SYL_COREF
ID SYL_COREF Reviewed; 957 AA.
AC Q8FLM0;
DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=CE2848;
OS Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189
OS / NBRC 100395).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=196164;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395;
RX PubMed=12840036; DOI=10.1101/gr.1285603;
RA Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S.,
RA Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.;
RT "Comparative complete genome sequence analysis of the amino acid
RT replacements responsible for the thermostability of Corynebacterium
RT efficiens.";
RL Genome Res. 13:1572-1579(2003).
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; BA000035; BAC19658.1; -; Genomic_DNA.
DR RefSeq; WP_006768798.1; NZ_GG700684.1.
DR AlphaFoldDB; Q8FLM0; -.
DR SMR; Q8FLM0; -.
DR STRING; 196164.23494692; -.
DR PRIDE; Q8FLM0; -.
DR EnsemblBacteria; BAC19658; BAC19658; BAC19658.
DR KEGG; cef:CE2848; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001409; 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 Gene3D; 3.40.50.620; -; 2.
DR Gene3D; 3.90.740.10; -; 1.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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 PANTHER; PTHR43740; PTHR43740; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; SSF47323; 1.
DR SUPFAM; SSF50677; SSF50677; 1.
DR TIGRFAMs; TIGR00396; leuS_bact; 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..957
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152006"
FT MOTIF 70..81
FT /note="'HIGH' region"
FT MOTIF 727..731
FT /note="'KMSKS' region"
FT BINDING 730
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 957 AA; 107399 MW; A6FFBF26AAFBC1FF CRC64;
MTNPSEGTSS SAQSLAYRYT PELANAIERE WQNYWTDKGT FNAPNPVGDL APEDGRELPG
DKLFVQDMFP YPSGAGLHVG HPLGYIATDV FARYNRMLGK NVLHTLGYDA FGLPAEQYAI
QTGTHPRTTT MANIENMKRQ LGALGLGHDP RRAVASTDPE FYKWTQWIFL QIFNSWFDEE
QQKARPISEL IPLLESGEIP TRDGADYNGL DRVAKQKAID EFRLVYRSNS TVNWCPGLGT
VLANEEVTAD GRSERGNFPV FRKNLSQWMM RITAYSDRLI DDLELLDWPE KVKSMQRNWI
GRSRGAEVDF TAEGETITVF TTRPDTLFGA TYMVLAPEHE LVDVLVSRGT GSYDGVDPRW
TNGQATPAEA VAAYRASIAA KSDLERQENK DKTGVFLGVH ATNPVNGEQI PVFIADYVLT
GYGTGAIMAV PAHDDRDYEF ATVFGLPIVE VVAGGNIAEA AYTASGESIN SANDQGLDIN
GLAMVDAVAR TIEWLEEKQL GRGTIQYKLR DWLFARQRYW GEPFPVVYDE DGVAYALPES
MLPVELPEVE DYKPVSFDPE DADSEPSPPL AKAREWVEVE LDLGDGVKKY TRDTNVMPQW
AGSSWYQLRY IDPTNDDQFC NLENEAYWTG PRPDVHGPND PGGVDLYVGG VEHAVLHLLY
SRFWHKVLYD LGYVTSKEPY RRLYNQGYIQ AFAYTDSRGV YVPAEEVEEK DGKFFYQGEE
VTQEYGKMGK SLKNAVAPDD ICNNYGADTL RVYEMSMGPL DTSRPWATKD VVGAQRFLQR
LWRLIVDENT GEVLTRDEAL TDEDNKHLHR TIAGVRDDYA NLRVNTVVAK LIEYVNYLTK
TYPDTIPTGA VLPLVVMVSP VAPHIAEELW KKLGHTDTVT YEPFPTFEEK WLTDDEVELP
VQINGKVRSR ITVAADASQE QIIEVALADE KIALQIEGKN LIKQIVIPGR MVNLVVK
