ID SYL_XANC5 Reviewed; 880 AA. AC Q3BRE4; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 20-MAY-2008, sequence version 2. DT 27-MAR-2024, entry version 123. 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=XCV2938; OS Xanthomonas campestris pv. vesicatoria (strain 85-10). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales; OC Xanthomonadaceae; Xanthomonas. OX NCBI_TaxID=316273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=85-10; RX PubMed=16237009; DOI=10.1128/jb.187.21.7254-7266.2005; RA Thieme F., Koebnik R., Bekel T., Berger C., Boch J., Buettner D., RA Caldana C., Gaigalat L., Goesmann A., Kay S., Kirchner O., Lanz C., RA Linke B., McHardy A.C., Meyer F., Mittenhuber G., Nies D.H., RA Niesbach-Kloesgen U., Patschkowski T., Rueckert C., Rupp O., Schneiker S., RA Schuster S.C., Vorhoelter F.J., Weber E., Puehler A., Bonas U., Bartels D., RA Kaiser O.; RT "Insights into genome plasticity and pathogenicity of the plant pathogenic RT Bacterium Xanthomonas campestris pv. vesicatoria revealed by the complete RT genome sequence."; RL J. Bacteriol. 187:7254-7266(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=CAJ24617.1; 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; AM039952; CAJ24617.1; ALT_INIT; Genomic_DNA. DR RefSeq; WP_041855068.1; NZ_CP017190.1. DR AlphaFoldDB; Q3BRE4; -. DR SMR; Q3BRE4; -. DR STRING; 456327.BJD11_08170; -. DR KEGG; xcv:XCV2938; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_6; -. DR Proteomes; UP000007069; 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..880 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000334839" 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; 98598 MW; A7CB171CE5E416A9 CRC64; MSTVEPNVYD PQQVETSAQQ FWDATRAFQV DENSEKPKFY CLSMLPYPSG ALHMGHVRNY TISDVVSRYK RMTGHNVLQP MGWDAFGLPA ENAAIKNKTA PAKWTYANIE HMRAQLKSLG YAIDWSREFA TCTPDYYVHE QRMFTRLMRK GLAYRRNAVV NWDPIDQTVL ANEQVIDGRG WRSGALVEKR EIPQWFLRIT DYAQELLDGL DQLDGWPDSV KTMQRNWIGR SEGLEIQFDV RDIDGAPLDP LRVFTTRPDT LMGVTFVSIA AEHPLALHAA KSNPELAALL ETLKHGGVSE AELETQEKRG MATGLTAVHP ISGEQVPVWV ANFVLMGYGT GAVMAVPGHD QRDFEFANKY GLPIVQVVKL REPRNEEEQT WDATHWRDWY TDKSRELELI NSAEFDGLDF GGAFEALAER FERKGQGQRR VNYRLRDWGV SRQRYWGCPI PVIYCAKCGA VPVPEDQLPV VLPENVEFSG TGSPIKTDPT WRQTTCPDCG GPAERETDTF DTFMESSWYV ARYTSPNARD MVDRRANYWM PADLYVGGIE HAILHLMYFR FYHKLMRDAR LVDSDEPVTN LLTQGMVIAE TFYRDADNGG KDWINPADVE IQRDERGRVT GAVLIADGQP VHIGGTEKMS KSKNNGVDPQ SMVAKYGADT VRLFSMFAAP PEQSLEWNEA GVDGMARFMR RLWVQVHKHV GEGAAVALDV AVLSAEQKAI RRKTHETIGK VSDDYGRRHS FNTAIAAVME LSNALAKFDD ASEQGRAVRQ EALEAMVLLL NPITPHASHA LWQVLGRGET LLENVAFPQA DASALVRDAL TLAVQINGKL RGTIDVAADA TREQIEALAQ AEPNAAKFLE GLSVRKIIIV PGKIVNIVAG //