SYL_THISH
ID SYL_THISH Reviewed; 817 AA.
AC B8GV13;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 78.
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=Tgr7_2279;
OS Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Thioalkalivibrio.
OX NCBI_TaxID=396588;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-EbGR7;
RX PubMed=21475584; DOI=10.4056/sigs.1483693;
RA Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73359.1; -; Genomic_DNA.
DR RefSeq; WP_012638835.1; NC_011901.1.
DR AlphaFoldDB; B8GV13; -.
DR SMR; B8GV13; -.
DR STRING; 396588.Tgr7_2279; -.
DR EnsemblBacteria; ACL73359; ACL73359; Tgr7_2279.
DR KEGG; tgr:Tgr7_2279; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002383; 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 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; 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; 2.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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; Reference proteome.
FT CHAIN 1..817
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199231"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 817 AA; 91879 MW; 4D8F3A4160C9299D CRC64;
MQEHYEPDAL ERQAQTWWDE HQTFRAREDA PGEPFYCLSM FPYPSGRLHM GHVRNYTIGD
VISRYQRMQG RNVLQPMGWD AFGLPAENAA IKHLVPPAKW TYENIAYMRG QLQRLGFGYD
WDRELATCRP EYYRWEQWLF TRLVKKGLAY KKTAMVNWDP VDQTVLANEQ VIDGKGWRSG
APVERREIPQ WFLRITDYAE ELLKGLDGLE GWPEQVRTMQ RNWIGRSEGV ELEFEVPGEA
PLTVYTTRPD TLMGVSYVGV APEHPLAARA AEGDGKLAAF IEACRHTKVS EADMATLEKK
GMDTGLKAVH PVTGEPVPVW VANFVLMEYG TGAVMAVPAH DQRDWEFARQ YGLPVRQVIL
PAEEGVAVDL DQAAFTDKGV LIESAQFNGL SSAQAFDAIA DFLEKQHKGR RRVNYRLRDW
GVSRQRYWGC PIPIINCPDC GPVPVPEEQL PVVLPEDVAF DGVGSPIKRM PEFIDTTCPE
CGGKAERETD TFDTFFESSW YYARYTCKDA DGAMLDERAR HWLPVDQYIG GIEHAVLHLL
YARFFHKLMR DEGLVDGDEP FTRLLTQGMV LKDGAKMSKS KGNTVDPEAL IERYGADTVR
LFMMFAAPPE LSLEWSDSGV EGAYRFLKRL WKQVHDHVQG GAAPALDKAA LNADQQALRR
KLHQTLAKVS DDIGRRTTFN TAIAACMELM NELGRFEDKS GQGRAVMQEA LETTVLMLSP
IVPHIAHALW SELGREGAAV DQPWPVVDES ALESDTVELV VQVNGKLRAQ IQVPAAAARA
AIEEAALADE NVQRHIEGKT VVKMVVVPGR LVNVVVK