SYL_BURM7
ID SYL_BURM7 Reviewed; 864 AA.
AC A3MPH9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
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=BMA10247_2640;
OS Burkholderia mallei (strain NCTC 10247).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=320389;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10247;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000548; ABO06808.1; -; Genomic_DNA.
DR RefSeq; WP_011832247.1; NZ_CP007802.1.
DR AlphaFoldDB; A3MPH9; -.
DR SMR; A3MPH9; -.
DR KEGG; bmaz:BM44_681; -.
DR KEGG; bmn:BMA10247_2640; -.
DR PATRIC; fig|320389.8.peg.749; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002284; Chromosome I.
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.
FT CHAIN 1..864
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009307"
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; 96207 MW; 78C08D37FEA718FE CRC64;
MHERYVPADV EAAAQSDWRA ADAYRSKEDA NRKKFYCVSM LPYPSGKLHM GHVRNYTIND
VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAQW TYENIAYMKK QMQAMGLAID
WSREVTTCKP DYYKWNQWLF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
AFVEKREIPM YYMRITQYAD ELLNDLDGLG WPERVKVMQH NWIGKSFGVN FGFPYELDGE
KKLLRVFTTR ADTIMGVTFC AIAAEHPLAA RLARDKPALQ AFIDECKRGG VAEADIATME
KKGVATGFSV SHPLTGEPVE VWIGNYVLMS YGEGAVMGVP AHDERDFAFA KKYGLPIRQV
IAVEGETYST DAWQEWYGDK TRAVCVNSGK YDGLAYDAAV DAIAAELKAG GLGDKQITYR
LRDWGISRQR YWGTPIPIIH CPSCGDVPVP EQDLPVVLPE DLVPDGTGNP LAKSDAFLNC
TCPKCGAVAK RETDTMDTFV DSAWYFSRYA APDAQTMVDA RTDYWMPMDQ YIGGIEHAIL
HLLYSRFWAK VMRDLGLVAF GEPAKNLLTQ GMVLNETFYR EDAAGKKTWY NPADVTVSFD
DKGRPVGAVL KSDGQPVELG GIEKMSKSKN NGVDPQMLID HYGADTARLF TMFAAPPEQQ
LEWSGAGVDG ASRFLRRVWA FGFANREALA VRAPFDAAQL AEAGKTLRRE IHGVLKQADF
DYQRLQYNTV VSAAMKMLNA IEGAKGATPA VLRETYGVLL RVLYPVVPHV TFELWKVLGY
ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ VNGKVRGALK VAKDASREAI EAAAVADGMF
AKFAEGRPAK KIIVVPGRLV NVVV
