ID SYL_PSEAB Reviewed; 873 AA. AC Q02SF5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 14-NOV-2006, sequence version 1. DT 27-MAR-2024, entry version 104. 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=PA14_12230; OS Pseudomonas aeruginosa (strain UCBPP-PA14). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=208963; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=UCBPP-PA14; RX PubMed=17038190; DOI=10.1186/gb-2006-7-10-r90; RA Lee D.G., Urbach J.M., Wu G., Liberati N.T., Feinbaum R.L., Miyata S., RA Diggins L.T., He J., Saucier M., Deziel E., Friedman L., Li L., Grills G., RA Montgomery K., Kucherlapati R., Rahme L.G., Ausubel F.M.; RT "Genomic analysis reveals that Pseudomonas aeruginosa virulence is RT combinatorial."; RL Genome Biol. 7:R90.1-R90.14(2006). 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; CP000438; ABJ13262.1; -; Genomic_DNA. DR RefSeq; WP_003137700.1; NZ_CP034244.1. DR AlphaFoldDB; Q02SF5; -. DR SMR; Q02SF5; -. DR KEGG; pau:PA14_12230; -. DR PseudoCAP; PA14_12230; -. DR HOGENOM; CLU_004427_0_0_6; -. DR BioCyc; PAER208963:G1G74-1017-MONOMER; -. DR Proteomes; UP000000653; 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..873 FT /note="Leucine--tRNA ligase" FT /id="PRO_1000009398" FT REGION 624..643 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 42..52 FT /note="'HIGH' region" FT MOTIF 632..636 FT /note="'KMSKS' region" FT BINDING 635 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 873 AA; 97650 MW; C3CCEB1C5DD016F2 CRC64; MHEQYQPLEI ETQAQNYWKE HQSFLVRELP DKEKFYCLSM FPYPSGKLHM GHVRNYTIGD VISRYHRMQG RNVLQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIAYMKS QLDSLGLAID WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG ALIEKREIPM YYFKITAYAE ELLESLDNLP GWPEQVKTMQ RNWIGKSRGM EIGFPYDQAS IGHAGQLKVF TTRPDTLMGA TYVAVAAEHP LATQAAQNDP QLQAFIDECK RGGVAEADIA TQEKKGMATS LFVEHPLTGD KLPVWVANYV LMNYGEGAVM AVPGHDERDF EFANKYGLPI RQVIAKVEGD DDFESSVWKE WYGAKDESVL TVNSGKYDNL GYQAAFDAIG ADLEAKGLGQ ARTQFRLRDW GISRQRYWGC PIPIIHCEAC GDVPVPADQL PVVLPEDVVP DGSGSPLAKM PEFYECSCPK CGQPAKRETD TMDTFVESSW YFARYACPQF EGGMLDRKAA DYWLPVDQYI GGIEHAILHL LYARFFHKLM RDEGLVGSDE PFKNLLTQGM VVADTYYRTT ANGGKDWFNP ADVEVERDAK AKVVGARLKS DGQPVEIGGT EKMSKSKNNG VDPQSMIDQY GADTCRLFMM FASPPDMSLE WSDAGVEGAN RFLRRVWRLA HAHVSAGLPG ALDVAALDDA QKQVRRAIHL AIRQASQDVG QHHKFNTAIA AVMTLMNVLE KAPNQDAQDR ALIQEGLETV VLLLAPITPH ICHVLWGQLG HAEAVIDARW PSVDESALVQ DTLQLVVQVN GKLRGHIDVA ASASREDVEA AARANENVLR FTEGLSIRKV IVVPGKLVNI VAN //