ID   SYL_DELAS               Reviewed;         911 AA.
AC   A9C1G8;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 96.
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=Daci_6003;
OS   Delftia acidovorans (strain DSM 14801 / SPH-1).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Delftia.
OX   NCBI_TaxID=398578;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 14801 / SPH-1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Lowry S., Clum A., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Schleheck D., Richardson P.;
RT   "Complete sequence of Delftia acidovorans DSM 14801 / SPH-1.";
RL   Submitted (NOV-2007) 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; CP000884; ABX38631.1; -; Genomic_DNA.
DR   RefSeq; WP_012207800.1; NC_010002.1.
DR   AlphaFoldDB; A9C1G8; -.
DR   SMR; A9C1G8; -.
DR   STRING; 398578.Daci_6003; -.
DR   GeneID; 24114088; -.
DR   KEGG; dac:Daci_6003; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   Proteomes; UP000000784; 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; 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; Reference proteome.
FT   CHAIN           1..911
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091312"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           659..663
FT                   /note="'KMSKS' region"
FT   BINDING         662
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   911 AA;  101345 MW;  BBEBCBD4F02DA4FD CRC64;
     MQEKYNHIDV ERAAQDHWSA RDAYRVTEDQ AKPKFYACSM LPYPSGKLHM GHVRNYTIND
     MLTRQLRMKG YNVLMPMGWD AFGLPAENAA LKNKVPPAQW TYDNIAYMKK QMQAMGLAID
     WSREIATCDP DYYKWNQWLF LKMLEKGIAY RKTQVVNWDP VDQTVLANEQ VIDGRGWRTG
     APVEKREIPG YYLKITDYAQ ELLDHVQVGG DKATLTGWPE KVRLMQENWI GKSSGVRFAF
     THDIRGADGQ PIQDGRLYVF TTRADTIMGV TFCAVAPEHP LALHAAATSP KLAAFIEECK
     KGGTTEAELA VKEKEGLPTG LFVTHPLTGA QVEVWVGNYV LMSYGDGAVM GVPAHDERDF
     AFAKKYGIAI RQVIAVEGET FSTEAWADWY GDKQRAVCIE SGELDGLPHA AAVDKVAELL
     AAKGLGEKKT TWRLRDWGVS RQRYWGTPIP IIHCEDCGAQ PVPAKDLPVV LPQDLVPDGS
     GNPLIKSEAF HAGVVCPCCG KSARRETDTM DTFVDSSWYF MRYCDARNSE QMVAEGAEYW
     MRDQNAATGG SGMDQYIGGI EHAILHLLYA RFWTKVMRDL GLVKVDEPFT KLLTQGMVLN
     HIYSRRTAKG AKEYFWPKDV EHVFDETGKI VGAKLKAEVD SADGLLPVGT DIDYEGVGTM
     SKSKNNGIDP QELIEKYGAD TARLYTMFTA PPELTLEWND AAVEGSYRFL RRVYNFGAKL
     SQMDMAGAVQ SVAGAKSLDD VEFGKAAKSL RLEIHTVLKQ VEYDYQRMQY NTVVSGAMKM
     INALEDFKSF DDAGAQVALI EGFGILLRVL YPATPHLAHA LWSELGYAAH LGDVLDAPWP
     QVDPQALVQD EISLVLQVNG KLRGAILVSS TADKAEIERI ALANEECQKF TNGAVPKKVI
     VVPGRLVNVV V
//