ID   SYL_PSEPW               Reviewed;         868 AA.
AC   B1J150;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, 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=PputW619_0627;
OS   Pseudomonas putida (strain W619).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=390235;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W619;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA   Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Taghavi S., Vangronsveld D., van der Lelie D.,
RA   Richardson P.;
RT   "Complete sequence of Pseudomonas putida W619.";
RL   Submitted (FEB-2008) 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; CP000949; ACA71132.1; -; Genomic_DNA.
DR   AlphaFoldDB; B1J150; -.
DR   SMR; B1J150; -.
DR   STRING; 390235.PputW619_0627; -.
DR   KEGG; ppw:PputW619_0627; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OrthoDB; 9810365at2; -.
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   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..868
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091348"
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;  97014 MW;  47EC8D7BB190EB97 CRC64;
     MHEQYTPRDI EAAAQHFWDE 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
     TQEKKGMPTS LLVEHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFAHKYNLPV
     KAVVRTSAGD EVGSEWQAAY GEHGQLINSG 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 VWRLAQGHVN QGLPGKLDLA ALNDEQKVIR RAIHTAIKQA
     STDVGQYHKF NTAIAQVMTV MNVLEKAPQS TEQDRALLQE GLEAVTLLLA PITPHISHEL
     WKALGHEQAV IDACWPVVDE SALVQDTVTL VVQVNGKLRG QVEMPAAASR EEIEAAARNN
     ENVLRFIDGL TIRKVIVVPG KLVNIVAN
//