ID   SYL_ACISJ               Reviewed;         910 AA.
AC   A1WCP8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 106.
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=Ajs_3917;
OS   Acidovorax sp. (strain JS42).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=232721;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS42;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T.,
RA   Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.;
RT   "Complete sequence of chromosome 1 of Acidovorax sp. JS42.";
RL   Submitted (DEC-2006) 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; CP000539; ABM44023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A1WCP8; -.
DR   SMR; A1WCP8; -.
DR   STRING; 232721.Ajs_3917; -.
DR   KEGG; ajs:Ajs_3917; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   Proteomes; UP000000645; 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   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   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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..910
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009285"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           658..662
FT                   /note="'KMSKS' region"
FT   BINDING         661
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   910 AA;  101205 MW;  C0549663194C215C CRC64;
     MQDKYNHTEV ERAAHAHWNA NDAYRVTEDQ AKPKFYACSM LPYPSGKLHM GHVRNYTIND
     MLTRSLRMKG HNVLMPMGWD AFGLPAENAA LKNGVPPAQW TYDNIAYMKK QMQAMGLAID
     WSREIATCDP DYYKWNQWLF LKMLDKGIAY RKTQVVNWDP VDQTVLANEQ VIDGRGWRTG
     ALVEKREIPG YYLKITDYAQ ELLDHVQIGN EKATLTGWPD KVRLMQENWI GKSAGVRFAF
     PHDIRNAAGE RIQDGKLYVF TTRADTIMGV TFCAVAPEHP LAQHAAASNA ALAAFIEECK
     KGGTTEAELA LKEKEGMPTG LFVTHPLTGE QVEVWVGNYV LMSYGDGAVM GVPAHDERDF
     AFALKYQLPI KQVVLVDGET FDFHQWQDWY GDKERGVTIN SGNFSGLSYQ DAVAAVAHAL
     AEKGLGELKT TWRLRDWGIS RQRYWGTPIP IIHCESCGAV PVPEKDLPVV LPQDLVPDGS
     GNPLAKCEAF LKVDCPCCGK PARRETDTMD TFVDSSWYFM RYCDPKNRDA MVAGGTDYWM
     RDQKAATGGS GMDQYIGGIE HAILHLLYAR FWTKVMRDLG LVKVDEPFTK LLTQGMVLNH
     IYSRRTAKGA KDYFWPHDVE HVYDEAGKIV GAKLKNPAES GDGLLPVGTP IDYEGVGTMS
     KSKNNGVDPQ QLIEKYGADT ARLYTMFTAP PELTLEWNDA AVEGSYRFLR RVWNFGVKLS
     AIDKDAALAS VAGAASLKDV QFGKEAKALR LEIHTVLKQV DYDYQRMQYN TVVSGAMKMI
     NALEDFKATD SAGAQVALIE GFGILLRVLY PATPHIAHVL WDELGYAGTL GDLLDAAWPQ
     VAPDALVQDE LELMLQVNGK LRGAIRVAAS ADKAAIEQAA LASEDFHKFA EGKAPKKVII
     VPGRLVNVVV
//