ID   SYL_ALIF1               Reviewed;         858 AA.
AC   Q5E6U8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAR-2024, entry version 134.
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};
GN   OrderedLocusNames=VF_0753;
OS   Aliivibrio fischeri (strain ATCC 700601 / ES114) (Vibrio fischeri).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=312309;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700601 / ES114;
RX   PubMed=15703294; DOI=10.1073/pnas.0409900102;
RA   Ruby E.G., Urbanowski M., Campbell J., Dunn A., Faini M., Gunsalus R.,
RA   Lostroh P., Lupp C., McCann J., Millikan D., Schaefer A., Stabb E.,
RA   Stevens A., Visick K., Whistler C., Greenberg E.P.;
RT   "Complete genome sequence of Vibrio fischeri: a symbiotic bacterium with
RT   pathogenic congeners.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:3004-3009(2005).
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; CP000020; AAW85248.1; -; Genomic_DNA.
DR   RefSeq; WP_011261460.1; NC_006840.2.
DR   RefSeq; YP_204136.1; NC_006840.2.
DR   AlphaFoldDB; Q5E6U8; -.
DR   SMR; Q5E6U8; -.
DR   STRING; 312309.VF_0753; -.
DR   EnsemblBacteria; AAW85248; AAW85248; VF_0753.
DR   KEGG; vfi:VF_0753; -.
DR   PATRIC; fig|312309.11.peg.746; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000537; 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   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   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; Reference proteome.
FT   CHAIN           1..858
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009462"
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;  97019 MW;  289398A66A4F8101 CRC64;
     MQEQYNPQDL EQKIQKHWDD NKTFVVTEDA NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VVSRYQRLQG KNVMQPIGWD AFGLPAENAA VKNKTAPAPW TYENIEYMKN QLKLLGFGYD
     WNREFATCTP EYYRWEQEFF TKLYNKGLVY KKTSSVNWCP NDQTVLANEQ VEDGCCWRCD
     TPVEQKKIPQ WFIKITEYAQ ELLDDLDNLD GWPEMVKTMQ RNWIGRSEGV ELSFAVNGET
     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 TIERDGKGRI
     EKAIDDQGRE 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
//