ID   SYL_EDWI9               Reviewed;         860 AA.
AC   C5BGC7;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   03-AUG-2022, entry version 89.
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=NT01EI_2936;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
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; CP001600; ACR70090.1; -; Genomic_DNA.
DR   RefSeq; WP_015872184.1; NC_012779.2.
DR   AlphaFoldDB; C5BGC7; -.
DR   SMR; C5BGC7; -.
DR   STRING; 67780.B6E78_06585; -.
DR   EnsemblBacteria; ACR70090; ACR70090; NT01EI_2936.
DR   GeneID; 7960214; -.
DR   KEGG; eic:NT01EI_2936; -.
DR   PATRIC; fig|634503.3.peg.2623; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001485; 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; 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; 3.
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.
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..860
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000202219"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   860 AA;  97160 MW;  913E815D3AC84093 CRC64;
     MQEQYRPEDI ESHVQRHWDE QKTFQVTEDA GKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
     VISRYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYANIDYMKN QLKLLGFGYD
     WSREIATCKP DYYRWEQWFF TKLYEKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
     SKVERKEIPQ WFIKITDYAD QLLNDLDRLE EWPEQVKTMQ RNWIGRSEGV EITFHVADRD
     DTFAVYTTRP DTFMGVSYLA IAAAHPLAQQ AATGNPALTQ FIDECKNTKV AEADMATMEK
     KGMATGLYAI HPLNGERLPI WVANFVLMDY GTGAVMSVPA HDQRDWEFAT RYDLPMKPVI
     LTADGQAPDI RAAAMTDKGV LFNSGEFDGL DFSAAFDAVA NRLIAAGVGE RKVNYRLRDW
     GVSRQRYWGA PIPMMTLEDG SVIPTPEEQL PVILPEDVVM NGITSPIKAD PSWAKTTVNG
     QPALRETDTF DTFMESSWYY ARYTCPQFDQ GMLDPQAANY WLPVDQYVGG IEHAIMHLMY
     FRFFHKLMRD AGLVDSDEPA KRLLCQGMVL ADAFYYTGTN GERNWVSPVD VTVERDDKGR
     ITQATDRDGR ELVYAGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PAEMTLEWQE
     SGVEGANRFL KRVWKLAFDH QQKGLASALD LTALNDDQKA LRRDLHKTIA KVSDDIGRRQ
     TFNTAIAAVM ELMNKLTRAP QESEQDRALM QEALLAVVRM LYPFTPHVCF TLWRALGGAG
     DIDTAPWPVA DDAAMVEDSK LIVVQVNGKV RGKITVAADA SEEQVRALAA QEPLVAKYLD
     GVTVRKVIFV PGKLLNLVVG