SYL_BURCC
ID SYL_BURCC Reviewed; 864 AA.
AC B1JVG9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 79.
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};
GN OrderedLocusNames=Bcenmc03_0621;
OS Burkholderia cenocepacia (strain MC0-3).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=406425;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MC0-3;
RA Copeland A., Lucas S., Lapidus A., Barry K., Bruce D., Goodwin L.,
RA Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S.,
RA Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cenocepacia MC0-3.";
RL Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000958; ACA89799.1; -; Genomic_DNA.
DR RefSeq; WP_006476924.1; NC_010508.1.
DR AlphaFoldDB; B1JVG9; -.
DR SMR; B1JVG9; -.
DR EnsemblBacteria; ACA89799; ACA89799; Bcenmc03_0621.
DR KEGG; bcm:Bcenmc03_0621; -.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002169; Chromosome 1.
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; 2.
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..864
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091297"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 624..628
FT /note="'KMSKS' region"
FT BINDING 627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 864 AA; 96284 MW; 2D97E3C136D570A7 CRC64;
MHERYVPADV EAAAQGDWRA ADAYKTKEDS QKPKFYCVSM LPYPSGKLHM GHVRNYTIND
VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAKW TYDNIDYMKG QMQSMGLAID
WSREIATCKP DYYKWNQWLF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALVEKREIPM YYLRITQYAD ELLNDLDGLG WPERVKIMQQ NWIGKSFGVN FGFPYELDGE
QKLLRVFTTR ADTIMGVTFC AIAAEHPLAT RLAQDKPELL AFIEECKRGG VAEADVATME
KKGVATGFSV KHPLTGEPVE VWIGNYVLMS YGEGAVMGVP GHDERDFAFA KKYDLPIRQV
IASEGQTYSL DAWQEWYGDK ETAVCVNSGK YDGLRYAEAV DAVAADLKAG GFGDKQVTWR
LRDWGVSRQR YWGTPIPIIH CPSCGDVPVP EQDLPVVLPE DLVPDGSGNP LAKSEAFLNC
TCPKCGAAAK RETDTMDTFV DSSWYFSRYT APDAETMVDA RTDYWMPMDQ YIGGIEHAIL
HLLYSRFWTK VMRDLGLVKF GEPAKNLLTQ GMVLNETYYR EDAAGKKTWY NPLDVTVTHD
DKGRPVGATL NADGQPVVLG GIEKMSKSKN NGVDPQLLID QYGADTARLF TMFAAPPEQQ
LEWSGAGVEG ASRFLRRVWS FGYGNREALA ARAGFDAATL GDADKALRRE IYSVLKQADF
DYQRLQYNTV VSAAMKMLNA IDGAKGATPA VLRETYGVLL RVLYPVVPHV TFELWKTLGY
ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ VNGKVRGALK VAKDASRDAI EAAAVADEAF
AKFSDGKPAK KIVVVPGRLV NIVV