ID SYL_MYCMS Reviewed; 804 AA.
AC Q6MSR0;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 2.
DT 27-MAR-2024, entry version 122.
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=MSC_0709;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(2004).
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 -!- SEQUENCE CAUTION:
CC Sequence=CAE77328.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BX293980; CAE77328.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_975686.1; NC_005364.2.
DR AlphaFoldDB; Q6MSR0; -.
DR SMR; Q6MSR0; -.
DR STRING; 272632.MSC_0709; -.
DR KEGG; mmy:MSC_0709; -.
DR PATRIC; fig|272632.4.peg.763; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_14; -.
DR Proteomes; UP000001016; 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; 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..804
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152047"
FT MOTIF 39..50
FT /note="'HIGH' region"
FT MOTIF 580..584
FT /note="'KMSKS' region"
FT BINDING 583
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 804 AA; 93178 MW; 8BD0473253647145 CRC64;
MDFSHKAIEK KWQKYWKENN IYKTTNNSEK KAYILDMFPY PSGAGLHVGH IKGYTATDVY
SRFKRMQGYD VLHPIGWDAF GLPAEQYALK TGNDPREFTL QNIENFKIQL NKMGFSYDYD
KEINTADPNY YKTTQWIFKQ LYKKGLAENR DIDVNWCQEL GTVLANDEII EKDGLMVSER
GEYPVVKKKM RQWVLKITDY ADKLLDGLDN LDWPNSVKEL QRNWIGKSEG CEINFKSNDI
NIPVFTTRAD TIFGVTYIVL ASENELVLKL TAPEKLEEVK KYIELTANKS EIERKDESRT
KTGVFIGSYA TNPLTKEQIQ IWISDYVLND YGSGAIMAVP AHDKRDWDFA AKFNLPIKFV
IQTKDQSKAF VGEGIHINSE FLNDLDRIQA LQVIHDYVDK NNLGKRKINY KLRDWLFSRQ
RFYGEPFPVL YDKDNNIVLI EDNNLPITLP ITDYIKPTNT GESPLANVKN WVNVKIGDKE
YKRETNTMPQ SAASSWYFIA YILANSKNNL IDLTSDEAKK RLEKWLPVDL YIGGQEHAVG
HLLYARFWTH FLYDLGLLPT NEPFKRLFNQ GMILGPDNRK MSKSWGNVIN PDDVIDTHGA
DALRLYEMFM GPLDASLPWS FDGLDASLKW LNRCYRMINK IEFSNTNNHK LDYVYNDVVK
KVTQMIQELK FNTAISQLMV LVNAIYKEEL NTVYKPYIEG FVKMLSLFAP HLSEELWEKL
GNNSSVTLQT WPEFDETKII KNAVVIALQV NGKLRSTIEV EKGTDKETLI KLAQENENII
RFIKDHKNLK YIAVVDRIVN IVIE
//
