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}.
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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
//
