ID   SYL_PSEF5               Reviewed;         868 AA.
AC   Q4K5H6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 131.
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=PFL_5439;
OS   Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=220664;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5;
RX   PubMed=15980861; DOI=10.1038/nbt1110;
RA   Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A.,
RA   Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J.,
RA   Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J.,
RA   Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C.,
RA   Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III,
RA   Thomashow L.S., Loper J.E.;
RT   "Complete genome sequence of the plant commensal Pseudomonas fluorescens
RT   Pf-5.";
RL   Nat. Biotechnol. 23:873-878(2005).
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; CP000076; AAY94649.1; -; Genomic_DNA.
DR   RefSeq; WP_011063657.1; NC_004129.6.
DR   AlphaFoldDB; Q4K5H6; -.
DR   SMR; Q4K5H6; -.
DR   STRING; 220664.PFL_5439; -.
DR   KEGG; pfl:PFL_5439; -.
DR   PATRIC; fig|220664.5.peg.5552; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   Proteomes; UP000008540; Chromosome.
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..868
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091347"
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;  96954 MW;  09C01DF96F163EAD CRC64;
     MHEHYQPREI EAAAQLFWDE QKSFEVSEQP GKETYYCLSM FPYPSGKLHM GHVRNYTIGD
     VISRYQRMQG KNVLQPMGWD AFGMPAENAA MKNNVAPAKW TYENIAYMKT QLRSLGLAVD
     WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP IDQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFKITAYAD ELLESLDELP GWPEQVKTMQ RNWIGKSRGM EVQFPYDQAS
     IGEAGTLKVF TTRPDTLMGA TYVAVAAEHP LATLAAQDNP ELQAFIAECK GGSVAEADMA
     TQEKKGLPTS LFVEHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFATKYNLPI
     KAVVRTSAGD ETPAPWQDAY GEHGELINSG EFNGLDFPGA FDAIEVALLK KNLGQSRTQF
     RLRDWGISRQ RYWGCPIPII HCDSCGDVPV PQEQLPVVLP EDVVPDGAGS PLARMPEFYE
     CSCPKCGAPA KRETDTMDTF VESSWYYARY ASPHYEGGLV DPAAANHWLP VDQYIGGIEH
     AILHLLYARF FHKLMRDEGL VSSNEPFKNL LTQGMVIAET YYRREANGSY TWYNPADVEL
     ERDSKAKIIG AKLISDGLPV EIGGTEKMAK SKNNGVDPQS MIEQYGADTC RLFMMFASPP
     DMSLEWSDSG VEGAHRFLKR VWRLAQAHVS QGLPGALDIA TLSDEQKAIR RAIHLAIKQA
     SQDVGQHHKF NTAIAQVMTL MNVLEKAPQG SEQDRALLQE GLQTVALLLA PITPHISHEL
     WGQLGQSGAI IDAGWPALDE SALVQDSLQL VIQVNGKLRG QIEMPASASR EEVEAAARSN
     ENVLRFTEGL TIRKVIVVPG KLVNIVAS
//