ID   SYL_BURP0               Reviewed;         864 AA.
AC   A3NZB6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 94.
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=BURPS1106A_3450;
OS   Burkholderia pseudomallei (strain 1106a).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=357348;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1106a;
RX   PubMed=20333227; DOI=10.1093/gbe/evq003;
RA   Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA   Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA   Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA   Nierman W.C.;
RT   "Continuing evolution of Burkholderia mallei through genome reduction and
RT   large-scale rearrangements.";
RL   Genome Biol. Evol. 2:102-116(2010).
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; CP000572; ABN89129.1; -; Genomic_DNA.
DR   RefSeq; WP_004535294.1; NC_009076.1.
DR   AlphaFoldDB; A3NZB6; -.
DR   SMR; A3NZB6; -.
DR   GeneID; 56528259; -.
DR   KEGG; bpl:BURPS1106A_3450; -.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   Proteomes; UP000006738; Chromosome I.
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.
FT   CHAIN           1..864
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009310"
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;  96151 MW;  C389C7051142A655 CRC64;
     MHERYVPADV EAAAQSDWRA ADAYRSKEDA NRKKFYCVSM LPYPSGKLHM GHVRNYTIND
     VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAQW TYENIAYMKK QMQSMGLAID
     WSREVTTCKP DYYKWNQWLF LKMLEKGVAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEKREIPM YYMRITQYAD ELLNDLDGLG WPERVKVMQH NWIGKSFGVN FGFPYELDGE
     KKLLRVFTTR ADTIMGVTFC AIAAEHPLAA RLARDKPALQ AFIDECKRGG VAEADIATME
     KKGVATGFSV SHPLTGEPVE VWIGNYVLMS YGEGAVMGVP AHDERDFAFA KKYGLPIRQV
     IAVEGETYST DAWQEWYGDK TRAVCVNSGK YDGLAHDAAV DAIAAELKAG GLGDKQITYR
     LRDWGISRQR YWGTPIPIIH CPSCGDVPVP EQDLPVVLPE DLVPDGTGNP LAKSDAFLNC
     TCPKCGAAAK RETDTMDTFV DSAWYFSRYA APDAQTMVDA RTDYWMPMDQ YIGGIEHAIL
     HLLYSRFWAK VMRDLGLVAF GEPAKNLLTQ GMVLNETFYR EDAAGKKTWY NPADVTVSFD
     DKGRPVGAVL KSDGQPVELG GIEKMSKSKN NGVDPQMLID HYGADTARLF TMFAAPPEQQ
     LEWSGAGVDG ASRFLRRVWA FGFANREALA VRAPFDAAQL AEADKTLRRE IHGVLKQADF
     DYQRLQYNTV VSAAMKMLNA IEGAKGATPA VLRETYGVLL RVLYPVVPHV TFELWKALGY
     ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ VNGKVRGALK VAKDASREAI EAAAVADGMF
     AKFAEGRPAK KIIVVPGRLV NVVV
//