SYL_PELTS
ID SYL_PELTS Reviewed; 827 AA.
AC A5D416;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
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=PTH_0839;
OS Pelotomaculum thermopropionicum (strain DSM 13744 / JCM 10971 / SI).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Desulfotomaculaceae;
OC Pelotomaculum.
OX NCBI_TaxID=370438;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 13744 / JCM 10971 / SI;
RX PubMed=18218977; DOI=10.1101/gr.7136508;
RA Kosaka T., Kato S., Shimoyama T., Ishii S., Abe T., Watanabe K.;
RT "The genome of Pelotomaculum thermopropionicum reveals niche-associated
RT evolution in anaerobic microbiota.";
RL Genome Res. 18:442-448(2008).
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; AP009389; BAF59020.1; -; Genomic_DNA.
DR AlphaFoldDB; A5D416; -.
DR SMR; A5D416; -.
DR STRING; 370438.PTH_0839; -.
DR PRIDE; A5D416; -.
DR EnsemblBacteria; BAF59020; BAF59020; PTH_0839.
DR KEGG; pth:PTH_0839; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000006556; 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; 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..827
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334789"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 583..587
FT /note="'KMSKS' region"
FT BINDING 586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 827 AA; 94245 MW; 963D6FAEEB49ADC3 CRC64;
MKERYDFKEI EEKWQARWAA QDLYAVPDYS DRPKYYCLEM FPYPSGKLHM GHVRNYSIGD
VVARFKTMQG YHVLHPMGWD AFGLPAENAA IKHGGVHPAE WTLDNIESMR AQLKQLGISY
DWNREVATCH PGYYRWTQWL FLQLFHNGLA YKKKAAVNWC PGCATVLANE QVKDGGCERC
KAPVEKRELE QWFFKITDYA ERLLKDLELL EGWPEKVKIM QENWIGRSEG AEIDFKVEGS
DDIITVYTTR PDTVFGVTYM VLAPEHPLVE KLIAGSKQEA EIKEFIRKVR NLREIDRTST
EAEKVGMPTG AHCINPLTGE KVPVLIANYV LMEYGTGCVM GVPAHDQRDF EFARKYGYPI
RVVIQPPGVE LDPAAMEAAY EEEGFLVNSG PFSGMPNKEA IRAITRHLEE KGRGRFRVTY
RLRDWLISRQ RYWGAPIPII YCDRCGTVPV PESDLPVLLP MDVEFKPTGQ SPLAECPEFV
NAACPSCGGP GKRETDTMDT FMCSSWYYYR YTSPRDNDAP WDRNKVDYWL PVDQYIGGVE
HAILHLLYSR FFTKVLYDLK LVSNLEPFSN LLTQGMVLKD GAKMSKSRGN VVSPEDIVAR
YGADTARLFI LFAAPPERDL EWSDQGVEGC YRFLNRVWRL VMPLAGLLKE APAAVSGKLV
GANREMRRVT HSTIKKVTED ISARFNFNTA VSAIMELVNA LYQFREIPES DRNPAVLREA
VESLLLLLAP FAPHITEELW EATGHRGSIH LQPWPSYDPE AIAEDEITIV VQINGRVRER
LLVPAGITPQ EMQDRVMKEP RVMRMVEGKK VAKVITVPGK LVNIVIK
