ID   SYL_PSEP1               Reviewed;         868 AA.
AC   A5W9H9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   03-AUG-2022, entry version 87.
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}; OrderedLocusNames=Pput_4669;
OS   Pseudomonas putida (strain ATCC 700007 / DSM 6899 / BCRC 17059 / F1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=351746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700007 / DSM 6899 / BCRC 17059 / F1;
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., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Parales R., Richardson P.;
RT   "Complete sequence of Pseudomonas putida F1.";
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ABQ80789.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000712; ABQ80789.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_004576918.1; NC_009512.1.
DR   AlphaFoldDB; A5W9H9; -.
DR   SMR; A5W9H9; -.
DR   STRING; 351746.Pput_4669; -.
DR   EnsemblBacteria; ABQ80789; ABQ80789; Pput_4669.
DR   KEGG; ppf:Pput_4669; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 32262at2; -.
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   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..868
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334795"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           627..631
FT                   /note="'KMSKS' region"
FT   BINDING         630
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   868 AA;  96698 MW;  E32FE998AEA4B688 CRC64;
     MHEQYTPRDI EAAAQKFWDE QQSFAVTEQP GKDTYYCLSM FPYPSGKLHM GHVRNYTIGD
     VIARYQRMLG KNVLQPMGWD AFGMPAENAA MKNNVAPAKW TYENIDYMKT QLKSLGLAID
     WAREVTTCKP DYYRWEQWLF TRLFEKGIIY RKNGTVNWDP ADQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFRITDYAD ELLESLDELP GWPEQVKTMQ RNWIGKSRGM EVQFPYDQAS
     IGHEGTLKVF TTRPDTLMGA TYVAVAAEHP LATQAAQGNP ALQAFIDECK SGSVAEADMA
     TQEKKGMATS LLVEHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFAHKYNLPV
     KAVVRTSAGD EVGSEWQAAY GEHGQLINSA EFDGLDFAGA FDAIEAALIR KELGKSRTQF
     RLRDWGISRQ RYWGCPIPII HCPSCGDVPV PEDQLPVTLP ENVVPDGAGS PLARMPEFYE
     CSCPKCGAAA KRETDTMDTF VESSWYFARY ASPNYDKGLV DPKAANHWLP VDQYIGGIEH
     AILHLLYARF FHKLMRDEGL VTSNEPFKNL LTQGMVVAET YYRVASNGGK DWFNPADVEI
     ERDAKAKIIG ARLKTDGLPV EIGGTEKMSK SKNNGVDPQS MIEAYGADTC RLFMMFASPP
     DMSLEWSDSG VEGASRFLRR VWRLAQAHVS QGLPGKLDVA ALDDAQKVIR RAIHAAIKQA
     STDVGQFHKF NTAIAQVMTV MNVLEKAPQA TEQDRALLQE GLEAVTLLLA PITPHISHAL
     WQHLGHAGSV IDAAWPSVDE QALVQDSITL VVQVNGKLRG QVEMPAAASR EEVEAAARSN
     ENVLRFIDGL TIRKVIVVPG KLVNIVAN