ID SYL_SORC5 Reviewed; 854 AA. AC A9EYY7; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 1. DT 27-MAR-2024, entry version 94. 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=sce7417; OS Sorangium cellulosum (strain So ce56) (Polyangium cellulosum (strain So OS ce56)). OC Bacteria; Myxococcota; Polyangia; Polyangiales; Polyangiaceae; Sorangium. OX NCBI_TaxID=448385; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=So ce56; RX PubMed=17965706; DOI=10.1038/nbt1354; RA Schneiker S., Perlova O., Kaiser O., Gerth K., Alici A., Altmeyer M.O., RA Bartels D., Bekel T., Beyer S., Bode E., Bode H.B., Bolten C.J., RA Choudhuri J.V., Doss S., Elnakady Y.A., Frank B., Gaigalat L., Goesmann A., RA Groeger C., Gross F., Jelsbak L., Jelsbak L., Kalinowski J., Kegler C., RA Knauber T., Konietzny S., Kopp M., Krause L., Krug D., Linke B., Mahmud T., RA Martinez-Arias R., McHardy A.C., Merai M., Meyer F., Mormann S., RA Munoz-Dorado J., Perez J., Pradella S., Rachid S., Raddatz G., Rosenau F., RA Rueckert C., Sasse F., Scharfe M., Schuster S.C., Suen G., RA Treuner-Lange A., Velicer G.J., Vorholter F.-J., Weissman K.J., Welch R.D., RA Wenzel S.C., Whitworth D.E., Wilhelm S., Wittmann C., Bloecker H., RA Puehler A., Mueller R.; RT "Complete genome sequence of the myxobacterium Sorangium cellulosum."; RL Nat. Biotechnol. 25:1281-1289(2007). 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; AM746676; CAN97586.1; -; Genomic_DNA. DR AlphaFoldDB; A9EYY7; -. DR SMR; A9EYY7; -. DR STRING; 448385.sce7417; -. DR KEGG; scl:sce7417; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_7; -. DR OrthoDB; 9810365at2; -. DR BioCyc; SCEL448385:SCE_RS37990-MONOMER; -. DR Proteomes; UP000002139; 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 Gene3D; 3.10.20.590; -; 1. DR Gene3D; 3.40.50.620; HUPs; 2. DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1. 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; 1. 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. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1..854 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000334822" FT REGION 1..32 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 69..80 FT /note="'HIGH' region" FT MOTIF 633..637 FT /note="'KMSKS' region" FT BINDING 636 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 854 AA; 95563 MW; 0D0B4545E599E4D8 CRC64; MARRDMAAET MDPRASTEPS PNEPREPARY DHAAVEPRWQ RAWEEGETFR AVRSADPARG KRYVLDMFPY PSGSGLHVGH PEGYTATDIM SRYFRMRGID VLHVMGWDAF GLPAEQHALE TGTHPADTTA RNIATFKRQL KMLGFSYDWS RELSTTDPRY VRWTQWIFLQ LFKKGLAYQD EVSVNWCPAL GTVLANEEVI DGKSERGSHP VYRTPLRQWM LRITAYADRL AEDLRLLDWP EGTVAMQRSW IGRSEGALIT FEVKGWGKGA LSVFTTRPDT LMGVTYVVLA PEHPLTTWLT SAESGASEPR REAVRAYVAA AAGKSDRERL AAAAREKTGV DTGLVAVHPI TGVEVPIWVA DYVLGGYGTG AVMAVPGHDE RDFSFARTYG LPIVEVVSPD GSLHDQLEAA YVDPGVAVRS GEFDGLATEE CKRAVIARLE ALGRGKREVN YKLRDWVFSR QRYWGEPIPI YFPVELADPQ GDPRKGAAHT IRYDQPIAVD EASLPIELPP LADFRPGDDP AGPLARAVDW RFFQRDGKWY ARETNTMPQW AGSCWYYLRF LDPQNDAEPF SEAAYDAWMP VDLYVGGAEH GVLHLLYARF WHKVLYDLGH VKHPEPFAKL VHQGMILGED NEKMSKSRGN VINPDDIVRA HGADVLRMYE MFMGPLEAVK PWQSGQIQGV VRFRDRVFAT CTRPLSDAMD DATSRQLHRT IKKVTGDIEG MAFNTAISAM MVFVNHLSSL PSPPREAVLR LILLVSPFAP HLAEELWRLT GHERSLSYEP WPTYDEAFCV DDVLEIPVQV NGKVRGRVML AKAASEEEAR AAALGLETVA ALAAGKQLKK FIYVAGKIVN IVVG //