ID   SYL_DEHMC               Reviewed;         813 AA.
AC   Q3ZWQ1;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 131.
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=cbdbA202;
OS   Dehalococcoides mccartyi (strain CBDB1).
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=255470;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBDB1;
RX   PubMed=16116419; DOI=10.1038/nbt1131;
RA   Kube M., Beck A., Zinder S.H., Kuhl H., Reinhardt R., Adrian L.;
RT   "Genome sequence of the chlorinated compound-respiring bacterium
RT   Dehalococcoides species strain CBDB1.";
RL   Nat. Biotechnol. 23:1269-1273(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; AJ965256; CAI82449.1; -; Genomic_DNA.
DR   RefSeq; WP_011308807.1; NC_007356.1.
DR   AlphaFoldDB; Q3ZWQ1; -.
DR   SMR; Q3ZWQ1; -.
DR   KEGG; deh:cbdbA202; -.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   Proteomes; UP000000433; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..813
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199194"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           580..584
FT                   /note="'KMSKS' region"
FT   BINDING         583
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   813 AA;  92974 MW;  C4AB5C597421734B CRC64;
     MAEKYNPQET EKKWQDKWAA DRLYHASEDS PKPKWYSLTM FPYTSGNLHI GHWYAEVPAD
     CFARYKRLRG FNVMRPVGFD SFGLPAENAA IKHNIHPRIW TLNNVENMRR QLKTIGAMFD
     WDREVITCLP EYYKWTQWFF LKLYEAGLAY RAKAPVNWCP SCQAVLANEQ VVDGTCWRCE
     TPTTRRDLEQ WFFRITNYAD ELKDHEGLDW PEKITAMQRN WVGKSYGAEV SFALDCPTAF
     EKEIKVFTTR PDTIYGVTFM VLAPEHPLVE KITTPENKAA VDAYIKKSRT CTEIERLSTE
     REKDGVFTGT YVTNRVNGQK VPVWIGDYVL QSYGTGAVMG VPAHDERDFV FAQKYHLPVI
     TVIAPSEYDG KPLEVAYINE GVMLNSGPFN GTPNTEGKEK VCDYLAEHGW GKKTVNYKLR
     DWLISRQRYW GAPIPMVYCE KCGIVPVPEK DLPVLLPEDV EFRSGGESPL KYNEGFVNTI
     CPVCGGKAKR ETDTMDTFMC SSWYFLRYTS PGYDKGPFDP VKLKYWMPVD LYTGGAEHAV
     MHLFYSRFFT KALRDMGIID FGEPFKKLFN QGIIVSNHQK MSKSKGNVVT PDNLVAEVGT
     DAVRAYLMFV GPWDQGGEWN DSGLSGMSRW LNRVWNLFTE EYTPQTASAE AERELKRTLH
     QTIKKITMDI ERLRFNTVVA ALMELSNSLA KLKETAAISA ENWQNTLQTF ALMLAPVAPH
     IAEELWANLG MKYSIHNQNW PTWDEELAKD EVITLIIQVN GKLRERLEMP AGISEAEAKE
     TALNSERVKP HLLGKTPVTV IYVPGKLVNI VVK
//