ID   SYL_BURM1               Reviewed;         864 AA.
AC   A9AHA9;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 101.
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=Bmul_2732, BMULJ_00505;
OS   Burkholderia multivorans (strain ATCC 17616 / 249).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX   NCBI_TaxID=395019;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Tiedje J.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Burkholderia multivorans ATCC
RT   17616.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17616 / 249;
RA   Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA   Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA   Hattori M., Tsuda M.;
RT   "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL   Submitted (APR-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; CP000868; ABX16416.1; -; Genomic_DNA.
DR   EMBL; AP009385; BAG42472.1; -; Genomic_DNA.
DR   RefSeq; WP_012214125.1; NC_010804.1.
DR   AlphaFoldDB; A9AHA9; -.
DR   SMR; A9AHA9; -.
DR   STRING; 395019.BMULJ_00505; -.
DR   KEGG; bmj:BMULJ_00505; -.
DR   KEGG; bmu:Bmul_2732; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   Proteomes; UP000008815; Chromosome 1.
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; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; 2.
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..864
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091299"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   864 AA;  95873 MW;  22F866E5CCBD9029 CRC64;
     MHERYVPADV EAAAQGDWRA ADAYKTQEDA QKPKFYCVSM LPYPSGKLHM GHVRNYTIND
     VMYRYLRMNG YNVLMPMGWD AFGMPAENAA MANGVPPAKW TYDNIDYMKG QMQSMGLAID
     WSREIATCKP DYYKWNQWLF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEKREIPM YYLRITQYAD ELLNDLDGLG WPERVKIMQQ NWIGKSFGVN FGFPYELDGE
     KQLLRVFTTR ADTIMGVTFC AIAAEHPLAT RLAQGKPELQ AFIDECKRGG VAEADMATME
     KKGVATGFSV THPLTGEPVE VWIGNYVLMS YGEGAVMGVP GHDERDFAFA KKYGLPIKQV
     IAAEGHTYSL DAWQEWYGDK DIAVCINSGK YDGLGYAAAV DAVAADLKAG GFGDKQVTWR
     LRDWGISRQR YWGTPIPIIH CPSCGDVPVP EKDLPVVLPE DLVPDGSGNP LAKSEAFLNC
     TCPKCGAAAK RETDTMDTFV DSSWYFSRYT APDAETMVDA RTDYWMPMDQ YIGGIEHAIL
     HLLYSRFWTK VMRDLGLVKF GEPAKNLLTQ GMVLNETYYR EDAAGKKTWY NPADVTVTHD
     DKGRPVGATL NADGQPVVLG GIEKMSKSKN NGVDPQVLID QYGADTARLF TMFAAPPEQQ
     LEWSGAGVEG ASRFLRRVWS FGYANREALA SRAGFDAAAL GDADKALRRE IYSVLKQADF
     DYQRLQYNTV VSAAMKMLNA IDGAKGATPG VLREAYGVLL RVLYPVVPHV TYELWKALGY
     ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ VNGKVRGALK VAKDASREAI EAAALADDAF
     AKFGEGKPAK KIVVVPGRLV NIVV
//