ID   SYL_XANC8               Reviewed;         879 AA.
AC   Q4UWK8;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   27-MAR-2024, entry version 129.
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=XC_1497;
OS   Xanthomonas campestris pv. campestris (strain 8004).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=314565;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=8004;
RX   PubMed=15899963; DOI=10.1101/gr.3378705;
RA   Qian W., Jia Y., Ren S.-X., He Y.-Q., Feng J.-X., Lu L.-F., Sun Q.,
RA   Ying G., Tang D.-J., Tang H., Wu W., Hao P., Wang L., Jiang B.-L., Zeng S.,
RA   Gu W.-Y., Lu G., Rong L., Tian Y., Yao Z., Fu G., Chen B., Fang R.,
RA   Qiang B., Chen Z., Zhao G.-P., Tang J.-L., He C.;
RT   "Comparative and functional genomic analyses of the pathogenicity of
RT   phytopathogen Xanthomonas campestris pv. campestris.";
RL   Genome Res. 15:757-767(2005).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY48565.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000050; AAY48565.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_029628914.1; NC_007086.1.
DR   AlphaFoldDB; Q4UWK8; -.
DR   SMR; Q4UWK8; -.
DR   KEGG; xcb:XC_1497; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   Proteomes; UP000000420; 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; 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.
FT   CHAIN           1..879
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334837"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   879 AA;  98416 MW;  F7E1CB145F1B4807 CRC64;
     MSTVEPNAYD PQQVETSAQQ FWDATRAFQV DENSDKPKFY CLSMLPYPSG ALHMGHVRNY
     TISDVVSRYK RMTGHNVLQP MGWDAFGLPA ENAAIKNKTA PAKWTYANIE HMRAQLKSLG
     YAIDWSREFA TCTPDYYVHE QRMFTRLMRK GLAYRRNAVV NWDPIDQTVL ANEQVIDGRG
     WRSGALVEKR EIPQWFLRIT DYAQELLDGL DQLDGWPDSV KTMQRNWIGR SEGLEIQFDV
     RDTTGAALDP LRVFTTRPDT LMGVTFVSIA AEHPLAQHAA KSNPELASML ETLKHGGVSE
     AELETQEKRG MATGLTAVHP ISGEEVPVWV ANFVLMGYGT GAVMAVPGHD QRDFEFANKY
     GLPIVQVVKL REPRNDDEQA WDATQWRDWY TDKSRELELI NSAEFDGLDY HGAFEALAER
     FERKGQGQRR INYRLRDWGV SRQRYWGCPI PVIYCAKCGA VPVPEDQLPV VLPENVEFAG
     TGSPIKTDPT WRQTTCPECG GPAERETDTF DTFMESSWYV ARYTSPNARD MVDRRANYWM
     PADLYVGGIE HAILHLMYFR FYHKLMRDAR LVDSDEPVTN LLTQGMVIAE TFYRDADNGG
     KDWINPADVE IQRDERGRVV GASLIADGQP VHIGGTEKMS KSKNNGVDPQ AMVAKYGADT
     VRLFSMFAAP PEQSLEWNEA GVDGMARFMR RLWVQVHKHV GEGAAALDVA SLSAEQKAIR
     RKTHETIGKV DDDYGRRHSF NTAIAAVMEL SNALAKFDDA SAQGRAVRQE ALEAMVLLLN
     PITPHASHAL WQVLGRGETL LENVPFPQVD AAALVRDALT LAIQVNGKLR GTIEVAADAA
     REQIEALALA EPNAAKFLDG LSVRKIIIVP GKIVNIVAG
//