ID   SYL_AERS4               Reviewed;         858 AA.
AC   A4SJW8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=ASA_1068;
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449;
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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; CP000644; ABO89190.1; -; Genomic_DNA.
DR   RefSeq; WP_005317327.1; NC_009348.1.
DR   AlphaFoldDB; A4SJW8; -.
DR   SMR; A4SJW8; -.
DR   STRING; 382245.ASA_1068; -.
DR   EnsemblBacteria; ABO89190; ABO89190; ASA_1068.
DR   KEGG; asa:ASA_1068; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000225; 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   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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..858
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009287"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           618..622
FT                   /note="'KMSKS' region"
FT   BINDING         621
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   858 AA;  96439 MW;  4D1851864482DA11 CRC64;
     MQEQYVPQSI EPAVQKHWDA KKTFKAVEKV DKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
     VISRYQRLNG KNVLQPIGWD AFGLPAENAA VKNNTAPAPW TYENIEYMKN QLKMLGLGYD
     WDRELATCKP DYYRWEQWFF TKLYEKGLVY KKTSSVNWCP NDMTVLANEQ VVDNCCWRCD
     TPVEQKEIPQ WFIKITDYAE ELLNDIDNLE GWPEMVKTMQ RNWIGRSEGV NISFAIEGQA
     EQLEVYTTRP DTFMGVTYVG IAAGHPLALQ AAATNPGLAA FIEECKNTKV AEAELATMEK
     KGMATGLYAI HPLDGRKVPV WVANFVLMNY GTGAVMAVPG HDQRDHEFAT KYGLDIKAVI
     KPADGEVDVS DAAYTEKGVL FASGEFDGLD FQGAFDAIAN KLEALGHGKR TVNFRLRDWG
     VSRQRYWGAP IPMLTLADGT VVPTPEDQLP VLLPEDVVMD GIQSPIKADA EWAKTTYNGQ
     EAFRETDTFD TFMESSWYYA RYCSPDYDKG MLDPAAANHW LPVDQYIGGI EHACMHLLYA
     RFFHKLLRDA GLVNSDEPFK RLLCQGMVLA DAFYYKDEKG GNVWVSPTDV KVERDEKGRI
     TKAIDNDGRE VIHSGMTKMS KSKNNGIDPQ LMVERYGADT VRLFMMFASP AEMTLEWSDS
     GVEGAQRFLR RLWRLTFEHV SAGAVPALDV AALTSEQKAV RRELHKTIAK VSDDVGRRQT
     FNTAIAAIME LMNNLAKLGS DEQDRALMQE ALETVVVMLS PITPHIGFEL WKMLGKGDDV
     DHATWPVADE AAMVETEKLV VVQINGKMRG KLTVPAEISQ ADVEKLAMAD ASVQKFTDGL
     TVRKVIYVPG KLLNIVAN