ID   SYL_XANOM               Reviewed;         880 AA.
AC   Q2P0N0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   03-AUG-2022, entry version 111.
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}; OrderedLocusNames=XOO3142;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests contribution of
RT   large numbers of effector genes and insertion sequences to its race
RT   diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(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}.
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DR   EMBL; AP008229; BAE69897.1; -; Genomic_DNA.
DR   RefSeq; WP_011409106.1; NC_007705.1.
DR   AlphaFoldDB; Q2P0N0; -.
DR   SMR; Q2P0N0; -.
DR   KEGG; xom:XOO3142; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
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   Gene3D; 3.40.50.620; -; 2.
DR   Gene3D; 3.90.740.10; -; 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   PANTHER; PTHR43740; PTHR43740; 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; SSF47323; 1.
DR   SUPFAM; SSF50677; SSF50677; 1.
DR   TIGRFAMs; TIGR00396; leuS_bact; 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..880
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009465"
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   880 AA;  98457 MW;  7033BDE6E7B4D707 CRC64;
     MSTVEPNVYD PHQVETSAQQ FWDATRAFQV DESSEKPKFY CLSMLPYPSG ALHMGHVRNY
     TISDVVSRYK RMTGHNVLQP MGWDAFGLPA ENAAIKNKTA PAKWTYANIA HMRAQLKSLG
     YAIDWSREFA TCTPDYYVHE QRMFTRLMRK GLAYRRNAVV NWDPIDQTVL ANEQVIDGRG
     WRSGAVVEKR EIPQWFLRIT DYAQELLDGL DQLDGWPDSV KTMQRNWIGR SEGLEIQFDV
     RDTNGAALDP LRVFTTRPDT LMGVTFVSIA AEHPLALHAA KSNPELAALL ETLKHGGVSE
     AELETQEKRG MATGLTAVHP ISGEQVPVWV ANFVLMGYGT GAVMAVPGHD QRDFEFANKY
     GLPIVQVVKL REPRNDDEQR WDATEWRDWY TDKSRELELI NSAEFDGLDF GGAFEALAER
     FERKGQGQRR VNYRLRDWGV SRQRYWGCPI PVIYCPKCGA VPVPEDQLPV VLPENVEFAC
     TGSPIKTDPT WRQTTCPDCG GPAERETDTF DTFMESSWYV ARYTSPNARE MVDRRANYWM
     PADLYVGGIE HAILHLMYFR FYHKLMRDAR LVDSDEPVTN LLTQGMVIAD TFYRDADNGG
     KDWINPADVE IQRDERGRVT GAVLIADGQP VHIGGTEKMS KSKNNGVDPQ SMVAKYGADT
     VRLFSMFAAP PEQSLEWNEA GVDGMARFMR RLWAQVHKHV GEGAAVALDV AALSAEQKAI
     RRKTHETIGK VSDDYGRRHS FNTAIAAVME LSNALAKFDD ASDQGRAVRQ EALEAMVLLL
     NPITPHASHA LWQVLGRGET LLENVAFPQA DVSALVRDAL TLAVQINGKL RGTIDVAADA
     AREQIEALAQ AEPNAAKFLD GLSVRKIIIV PGKIVNIVAG