SYL_BURVG
ID SYL_BURVG Reviewed; 864 AA.
AC A4JBI1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
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=Bcep1808_0622;
OS Burkholderia vietnamiensis (strain G4 / LMG 22486) (Burkholderia cepacia
OS (strain R1808)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=269482;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G4 / LMG 22486;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia vietnamiensis G4.";
RL Submitted (MAR-2007) 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; CP000614; ABO53634.1; -; Genomic_DNA.
DR AlphaFoldDB; A4JBI1; -.
DR SMR; A4JBI1; -.
DR STRING; 269482.Bcep1808_0622; -.
DR EnsemblBacteria; ABO53634; ABO53634; Bcep1808_0622.
DR KEGG; bvi:Bcep1808_0622; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002287; 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 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; 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; Reference proteome.
FT CHAIN 1..864
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009313"
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; 95894 MW; F36A604A3974ED22 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
KALLRVFTTR ADTIMGVTFC AIAAEHPLAT RLAQGKPELQ AFIDECKRGG VAEADVATME
KKGIATGFSV THPLTGEAVE VWIGNYVLMS YGEGAVMGVP GHDERDFAFA KKYGLPIKQV
IAAEGQTYSL DAWQEWYGDK DAAVCVNSGK YDGLRYTEAV DAVAADLKAG GFGDKQVTWR
LRDWGVSRQR YWGTPIPIIH CPSCGDVPVP EQDLPVVLPE DLVPDGTGNP LAKSEAFLNC
TCPKCGAAAK RETDTMDTFV DSSWYFSRYT APDADTMVDA RTDYWMPMDQ YIGGIEHAIL
HLLYSRFWTK VMRDLGLVKF GEPAKNLLTQ GMVLNETYYR EDATGKKTWY NPADVTVTHD
DKGRPVGATL NADGQPVVLG GIEKMSKSKN NGVDPQVLID QYGADTARLF TMFAAPPEQQ
LEWSGAGVEG ASRFLRRVWS FGAGNREALA ARAGFDAASL GDADKALRRE IYSVLKQADF
DYQRLQYNTV VSAAMKMLNA IDGAKGATPG VLRETYGVLL RVLYPVVPHV TFELWKALGY
ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ VNGKVRGALK VAKDATREAI EVAAVADEAF
AKFSDGKPAK KIVVVPGRLV NIVV