ID SYL_MYCGE Reviewed; 792 AA. AC P47508; Q49228; Q49290; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 27-MAR-2024, entry version 143. 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}; OrderedLocusNames=MG266; OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37) OS (Mycoplasmoides genitalium). OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae; OC Mycoplasmoides. OX NCBI_TaxID=243273; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=7569993; DOI=10.1126/science.270.5235.397; RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A., RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M., RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L., RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M., RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S., RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.; RT "The minimal gene complement of Mycoplasma genitalium."; RL Science 270:397-403(1995). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-96 AND 208-319. RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37; RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993; RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III; RT "A survey of the Mycoplasma genitalium genome by using random sequencing."; RL J. Bacteriol. 175:7918-7930(1993). 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; L43967; AAC71488.1; -; Genomic_DNA. DR EMBL; U01780; AAD10600.1; -; Genomic_DNA. DR EMBL; U02167; AAD12449.1; -; Genomic_DNA. DR PIR; D64229; D64229. DR RefSeq; WP_010869401.1; NC_000908.2. DR AlphaFoldDB; P47508; -. DR SMR; P47508; -. DR STRING; 243273.MG_266; -. DR KEGG; mge:MG_266; -. DR eggNOG; COG0495; Bacteria. DR HOGENOM; CLU_004427_0_0_14; -. DR InParanoid; P47508; -. DR OrthoDB; 9810365at2; -. DR BioCyc; MGEN243273:G1GJ2-322-MONOMER; -. DR Proteomes; UP000000807; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. 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; IBA:GO_Central. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central. DR CDD; cd00812; LeuRS_core; 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; 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; 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..792 FT /note="Leucine--tRNA ligase" FT /id="PRO_0000152045" 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" FT CONFLICT 86 FT /note="Q -> R (in Ref. 2; AAD10600)" FT /evidence="ECO:0000305" FT CONFLICT 225 FT /note="W -> V (in Ref. 2; AAD12449)" FT /evidence="ECO:0000305" SQ SEQUENCE 792 AA; 91474 MW; D2146C8681E10DA5 CRC64; MYNHNLIEEK WLKKWKNKDV NRFESDSNKK KYYVLDMFPY PSAAGLHLGH VRAYTITDVI SRYYKAKGFN VIHPIGFDAF GLPAEQYAIN SNQNPGSWTD QNINNFINQL TSFGFDYDYH LSLKTTDPRY YKYTQWIFSE LFKANLAELV DIDVNWCEQL GTVLANEEVL IDSNGNAVSE RGSFSVEKRK MKQWVLKITT FADALLEGLD TLDWPEPIKE MQRNWIGKSK GVTINFQLKD HKEAIAIFTT KPQTIFGVSF LAVSTNHWLA KKIAETNKKV ASFLKKQLQK TTTLKQKATL YDGIDLLTNA IHPLTNELIP VYVANYVIEG YGTDAIMGVG AHNENDNFFA RKQKLKIINV IDKKERLQNS FAYNGLTTKE AQVAITNELI SQNKAKLTTV YKLRDWIFSR QRYWGEPFPI IFDENNTPHL VEQLPVELPL LENYKPDGSG NSPLMRNQAW VNIVKDNIHY QRETNTMPQW AGSCWYYLGY LMLIKNPNFW PIDSKEAKKL FDQYLPVDLY VGGAEHAVLH LLYARFWHKF LFDKKLVSTK EPFQKLINQG MVLGPDGKKM SKSKGNTINP TPLVDSHGAD ALRLYLMFMG PISASLTWND EGLNGMRRWL DRVYNFFFNH AVVTDQVSQE TIFAYNLFLK NSYCHLDKHE LNLVISEMMI FLNFLYKTKK ISLNYAKGFL TVLSFFAPFL AEELNEKCGL EPFVVKQAIS LVDYQLFETA KTKVILSING KFKAAKEFTK GSLEIDVLES FKQDKEINDI LNQPIERVVY VQDRIINVLL KK //