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 27-MAR-2024, entry version 96.
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; Pseudomonadota; 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 GeneID; 69539819; -.
DR KEGG; eic:NT01EI_2936; -.
DR PATRIC; fig|634503.3.peg.2623; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OrthoDB; 9810365at2; -.
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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..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
//
