ID SYL_BURM7 Reviewed; 864 AA. AC A3MPH9; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 03-APR-2007, sequence version 1. DT 27-MAR-2024, entry version 97. 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=BMA10247_2640; OS Burkholderia mallei (strain NCTC 10247). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=320389; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NCTC 10247; RX PubMed=20333227; DOI=10.1093/gbe/evq003; RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S., RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J., RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P., RA Nierman W.C.; RT "Continuing evolution of Burkholderia mallei through genome reduction and RT large-scale rearrangements."; RL Genome Biol. Evol. 2:102-116(2010). 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 --------------------------------------------------------------------------- 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; CP000548; ABO06808.1; -; Genomic_DNA. DR RefSeq; WP_011832247.1; NZ_CP007802.1. DR AlphaFoldDB; A3MPH9; -. DR SMR; A3MPH9; -. DR KEGG; bmaz:BM44_681; -. DR KEGG; bmn:BMA10247_2640; -. DR PATRIC; fig|320389.8.peg.749; -. 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..864 FT /note="Leucine--tRNA ligase" FT /id="PRO_1000009307" FT MOTIF 42..52 FT /note="'HIGH' region" FT MOTIF 624..628 FT /note="'KMSKS' region" FT BINDING 627 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 864 AA; 96207 MW; 78C08D37FEA718FE CRC64; MHERYVPADV EAAAQSDWRA ADAYRSKEDA NRKKFYCVSM LPYPSGKLHM GHVRNYTIND VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAQW TYENIAYMKK QMQAMGLAID WSREVTTCKP DYYKWNQWLF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG AFVEKREIPM YYMRITQYAD ELLNDLDGLG WPERVKVMQH NWIGKSFGVN FGFPYELDGE KKLLRVFTTR ADTIMGVTFC AIAAEHPLAA RLARDKPALQ AFIDECKRGG VAEADIATME KKGVATGFSV SHPLTGEPVE VWIGNYVLMS YGEGAVMGVP AHDERDFAFA KKYGLPIRQV IAVEGETYST DAWQEWYGDK TRAVCVNSGK YDGLAYDAAV DAIAAELKAG GLGDKQITYR LRDWGISRQR YWGTPIPIIH CPSCGDVPVP EQDLPVVLPE DLVPDGTGNP LAKSDAFLNC TCPKCGAVAK RETDTMDTFV DSAWYFSRYA APDAQTMVDA RTDYWMPMDQ YIGGIEHAIL HLLYSRFWAK VMRDLGLVAF GEPAKNLLTQ GMVLNETFYR EDAAGKKTWY NPADVTVSFD DKGRPVGAVL KSDGQPVELG GIEKMSKSKN NGVDPQMLID HYGADTARLF TMFAAPPEQQ LEWSGAGVDG ASRFLRRVWA FGFANREALA VRAPFDAAQL AEAGKTLRRE IHGVLKQADF DYQRLQYNTV VSAAMKMLNA IEGAKGATPA VLRETYGVLL RVLYPVVPHV TFELWKVLGY ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ VNGKVRGALK VAKDASREAI EAAAVADGMF AKFAEGRPAK KIIVVPGRLV NVVV //