ID SYL_HAEIG Reviewed; 861 AA. AC A5UI62; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 99. 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=CGSHiGG_08170; OS Haemophilus influenzae (strain PittGG). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Haemophilus. OX NCBI_TaxID=374931; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PittGG; RX PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103; RA Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., RA Ehrlich G.D.; RT "Characterization and modeling of the Haemophilus influenzae core and RT supragenomes based on the complete genomic sequences of Rd and 12 clinical RT nontypeable strains."; RL Genome Biol. 8:R103.1-R103.18(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; CP000672; ABR00468.1; -; Genomic_DNA. DR AlphaFoldDB; A5UI62; -. DR SMR; A5UI62; -. DR KEGG; hiq:CGSHiGG_08170; -. DR HOGENOM; CLU_004427_0_0_6; -. DR Proteomes; UP000001990; 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..861 FT /note="Leucine--tRNA ligase" FT /id="PRO_1000009349" FT MOTIF 42..52 FT /note="'HIGH' region" FT MOTIF 619..623 FT /note="'KMSKS' region" FT BINDING 622 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 861 AA; 97692 MW; 4F63A50073431A45 CRC64; MQEQYRPDMI EPKVQQYWVE NKVFKAIKDE SKEKYYCLSM FPYPSGRLHM GHVRNYTIGD VISRYQRMLG KNVLQPFGWD AFGLPAEGAA IKNKTAPAKW TYENIAYMKK QLQLLGFGFD WDREIATCKP EYYKWEQWFF TELYKKGLVY KKTSTVNWCP NDETVLANEQ VHEGCCWRCD TPVEQKEIPQ WFIKITDYAE QLLGGLDTLP QWPDMVKTMQ RNWIGRSEGV EITFDVANTN EKVAVYTTRP DTFYGVSYLG IAAAHPLASL AAQNNPELAA FIQEAKNAKV AEADLATMEK KGMATGLFAI HPLTGEKLPI WVANFVLMHY GTGAVMAVPA HDQRDFEFAQ KYSLPIKQVI APLADEEIDL TKQAFVEHGK LVNSAEFDGK DFDGAFNGIA DKLEKLGVGK RQVNYRLRDW GVSRQRYWGA PIPMLTLENG DVVPAPMEDL PIILPEDVVM DGVKSPIKAD PNWAKTTLNG TPALKETDTF DTFMESSWYY ARYTCPQYQN GMLDAEEANY WLPVDQYIGG IEHATMHLLY FRFFHKLLRD AGFVTSEEPA DKLLCQGMVL ADAFYYTSPT NERIWVSPTQ VTLERDEKGR IIKATDPEGR ELVHSGMTKM SKSKNNGIDP QEMVEKYGAD TVRLFMMFAS PAEMTLEWQE SGVEGAKRFL GRVWNLVYQY QQNPAKTSLD ITALSAEQKV LRREVHKTIA KVSDDIGRRQ TFNTAIAAVM ELMNKLTKAP LDSEQDRAVM AEALSAVVRM LYPITPHICF ELWQALGNES AIDTAEWVKA DEAAMVEDEK LIVVQVNGKV RGKVTVAADA DEDTVKTIAF ADENVKKFID NQHIVKVIYV VGKLLNVVVK P //