ID   SYL_LIMF3               Reviewed;         805 AA.
AC   B2GDF8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   27-MAR-2024, 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};
GN   OrderedLocusNames=LAF_1354;
OS   Limosilactobacillus fermentum (strain NBRC 3956 / LMG 18251) (Lactobacillus
OS   fermentum).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Limosilactobacillus.
OX   NCBI_TaxID=334390;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 3956 / LMG 18251;
RX   PubMed=18487258; DOI=10.1093/dnares/dsn009;
RA   Morita H., Toh H., Fukuda S., Horikawa H., Oshima K., Suzuki T.,
RA   Murakami M., Hisamatsu S., Kato Y., Takizawa T., Fukuoka H., Yoshimura T.,
RA   Itoh K., O'Sullivan D.J., McKay L.L., Ohno H., Kikuchi J., Masaoka T.,
RA   Hattori M.;
RT   "Comparative genome analysis of Lactobacillus reuteri and Lactobacillus
RT   fermentum reveal a genomic island for reuterin and cobalamin production.";
RL   DNA Res. 15:151-161(2008).
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; AP008937; BAG27690.1; -; Genomic_DNA.
DR   RefSeq; WP_012391498.1; NC_010610.1.
DR   AlphaFoldDB; B2GDF8; -.
DR   SMR; B2GDF8; -.
DR   KEGG; lfe:LAF_1354; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   Proteomes; UP000001697; 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; 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; 1.
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..805
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091326"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           577..581
FT                   /note="'KMSKS' region"
FT   BINDING         580
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   805 AA;  92621 MW;  FF59FADFE65E77FA CRC64;
     MAYDHKAIEK KWQRYWKQHK TFKATLDKDQ KKYYALDMFP YPSGQGLHVG HPEGYTATDV
     MSRLKRMQGF NVLHPMGWDA FGLPAEQYAL KTGHNPADFT NQNVDHFRDQ IQSLGFSYDW
     DREVNTTDPN YYKWTQWIFE QLYKKGLAYE DEIMVNWAPD FMGGTVVANE EVVDGKTERG
     GYPVYRVPMR QWVLKITAYA DRLIDDLDLV DWPESVKEMQ RNWIGRSEGA SVKFKVVGHD
     GVEIEVFTTR ADTLFGASYV VLAPENELVD QLTTPEQKAA VDAYKEEVSR RSDLERTELS
     KEKTGVFTGA YVINPVNGEQ LPIWTADYVL NSYGTGAVMA VPSGDQRDFE FATKFNLPIT
     PVVEGFNGEE AYTEDGAHVN SGFLDGLNIK EAKAKMVEWL EEHDCGGKKV NYRLRDWIFS
     RQRYWGEPIP VIHWDDGTTS LVPEDELPLR LPETDNIEPS GTGESPLANI EDWVNVYDEN
     GRHGKRETNT MPQWAGSSWY WLRYTDPTND KEFASKEALD YWSPVDLYVG GAEHAVLHLL
     YARFWHKVLY DLGLVPTKEP FMKLVNQGMI LGSNHEKMSK SKGNVVNPDD IVDQYGADTL
     RLYEMFMGPL EESVPWDEKG LHGSNKWVQR VWRLLMDDNN HLRDRVSTYN DGKLTKVYNQ
     TVKKVTDDFE RMHFNTAISQ LMVFVNEAYK VDDLPLEYMK GFVKMIAPLM PHLAEELWSQ
     FNESETITYQ PWPTYDEKAL VEDEVEMIVQ VNGKVRAKIK MAKDADNKDV EDAALANEHV
     HSFVDGKDVK KVIVIPNRIV NIVVK
//