ID   SYL_PARC0               Reviewed;         897 AA.
AC   A1TVU7;
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=Aave_4548;
OS   Paracidovorax citrulli (strain AAC00-1) (Acidovorax citrulli).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Paracidovorax.
OX   NCBI_TaxID=397945;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AAC00-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., 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 Acidovorax avenae subsp. citrulli AAC00-1.";
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; CP000512; ABM35085.1; -; Genomic_DNA.
DR   RefSeq; WP_011797553.1; NC_008752.1.
DR   AlphaFoldDB; A1TVU7; -.
DR   SMR; A1TVU7; -.
DR   STRING; 397945.Aave_4548; -.
DR   KEGG; aav:Aave_4548; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000002596; 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; 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; 1.
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..897
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009284"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           645..649
FT                   /note="'KMSKS' region"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   897 AA;  99830 MW;  9B4C0A3011D76274 CRC64;
     MQDKYTPAEV ERAAHSHWTA RDAYRVTEDA GKKKFYACSM LPYPSGKLHM GHVRNYTIND
     MLTRYLRMNG HNVLMPMGWD AFGLPAENAA LKNGVPPAQW TYDNIAYMKK QMQAMGLAID
     WSREVATCDP DYYKWNQWLF LKMLEKGIAY RKTQVVNWDP VDQTVLANEQ VIDGRGWRTG
     ALVEKREIPG YYLKITDYAQ ELLDHVQVGN PNATLTGWPD KVRLMQENWI GKSEGVRFAF
     THDIRGEDGQ PIGDGRMYVF TTRADTIMGV TFCAVAPEHP LAAHAARSNP DVAAFIQECK
     TGGTTEAELA TQEKKGVRTG LTVTHPLTDE PIEVWVGNYV LMGYGDGAVM GVPAHDERDF
     AFALKYGIEI KQVVLVDGET FDYHRWQDWY GDKQNGVTIN SDNFSGLSYQ EAVSAVAHAL
     QEKGLGEKKT TWRLRDWGVS RQRYWGTPIP IIHCDEHGAV PVPEKDLPVV LPQDCIPDGS
     GNPLHKHEGF HAGVKCPVCG KAARRETDTM DTFVDSSWYF MRYCDPKNAD AMVAGGADYW
     MPMDQYIGGI EHAILHLLYA RFWTKVMRDL GLVKVDEPFT KLLTQGMVLN HIYSRRTDKG
     GKEYFWPHDV EHIQDEAGKI TGARLKNAVG DLPAGTPIDY EGVGTMSKSK NNGVDPQELI
     EKYGADTARL YTMFTAPPEA TLEWNDAAVE GSYRFLRRVW NFGVKLAGID AAATEAAIQG
     AQSLQDVQFG KEAKALRLEI HTVLKQVDYD YQRMQYNTVV SGAMKMLNAL EDFKSADAPG
     GLVALIEGFG ILLRVLYPAT PHIAHGLWSG LGYAGSLGDL LDAPWPQVDA GALMQDEIEL
     VLQINGKLRG AIRVPSGADK AEIERIALAS EDFHKHAAGA APKKVVVVPG RLVNVVV
//