SYL_BURPS
ID SYL_BURPS Reviewed; 864 AA.
AC Q63QT6;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=BPSL2938;
OS Burkholderia pseudomallei (strain K96243).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=272560;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K96243;
RX PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT pseudomallei.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
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; BX571965; CAH36948.1; -; Genomic_DNA.
DR RefSeq; WP_004535294.1; NZ_CP009538.1.
DR RefSeq; YP_109532.1; NC_006350.1.
DR AlphaFoldDB; Q63QT6; -.
DR SMR; Q63QT6; -.
DR STRING; 272560.BPSL2938; -.
DR EnsemblBacteria; CAH36948; CAH36948; BPSL2938.
DR GeneID; 56528259; -.
DR KEGG; bps:BPSL2938; -.
DR PATRIC; fig|272560.51.peg.2342; -.
DR eggNOG; COG0495; Bacteria.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000000605; 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_0000151991"
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; 96151 MW; C389C7051142A655 CRC64;
MHERYVPADV EAAAQSDWRA ADAYRSKEDA NRKKFYCVSM LPYPSGKLHM GHVRNYTIND
VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAQW TYENIAYMKK QMQSMGLAID
WSREVTTCKP DYYKWNQWLF LKMLEKGVAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALVEKREIPM YYMRITQYAD ELLNDLDGLG WPERVKVMQH NWIGKSFGVN FGFPYELDGE
KKLLRVFTTR ADTIMGVTFC AIAAEHPLAA RLARDKPALQ AFIDECKRGG VAEADIATME
KKGVATGFSV SHPLTGEPVE VWIGNYVLMS YGEGAVMGVP AHDERDFAFA KKYGLPIRQV
IAVEGETYST DAWQEWYGDK TRAVCVNSGK YDGLAHDAAV DAIAAELKAG GLGDKQITYR
LRDWGISRQR YWGTPIPIIH CPSCGDVPVP EQDLPVVLPE DLVPDGTGNP LAKSDAFLNC
TCPKCGAAAK RETDTMDTFV DSAWYFSRYA APDAQTMVDA RTDYWMPMDQ YIGGIEHAIL
HLLYSRFWAK VMRDLGLVAF GEPAKNLLTQ GMVLNETFYR EDAAGKKTWY NPADVTVSFD
DKGRPVGAVL KSDGQPVELG GIEKMSKSKN NGVDPQMLID HYGADTARLF TMFAAPPEQQ
LEWSGAGVDG ASRFLRRVWA FGFANREALA VRAPFDAAQL AEADKTLRRE IHGVLKQADF
DYQRLQYNTV VSAAMKMLNA IEGAKGATPA VLRETYGVLL RVLYPVVPHV TFELWKALGY
ADEFGPLLDA PWPKVDEAAL EQAEIELVLQ VNGKVRGALK VAKDASREAI EAAAVADGMF
AKFAEGRPAK KIIVVPGRLV NVVV
