ID   SYL_ALIFM               Reviewed;         858 AA.
AC   B5FBK7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   03-AUG-2022, entry version 81.
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=VFMJ11_0772;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) 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; CP001139; ACH65672.1; -; Genomic_DNA.
DR   RefSeq; WP_012533208.1; NC_011184.1.
DR   AlphaFoldDB; B5FBK7; -.
DR   SMR; B5FBK7; -.
DR   PRIDE; B5FBK7; -.
DR   EnsemblBacteria; ACH65672; ACH65672; VFMJ11_0772.
DR   KEGG; vfm:VFMJ11_0772; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001857; Chromosome I.
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; -; 1.
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.
FT   CHAIN           1..858
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091377"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           618..622
FT                   /note="'KMSKS' region"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   858 AA;  97020 MW;  31E925A69B10ED41 CRC64;
     MQEQYNPQDL EQKIQKHWDD NKTFVVTEDA NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRYQRLQG KNVMQPIGWD AFGLPAENAA VKNKTAPAPW TYENIEYMKN QLKLLGFGYD
     WNREFATCTP EYYRWEQEFF TKLYSKGLVY KKTSSVNWCP NDQTVLANEQ VEDGCCWRCD
     TPVEQKKIPQ WFIKITEYAQ ELLDDLDNLD GWPEMVKTMQ RNWIGRSEGV ELSFAVNGEE
     SPLEVYTTRP DTLMGVTYVG IAAGHPLAEK ASQNNPELAA FVEECRNTKV AEAELATMEK
     KGMDTGLRAI HPLNGREVPV FVANFVLMDY GTGAVMAVPA HDQRDFEFAT KYGLDIIPVI
     KPEDGSDLDV SEAAYTEKGV LFDSGEFDGL AFQEAFDAIA AKLEAEGKGK KTVNFRLRDW
     GVSRQRYWGA PIPMVTTEDG EVHPVPADQL PVILPEDVVM DGVTSPIKAD KEWAKTTFNG
     EPALRETDTF DTFMESSWYY ARYCSPQADD ILDPEKANYW LPVDQYIGGI EHACMHLLYS
     RFFHKLLRDA GYVTSDEPFK QLLCQGMVLA DAFYYTNDKG GKEWVAPTDV TIERDAKGRI
     EKAVDDQGRE VEHSGMIKMS KSKNNGIDPQ EMVDKYGADT VRLFMMFASP ADMTLEWQES
     GVEGANRFLK RVWKLVHEHT NKGTTEALDT SSLTGDQKAL RRDVHKTIAK VSDDIGRRQT
     FNTAIAAIME LMNKLNKAPQ ESAQDRALLD EALKAVVAML YPMTPHASFA MWEALGESDL
     DSATWPTFDE NALVEDEKTI VVMINGKLRA KLVVAADATE EHVRELGLKD ENAMKFLDGL
     TIRKVIYVPG KLLNIVAN