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   27-MAR-2024, entry version 119.
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=Daro_0544;
OS   Dechloromonas aromatica (strain RCB).
OC   Bacteria; Pseudomonadota; 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};
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000089; AAZ45301.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q47IN0; -.
DR   SMR; Q47IN0; -.
DR   STRING; 159087.Daro_0544; -.
DR   KEGG; dar:Daro_0544; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OrthoDB; 9810365at2; -.
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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   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.
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
//