ID   SYL_DEHMB               Reviewed;         813 AA.
AC   A5FP73;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=DehaBAV1_0159;
OS   Dehalococcoides mccartyi (strain ATCC BAA-2100 / JCM 16839 / KCTC 5957 /
OS   BAV1).
OC   Bacteria; Chloroflexota; Dehalococcoidia; Dehalococcoidales;
OC   Dehalococcoidaceae; Dehalococcoides.
OX   NCBI_TaxID=216389;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-2100 / JCM 16839 / KCTC 5957 / BAV1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Pitluck S., Lowry S., Clum A.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E.,
RA   Ritalahti K.M., Loeffler F., Richardson P.;
RT   "Complete sequence of Dehalococcoides sp. BAV1.";
RL   Submitted (MAY-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000688; ABQ16750.1; -; Genomic_DNA.
DR   AlphaFoldDB; A5FP73; -.
DR   SMR; A5FP73; -.
DR   KEGG; deb:DehaBAV1_0159; -.
DR   PATRIC; fig|216389.18.peg.179; -.
DR   HOGENOM; CLU_004427_0_0_0; -.
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_1000199193"
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;  92816 MW;  FC5F0958E48100CB 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
     TVIAPSAYDG KPLEAAYINE GVMLNSGPFN GTPNTEGKEK VCDYLAEHGW GKKTVNYKLR
     DWLISRQRYW GAPIPMVYCE KCGIVPVPEK DLPVLLPEDV GFRSGGESPL 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
//