ID   SYL_DEHM1               Reviewed;         813 AA.
AC   Q3ZA07;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   27-MAR-2024, entry version 124.
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=DET0194;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2266 / KCTC 15142 / 195)
OS   (Dehalococcoides ethenogenes (strain 195)).
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=243164;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2266 / KCTC 15142 / 195;
RX   PubMed=15637277; DOI=10.1126/science.1102226;
RA   Seshadri R., Adrian L., Fouts D.E., Eisen J.A., Phillippy A.M., Methe B.A.,
RA   Ward N.L., Nelson W.C., DeBoy R.T., Khouri H.M., Kolonay J.F., Dodson R.J.,
RA   Daugherty S.C., Brinkac L.M., Sullivan S.A., Madupu R., Nelson K.E.,
RA   Kang K.H., Impraim M., Tran K., Robinson J.M., Forberger H.A., Fraser C.M.,
RA   Zinder S.H., Heidelberg J.F.;
RT   "Genome sequence of the PCE-dechlorinating bacterium Dehalococcoides
RT   ethenogenes.";
RL   Science 307:105-108(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; CP000027; AAW40547.1; -; Genomic_DNA.
DR   RefSeq; WP_010935997.1; NC_002936.3.
DR   AlphaFoldDB; Q3ZA07; -.
DR   SMR; Q3ZA07; -.
DR   STRING; 243164.DET0194; -.
DR   KEGG; det:DET0194; -.
DR   PATRIC; fig|243164.10.peg.179; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_0; -.
DR   InParanoid; Q3ZA07; -.
DR   Proteomes; UP000008289; 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; 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   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_1000199192"
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;  92868 MW;  493634ACB295ADB9 CRC64;
     MAEKYNPQET EKKWQDKWAA DRLYHAGEDS PKPKWYSLTM FPYTSGNLHI GHWYAEVPAD
     CFARYKRLNG FNVMRPVGFD SFGLPAENAA IKHHIHPRIW TLNNVENMRR QLKTIGAMFD
     WDREVITCLP EYYKWTQWFF LKLYEAGLAY RAKAPVNWCP SCQAVLANEQ VVDGTCWRCE
     TPTTRRDLEQ WFFRITNYAD ELKDHDGLDW PEKITAMQRN WVGKSYGAEV SFALDCPAAP
     EQEIKVFTTR PDTIYGVTFM VLAPEHPLVE KITTPENKAA VDEYIKKSRA CTEIERLSTE
     REKDGVFTGA YVTNRVNGHK VPVWIGDYVL QSYGTGAVMG VPAHDERDFV FAQKYDLPVI
     TVIAPPDYDG QPLEAAYINE GVMQNSGPFN GLPNTEGKEK VCDYLAEHGW GKKTVNYKLR
     DWLISRQRYW GAPIPMIYCE KCGIVPVPEK DLPVLLPEDV EFRSGGESPL KYNEGFVNTT
     CPVCGGKAKR ETDTMDTFMC SSWYFLRYTS PGYDKGPFDP EKLRYWMPVD LYTGGAEHAV
     MHLFYSRFFT KALRDMGIID FGEPFKKLFN QGIIVSNHQK MSKSKGNVVT PDNLVAEVGT
     DAVRAYLMFV GPWDQGGEWN DSGLSGMSRW LNRVWNLFTE EYTPQTASAE AERELKRTLH
     QTIKKITMDI ERLRFNTVVA ALMELSNSLA KFKEAAAVSA ESWQNSLKTF ALMLAPVAPH
     IAEELWANLD MEYSIHNQSW PKWDEELAKD EVITLIIQVN GKLRERLEMP AGISEDEAKE
     TALNSTRVKP HLQGKTPASV IYVPGKLVNI VVK
//