.A., Zhang X.,
RA   Diaz L.A. Jr., Velculescu V.E., Parmigiani G., Kinzler K.W., Vogelstein B.,
RA   Zhou S.;
RT   "The genome and transcriptomes of the anti-tumor agent Clostridium novyi-
RT   NT.";
RL   Nat. Biotechnol. 24:1573-1580(2006).
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; CP000382; ABK61363.1; -; Genomic_DNA.
DR   RefSeq; WP_011721463.1; NC_008593.1.
DR   AlphaFoldDB; A0PYK3; -.
DR   SMR; A0PYK3; -.
DR   STRING; 386415.NT01CX_1372; -.
DR   EnsemblBacteria; ABK61363; ABK61363; NT01CX_1372.
DR   KEGG; cno:NT01CX_1372; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008220; 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   HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
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   PANTHER; PTHR43740; PTHR43740; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   PRINTS; PR00985; TRNASYNTHLEU.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..812
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009328"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           572..576
FT                   /note="'KMSKS' region"
FT   BINDING         575
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   812 AA;  92378 MW;  D95725B24357888A CRC64;
     MGNYGTTVDE KWQKKWEESG LHNFDENAPG EKLYVLEMFS YPSAAKLHAG HWFNYGPTDS
     WARFKKMNGY NVFQPMGFDA FGLPAENFAI KTGIHPQDST MKNIENMEEQ LRSMGAMFNW
     DHEIITCLPD YYKWTQWVFL KLYEKGLAYR KNAPVNWCPS CNTVLANEQV LDGHCERCDS
     LVEKKALTQW FLKITDYADE LLEKLDGLDW PEKTKAMQKH WIGKSKGVEA TFKVENSDIT
     FDVFTTRVDT LNGVTYVVLA PENELVDSLT TEENKAAVEA YKIEAQKQSD IERQSSTREK
     TGVFTGSYAI NPINGNKVPI WVGDYVLATY GTGCVMAVPA HDERDYAFAT KYDLPIVRVI
     EGGDSLPFTE YGSLVNSGEF DGLYGEEAKE AIVKKLQEQK LGNWKVNYRL RDWLVSRQRY
     WGAPIPVVYC DKCGTVAVPE EQLPVELPYN IEFTPDGKSP LSKSEEFLHT TCPKCGGHAV
     RETDTLDTFV CSSWYYLRYV DNNNSEKAFD IDKVNKMLPV DKYVGGPEHA CMHLLYARFI
     TKALRDMGYL NFDEPFTSLT HQGLILGPDG LKMSKSKGNT IAPDDYIKEY GADVFRMYLM
     FGFAYSEGGA WSDDAIKSMS KFVDKVERIL ADSRTQMADS KNTKTTIEKA EKELNYTRHY
     AIQHVTEDTE KFQFNTAIAR IMEYTNSLSK YLNEENLNVE FLKEALTDYI KLLAPFAPHF
     SEEQWELLGN TSSVFTTSWP KFDPKALVKD EVEIAIQILG KIKARMNIAT NLTDEEIKEA
     ALNNETIKGL LEGKNIIKVI VVKGSLVNIV AK