SYL_DECAR
ID SYL_DECAR Reviewed; 870 AA.
AC Q47IN0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 112.
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=Daro_0544;
OS Dechloromonas aromatica (strain RCB).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales; Azonexaceae;
OC Dechloromonas.
OX NCBI_TaxID=159087;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RCB;
RX PubMed=19650930; DOI=10.1186/1471-2164-10-351;
RA Salinero K.K., Keller K., Feil W.S., Feil H., Trong S., Di Bartolo G.,
RA Lapidus A.;
RT "Metabolic analysis of the soil microbe Dechloromonas aromatica str. RCB:
RT indications of a surprisingly complex life-style and cryptic anaerobic
RT pathways for aromatic degradation.";
RL BMC Genomics 10:351-351(2009).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAZ45301.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000089; AAZ45301.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041224677.1; NC_007298.1.
DR AlphaFoldDB; Q47IN0; -.
DR SMR; Q47IN0; -.
DR STRING; 159087.Daro_0544; -.
DR EnsemblBacteria; AAZ45301; AAZ45301; Daro_0544.
DR KEGG; dar:Daro_0544; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OrthoDB; 32262at2; -.
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.
FT CHAIN 1..870
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334747"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 629..633
FT /note="'KMSKS' region"
FT BINDING 632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 870 AA; 96514 MW; 47B018626FEE15DB CRC64;
MQDKYTPADI ERAAQQHWDK TGAARAVEDA TKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
VLSRFHKMQG YNVLQPMGWD AFGMPAENAA LQNNVPPAGW TYSNIDYMRQ QLKSLGFAID
WEREFATCTP EYYRWEQWLF TRLYEKGLVY KKLGTVNWDP VDHTVLANEQ VIDGRGWRSG
ALIEKREIPM YYMKITAYAE ELLSELDNLP GWPEQVRLMQ KNWIGKSTGV RFAFPLADNP
DEKLWVFTTR ADTIMGVTFV AVAAEHPLAT KAAANNPELA AFIEECKKGG VAEADIATME
KKGMPTGIYV THPLTGQQVE VWVGNYVLMS YGDGAVMAVP AHDERDFAFA LKYNLPIKQV
VAVDGETAFS HEAWAEWYAD KAKGKLVNSG KYDGLGYEAA VDAIAADLAA KNLGDKKVQF
RLRDWGISRQ RYWGCPIPII HCKTCGDVPV PDDQLPVVLP ENVEITGAGS PLAKMPEFYE
CQCPKCGGDA RRETDTMDTF FESSWYFLRY ACPDNTTAMV DERVAYWCKG GIDQYIGGIE
HAILHLLYSR FFTKLMRDVG LIGDLGEPFA NLLTQGMVVA PTFYRELDGG KKQWINPADV
DVVTDERGRP TGATLKTDGL PVVIGGTEKM SKSKNNGVDP QALIDQYGAD TARLFIMFAS
PPDQSLEWSD AGVEGAYRFL RRLWKTTYDH LQAGLVAAST SNDGLSSAQA DLRRKLHQTM
GKVADDYGRR KQFNTAIAAV MELLNAYDKC DLKDAAGRAL AQESLESIAL LLFPIVPHIG
QALYAQLRPG ADAGNAAFPK ADPAALKQDE IELMVQVNGK LRGAIRVSAE ADKATIEATA
LANEDAIKFM EGKPAKKVIV VPGRLVNIVA