SYL_SHIB3
ID SYL_SHIB3 Reviewed; 860 AA.
AC B2TU77;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-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};
GN OrderedLocusNames=SbBS512_E0609;
OS Shigella boydii serotype 18 (strain CDC 3083-94 / BS512).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=344609;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CDC 3083-94 / BS512;
RA Rasko D.A., Rosovitz M., Maurelli A.T., Myers G., Seshadri R., Cer R.,
RA Jiang L., Ravel J., Sebastian Y.;
RT "Complete sequence of Shigella boydii serotype 18 strain BS512.";
RL Submitted (MAY-2008) 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; CP001063; ACD09066.1; -; Genomic_DNA.
DR AlphaFoldDB; B2TU77; -.
DR SMR; B2TU77; -.
DR STRING; 344609.SbBS512_E0609; -.
DR EnsemblBacteria; ACD09066; ACD09066; SbBS512_E0609.
DR KEGG; sbc:SbBS512_E0609; -.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000001030; 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 Gene3D; 3.40.50.620; -; 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; 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; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 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..860
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091364"
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 860 AA; 97208 MW; 7DB0BDF4F21F8034 CRC64;
MQEQYRPEEI ESKVQLHWDE KRTFEVTEDE SKEKYYCLSM LPYPSGRLHM GHVRNYTIGD
VIARYQRMLG KNVLQPIGWD AFGLPAEGAA VKNNTAPAPW TYDNIAYMKN QLKMLGFGYD
WSRELATCTP EYYRWEQKFF TELYKKGLVY KKTSAVNWCP NDQTVLANEQ VIDGCCWRCD
TKVERKEIPQ WFIKITAYAD ELLNDLDKLD HWPDTVKSMQ RNWIGRSEGV EITFNVNDYD
NTLTVYTTRP DTFMGCTYLA VAAGHPLAQK AAENNPELAA FIDECRNTKV AEAEMATMEK
KGVDTGFKAV HPLTGEEIPV WAANFVLMEY GTGAVMAVPG HDQRDYEFAS KYGLNIKPVI
LAADGSEPDL SQQALTEKGV LFNSGEFNGL DHEAAFNAIA DKLTAMGVGE RKVNYRLRDW
GVSRQRYWGA PIPMVTLEDG TVMPTPDDQL PVILPEDVVM DGITSPIKAD PEWAKTTVNG
MPALRETDTF DTFMESSWYY ARYTCPEYKE GMLDSEAANY WLPVDIYIGG IEHAIMHLLY
FRFFHKLMRD AGMVNSDEPA KQLLCQGMVL ADAFYYVGEN GERNWVSPVD AIVERDEKGR
IVKAKDAAGH ELVYTGMSKM SKSKNNGIDP QVMVERYGAD TVRLFMMFAS PADMTLEWQE
SGVEGANRFL KRVWKLVYEH TAKGDVAALN VDGLTEDQKA LRRDVHKTIA KVTDDIGRRQ
TFNTAIAAIM ELMNKLAKAP TDGEQDRALM QEALLAVVRM LNPFTPHICF TLWQELKGEG
DIDNAPWPVA DEKAMVEDST LVVVQVNGKV RAKITVPVDA TEEQVRERAG QEHLVAKYLD
GVTVRKVIYV PGKLLNLVVG