ID SYL_MYCPN Reviewed; 793 AA. AC P75398; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 137. 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=MPN_384; ORFNames=MP453; OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1) OS (Mycoplasmoides pneumoniae). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=272634; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 29342 / M129 / Subtype 1; RX PubMed=8948633; DOI=10.1093/nar/24.22.4420; RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.; RT "Complete sequence analysis of the genome of the bacterium Mycoplasma RT pneumoniae."; RL Nucleic Acids Res. 24:4420-4449(1996). 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; U00089; AAB96101.1; -; Genomic_DNA. DR PIR; S73779; S73779. DR RefSeq; NP_110072.1; NC_000912.1. DR RefSeq; WP_010874740.1; NC_000912.1. DR AlphaFoldDB; P75398; -. DR SMR; P75398; -. DR STRING; 272634.MPN_384; -. DR EnsemblBacteria; AAB96101; AAB96101; MPN_384. DR KEGG; mpn:MPN_384; -. DR PATRIC; fig|272634.6.peg.415; -. DR HOGENOM; CLU_004427_0_0_14; -. DR OrthoDB; 9810365at2; -. DR BioCyc; MPNE272634:G1GJ3-608-MONOMER; -. DR Proteomes; UP000000808; 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; cd00812; LeuRS_core; 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; 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; 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. 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; Reference proteome. FT CHAIN 1..793 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000152050" FT MOTIF 39..50 FT /note="'HIGH' region" FT MOTIF 569..573 FT /note="'KMSKS' region" FT BINDING 572 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049" SQ SEQUENCE 793 AA; 91084 MW; DAD90195932B62D9 CRC64; MYNHNLLEEK WLQLWKTKQV NRFFDDKTKP KYYILDMFPY PSAAGLHLGH VRAYTITDVL SRYHKAKGFN VIHPIGFDAF GLPAEQYAIA SNKHPGDWTD KNITNFIEQL TAFGFDYDYQ LSLKTTDPRY YQYTQWIFGQ LFEAGLAEVK EIDVNWCAEL GTVLANEEVL IDSNGNAVSE RGEFPVTKRK MKQWVLKITA FAESLLNGLA ELDWHQSIKE MQTNWIGKSE GVEVTFDIEN SKETITIFTT KVQTIFGVTF LALSNSHPLV KEVAKTNPKI AQFLQKQAQK TTTVKQPETL HDGVDLKLKA INPATNTAIP LYVANYVVEG YGTDAVMGVP AHNENDNFFA RKQKLPIITV IDKQERLQHS GQFSGLNSQT ANTQITQMLV ERQKAKKTTV YKLRDWIFSR QRYWGEPFPI LFDENNQPHL VKELPVTLPA LANYQPDGST NPPLWRNQEW AKVKQGNQTF TRETSTMPQW AGSCWYYLGY LMLINNENFW PIDSREAKDL FERYLPVDLY VGGAEHAVLH LLYARFWHQF LYQKGIVTTK EPFKKLINQG MVLGPDGKKM SKSKGNTINP TPLIDSHGAD ALRLYLMFMG PISAALTWLD DGLNGMRRWL DRVHNFFHKE NIIKETVDQE TVYGYNLFLK RSFEHLEKQE LNLVISQMMI FLNLLYKTKQ LTLAYAKGFL TVLSFFAPYL AEELNAKLGM EPFIVHAQLP NVDNSVLETD KVKIILSVNG RFKGTKEFAK GVDEQTVLKA FKTDPEFQAL FDQPLARVVF VPNRIINVLL KSE //