ID   SYL_PARDP               Reviewed;         844 AA.
AC   A1B5Q5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
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=Pden_2765;
OS   Paracoccus denitrificans (strain Pd 1222).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=318586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pd 1222;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Spiro S.,
RA   Richardson D.J., Moir J.W.B., Ferguson S.J., van Spanning R.J.M.,
RA   Richardson P.;
RT   "Complete sequence of chromosome 1 of Paracoccus denitrificans PD1222.";
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; CP000489; ABL70849.1; -; Genomic_DNA.
DR   RefSeq; WP_011749040.1; NC_008686.1.
DR   AlphaFoldDB; A1B5Q5; -.
DR   SMR; A1B5Q5; -.
DR   STRING; 318586.Pden_2765; -.
DR   EnsemblBacteria; ABL70849; ABL70849; Pden_2765.
DR   GeneID; 75502225; -.
DR   KEGG; pde:Pden_2765; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000361; Chromosome 1.
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; Reference proteome.
FT   CHAIN           1..844
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334787"
FT   MOTIF           39..49
FT                   /note="'HIGH' region"
FT   MOTIF           621..625
FT                   /note="'KMSKS' region"
FT   BINDING         624
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   844 AA;  93879 MW;  1DE1B82D42F62E75 CRC64;
     MPYDPAISEP RWQEAWEQAD TFRAVRDERP KYYVLEMFPY PSGRIHMGHV RNYTMGDVVA
     RFKRAQGFSV LHPMGWDAFG MPAENAAMEQ GGHPRDWTYG NIATMRGQLK PLGLSIDWSR
     EFATCDDAYV AQQQALFLDM LEAGLITRKS AQVNWDPVDM TVLANEQVID GKGWRSGATV
     ERKELTQWFF KISDYSDELL SALDGLEGWP EKVRLMQANW IGKSRGLQFR FHTVDLPDFP
     TIEVYTTRPD TLMGASFVAL SPDHPLVKAL AASDPKVAAF VEECRRIGTT EEAIETAPKM
     GFDTGLTVRH PLDADWRLPI WIANFVLMDY GTGAIFGSPA HDERDHEFAT KYGLPIRATF
     GERGMDLEQA DALVAKAPFV PLKSETVTYV RGFAGAADQT GEAAVDAAIR HAEVAGYGEG
     VTKFRLRDWG ISRQRYWGCP IPVVHCDACG TVPEAKANLP VLLPQDVSFE VPGNPLNRHP
     TWAATTCPKC GGPARRETDT MDTFVDSSWY YARFTSPHAA TPTDRPETDY WMNVDQYIGG
     IEHAILHLLY SRFFARAMVK TGHLPESAKE PFDALFTQGM VTHEIYMTRD ERGRPVYHLP
     EDVVDGKLAD GTPVEVIPSA KMSKSKKNVV DPVNIVEGFG ADTARWFMLS DSPPERDVEW
     TAAGAEAANR FLARVWRLAD EIPEDGADPD LTRAAHRAID EVTRAIEGFA FNKAVAKIYE
     LANAIAKSGA GGESRREALR IMAQLMAPMV PHLAEEIWMK AGGQGMVVDA TWPKADPALL
     VSDSVVLPIQ INGKRRAEIE VPKDMPKDQI EAIVLADETV RRFMEGQAPK KLIVVPGRIV
     NVVV
//