SYL_LEUCK
ID SYL_LEUCK Reviewed; 803 AA.
AC B1MY11;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=LCK_00580;
OS Leuconostoc citreum (strain KM20).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=349519;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KM20;
RX PubMed=18281406; DOI=10.1128/jb.01862-07;
RA Kim J.F., Jeong H., Lee J.-S., Choi S.-H., Ha M., Hur C.-G., Kim J.-S.,
RA Lee S., Park H.-S., Park Y.-H., Oh T.K.;
RT "Complete genome sequence of Leuconostoc citreum KM20.";
RL J. Bacteriol. 190:3093-3094(2008).
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; DQ489736; ACA82413.1; -; Genomic_DNA.
DR RefSeq; WP_004908127.1; NC_010471.1.
DR AlphaFoldDB; B1MY11; -.
DR SMR; B1MY11; -.
DR STRING; 349519.LCK_00580; -.
DR EnsemblBacteria; ACA82413; ACA82413; LCK_00580.
DR GeneID; 61102488; -.
DR KEGG; lci:LCK_00580; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002166; 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 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 PANTHER; PTHR43740; PTHR43740; 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; 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.
FT CHAIN 1..803
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091334"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 575..579
FT /note="'KMSKS' region"
FT BINDING 578
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 803 AA; 91586 MW; 2E4AF1E47D8BE59C CRC64;
MPYEHQQIEQ KWQKFWDDNQ TFATSDTTDK PKYYAVDMFP YPSGQGLHVG HPEGYTATDI
MSRFKRAKGF NVLHPMGWDA FGLPAEQYAM KTGHNPADFT SQNIDHFREQ IKSLGLSYDW
NREINTTDPS YYKWTQWIFE KLYEKGLAYE SNMMVNWDPI DRVVLANEEV IDGKSERSGN
KVERKALRQW VLKITAYADR LVDDLDDLDW PEAIKEQQRN WIGRSKGAAV FFNVDHADAK
IEVYTTRPDT LFGATYMVLA PEHELVDSIV TAEQKQAVAD YRAAIAAKSD LERTDLNKDK
TGVFTGAYGI NPINGEKLPI WIADYVLASY GTGAIMAVPA HDDRDFEFAK KFDLAIKPVI
AGGENDDVAY TGDGVHINSD FLDGLDKATA IDQAIDWLEA HQAGHAQTNF RLRDWIFSRQ
RYWGEPIPVI HWEDGTTSLV PENELPLLLP HATELRPSGS GESPLANLTD WLEVTRDDGV
KGRRETNTMP QWAGSSWYFL RYIDPHNDHQ LADPEKLKYW MNVDLYVGGA EHAVLHLLYA
RFWHKFLYDL GVVPTKEPFQ KLVNQGMILG ANHEKMSKSK GNVVNPDDIV REYGADTLRV
YEMFMGPLTQ SKPWSEEGIT GSRRWLDRVW RLLIDDEGQL RDHVTTVNPG DLDKIYHQTV
KKVTDDLENM RFNTAISQMM VFVNDAYKSD ALPVTYMNGF IQLLAPFAPH LAEELWVRLG
NRESISYVSW PTYDDTKLVD DTVEIIFQVN GKVRGKATVA RDINQDDMIT AAKADDNVQN
FITGKTVRKV IAIPGKFVNI VVS