SYL_PARP8
ID SYL_PARP8 Reviewed; 864 AA.
AC B2JGX6;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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=Bphy_2588;
OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 /
OS STM815) (Burkholderia phymatum).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=391038;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815;
RX PubMed=25197461; DOI=10.4056/sigs.4861021;
RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R.,
RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D.,
RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M.,
RA Bristow J., Riley M.;
RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host
RT range and efficient nitrogen-fixing symbiont of Mimosa species.";
RL Stand. Genomic Sci. 9:763-774(2014).
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; CP001043; ACC71760.1; -; Genomic_DNA.
DR RefSeq; WP_012401962.1; NZ_CADFGH010000021.1.
DR AlphaFoldDB; B2JGX6; -.
DR SMR; B2JGX6; -.
DR STRING; 391038.Bphy_2588; -.
DR PRIDE; B2JGX6; -.
DR EnsemblBacteria; ACC71760; ACC71760; Bphy_2588.
DR KEGG; bph:Bphy_2588; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001192; 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_1000091300"
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; 96522 MW; 4D68B9ABCB2DFD12 CRC64;
MHEKYVPSDV ESAAQGQWRA TDAYKTTETA DKPKFYCVSM LPYPSGKLHM GHVRNYTIND
VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAKW TYDNIAYMKK QMQSMGLAID
WSREVATCSP DYYKWNQWIF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALVEKREIPM YYMRITQYAD ELLNDLDGLG WPERVKVMQQ NWIGKSFGVN FGFPYELDGE
QKLLRVFTTR ADTIMGVTFC AVAAEHPLAT RLAQGRPDLQ SFIDECKHGG VAEADMATME
KKGMATGFFV THPLTQEKVE VWIGNYVLMS YGEGAVMGVP AHDERDFAFV KKYGIPVKQV
VAVEGETFST DAWQESYGDK ENGVLINSGK YDGLKYGEAV DAIAADLKAL GLGEKQVTWR
LRDWGISRQR YWGTPIPIIH CPSCGDVPVP EKDLPVVLPE DLVPDGTGNP LAKSEAFLNC
TCPTCGAAAK RETDTMDTFV DSSWYFYRYA APDAKTMVDA RTDYWMPMDQ YIGGIEHAIL
HLLYSRFWAK VCRDLGIVKF GEPAKNLLTQ GMVLNETYYR ENDAGKKTWY NPADVTVTHD
DKGRPVGATL NADGQPVVLG GVEKMSKSKN NGVDPQVLID QYGADTARLF TMFAAPPEQQ
LEWSGAGVEG ASRFLRRVWA FGQANETALT ERAPFDAAKL ADTEKTLRRE IYSVLKQADF
DYQRLQYNTV VSAAMKMLNA IEGAKGASAA VLRETYGVLL RVLYPVVPHV TFQLWRELGY
EGEFGSLLDA PWPKVDEKAL EQSEIELVLQ VNGKVRGAVT VAKDASREAI EAVALAHEMF
AKFSEGKPAK KVIVVPGRLV NVVV
