ID   SYL_DESHY               Reviewed;         827 AA.
AC   Q24SP5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-APR-2006, sequence version 1.
DT   27-MAR-2024, entry version 111.
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=DSY3158;
OS   Desulfitobacterium hafniense (strain Y51).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC   Desulfitobacterium.
OX   NCBI_TaxID=138119;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y51;
RX   PubMed=16513756; DOI=10.1128/jb.188.6.2262-2274.2006;
RA   Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA   Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT   "Complete genome sequence of the dehalorespiring bacterium
RT   Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT   ethenogenes 195.";
RL   J. Bacteriol. 188:2262-2274(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP008230; BAE84947.1; -; Genomic_DNA.
DR   RefSeq; WP_011460890.1; NC_007907.1.
DR   AlphaFoldDB; Q24SP5; -.
DR   SMR; Q24SP5; -.
DR   STRING; 138119.DSY3158; -.
DR   KEGG; dsy:DSY3158; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   Proteomes; UP000001946; 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; Reference proteome.
FT   CHAIN           1..827
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334749"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           583..587
FT                   /note="'KMSKS' region"
FT   BINDING         586
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   827 AA;  94532 MW;  9ABC3B33C891064E CRC64;
     MQEKYLFSEI EPKWQKKWVD RKDYQAEEHS DKPKFYALAM FPYPSGNLHM GHVRNYSIVD
     VIARFKRMRG YNVLHPIGWD SFGLPAENAA IKNQTPPAEW TWKNIANMKR QLQEMGISYD
     WEREVTTCHP DYYKFTQWIF LEFYKHGLVY KKKAGVNWCP SCATVLANEQ VVDGACERCD
     TAVTKKDLEQ WFFKITDYAQ VLLDDLEKLP GWPDKVKTMQ KNWIGRSEGA EVEFDLENHG
     DKIRVYTTRV DTIFGVSYVV LAPEHPLVQK LIAGTEYEND VQAFIERMKG LNEIARTSTE
     TEKEGLFTGA YCINPYSGEK VPIWIANYVL FEYGTGAVMG VPAHDERDFE FAGKYKLPIK
     TVILPEGTPV EEKDTPLQAA FVEEGMMVNS GEYDGLKNVE AWEKMCDKAE HDGFGERKVN
     FRLRDWLISR QRYWGAPIPM IYCDHCGIVP VPQDQLPVML PDDVVFKAGE NPLTTSESFK
     QTICPTCGGK ARRETDTMDT FMCSSWYFLR YTDPHNAQLP FAKEAADHWM NVDQYVGGVE
     HAILHLLYSR FFTKALRDFG YLKVDEPFAN LLTQGMVCLG GAKMSKSKGN VVSPEEIISK
     YGADTARLFI LFAAPPERDL EWNDQGVEGC YRFLNRVWRL AAQYEEVLKT TGAGANEFGE
     LDKAAKDMRR QTHQTIQRVT SDVGARFNFN TAVSAIMELV NALYLYKEQP QVNLAVAREA
     LESILILLAP FAPHITEEIW SELGHEDSIH SREWPQVDEE ALVQEEVTVV LQINGKVKER
     IQVPAQISAA ELEAQVRQLP RLGEWTQGKQ ILKIVTVPGK LVNVVVK
//