ID   SYL_PARXL               Reviewed;         863 AA.
AC   Q13U82;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   27-MAR-2024, entry version 111.
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=Bxeno_A3819; ORFNames=Bxe_A0576;
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400;
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA   Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA   Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA   Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT   shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
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; CP000270; ABE32357.1; -; Genomic_DNA.
DR   RefSeq; WP_011489837.1; NZ_CP008760.1.
DR   AlphaFoldDB; Q13U82; -.
DR   SMR; Q13U82; -.
DR   STRING; 266265.Bxe_A0576; -.
DR   KEGG; bxb:DR64_2749; -.
DR   KEGG; bxe:Bxe_A0576; -.
DR   PATRIC; fig|266265.5.peg.4035; -.
DR   eggNOG; COG0495; Bacteria.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001817; 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.
FT   CHAIN           1..863
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009314"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           623..627
FT                   /note="'KMSKS' region"
FT   BINDING         626
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   863 AA;  96985 MW;  C4CA8F1BAC7F1069 CRC64;
     MHEKYVPSDV ESAAQGQWRA IDAYKTTEVT DKPKFYCVSM LPYPSGKLHM GHVRNYTIND
     VMYRYLRMNG YNVLMPMGWD AFGMPAENAA MANNVPPAKW TYDNIAYMKK QMQSMGLAID
     WSREVATCSP DYYKWNQWLF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEKREIPM YYMRITQYAD ELLNDLEGLG WPERVKIMQQ NWIGKSFGVN FGFPYEIDGE
     QKLLRVFTTR ADTIMGVTFC AIAAEHPLAT RLAKDKPELQ AFIEECKRGG VAEADVATME
     KKGMATGFTV THPLTQEQVE VWIGNYVLMS YGEGAVMGVP AHDERDFAFV KKYGLPVRQV
     VAVEGKEFST EAWQEWYGEK TGTLINSGKY DGLNYEQAVD RIAADLKELG LGDKQITWRL
     RDWGVSRQRY WGTPIPIIHC PTCGDVPVPE KDLPVVLPED LVPDGTGNPL ARSEAFVNCT
     CPTCGGAAKR ETDTMDTFVD SSWYFYRYAS PGAKTMVDER TDYWAPMDQY IGGIEHAILH
     LLYSRFWAKV MRDLGLIRFG EPAKNLLTQG MVLNETYYRE NEAGKKTWYN PAEVTVSFDD
     KGRPVGAILN EDGQPVVLGG VEKMSKSKNN GVDPQLLIDQ HGADTARLFV MFAAPPEQSL
     EWSGSGVEGA SRFLRRVWSF SQANEAALRQ GGTFDAAQLS DVEKVLRREI YSVLKQADFD
     YQRLQYNTVV SAAMKMLNAL DSAKGARPAV LRETCSVMLR VLYPVVPHLT FQLWQELGYA
     DELGSLLDAP WPKVDEKALE QSEIELVLQV NGKVRGAITV AKDASREAIE QLAAAHEMVA
     KFSEGKAPKK IVVVPGRLVN VVV
//