ID SYL_WIGBR Reviewed; 864 AA.
AC Q8D333;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 27-MAR-2024, entry version 110.
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=WIGBR1680;
OS Wigglesworthia glossinidia brevipalpis.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Wigglesworthia.
OX NCBI_TaxID=36870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12219091; DOI=10.1038/ng986;
RA Akman L., Yamashita A., Watanabe H., Oshima K., Shiba T., Hattori M.,
RA Aksoy S.;
RT "Genome sequence of the endocellular obligate symbiont of tsetse flies,
RT Wigglesworthia glossinidia.";
RL Nat. Genet. 32:402-407(2002).
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; BA000021; BAC24314.1; -; Genomic_DNA.
DR AlphaFoldDB; Q8D333; -.
DR SMR; Q8D333; -.
DR STRING; 36870.gene:10368656; -.
DR KEGG; wbr:leuS; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000000562; Chromosome.
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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_0000152117"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 619..623
FT /note="'KMSKS' region"
FT BINDING 622
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 864 AA; 102169 MW; 62C8A9BD84031F3F CRC64;
MKKEYSCKEI ERFVQKHWEI NDTFKVLEDS KKDKYYCVSM MPYPSGKLHM GHVRNYVLGD
VIARYQRMLG KNVLHPIGWD AFGLPAETAA INNKISPEKW TISSIEYMKN QLKLLGCSYD
WSREIITCDP KYYKWEQLLF TKLYNKNKAY KKKSIVNWCP KDKTVLANEQ VIDNLCWRCS
SNIEMKKIFQ WFIKITDYAD ELLNDLNDLK LWPKKVKVMQ RNWIGKSKGI DVLFHIKDTN
EKILIYVSKL EIFMGITFIV ISKEHKLIKF IENKLPSIAK LIKNYNNEKT LELNLRKKTK
DGIFTSLFAI HPISKKILPI WISNFFFTNN DIYQSIAAIP AYNKNELDFA KKYNLPIRYV
IKDYFEKIID FKKYNNLKEG ILFNSNIFNG LNLKNGYDRI SKFLISNKIG KRSTHYKLRD
WCISRQRYWG APIPVLITKE NKILVVSENE LPVILPKAKN NNIIHSLNSY KDWIYVLNDN
KLVKREVDTF DTFMESSWYL HRYTCTKYTK DILDPNATNY WFPVDQYIGG IEHATMHLLY
LRFYHKILRD MNFVKCDEPV NRLLCQGMVL SDTFYYFSKS GNKIWTSPKN KNFERNKDNK
IINAIDSLGN KLTHIGMSKM SKSKNNGVDP QGIINKYGSD TLRLFIMFAA PPELSLEWSD
KGIIGANRFI KKLWKITYNY LNLKKNNNYV FYKKLKEQDN ILLEKSFYVI NKVTKDIDKN
QTFNTAIAEI MKLTNHLNSY INKNEYNNIS IIKKVLMIII RLLYPFIPHV CFVLWNEINK
NNDIDKTKWP KIKMPFIKNK KKNIVVQING KLKTVISFDI SCNEFLIKKC VIENNKIKNL
LNKKKIKNII YVKNKIINIV LDDK
//
