ID   SYL_THIDA               Reviewed;         857 AA.
AC   Q3SG58;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 118.
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=Tbd_2445;
OS   Thiobacillus denitrificans (strain ATCC 25259).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Thiobacillaceae; Thiobacillus.
OX   NCBI_TaxID=292415;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25259;
RX   PubMed=16452431; DOI=10.1128/jb.188.4.1473-1488.2006;
RA   Beller H.R., Chain P.S., Letain T.E., Chakicherla A., Larimer F.W.,
RA   Richardson P.M., Coleman M.A., Wood A.P., Kelly D.P.;
RT   "The genome sequence of the obligately chemolithoautotrophic, facultatively
RT   anaerobic bacterium Thiobacillus denitrificans.";
RL   J. Bacteriol. 188:1473-1488(2006).
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; CP000116; AAZ98398.1; -; Genomic_DNA.
DR   RefSeq; WP_011312957.1; NC_007404.1.
DR   AlphaFoldDB; Q3SG58; -.
DR   SMR; Q3SG58; -.
DR   STRING; 292415.Tbd_2445; -.
DR   EnsemblBacteria; AAZ98398; AAZ98398; Tbd_2445.
DR   KEGG; tbd:Tbd_2445; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000008291; 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; 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; Reference proteome.
FT   CHAIN           1..857
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009458"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           620..624
FT                   /note="'KMSKS' region"
FT   BINDING         623
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   857 AA;  94939 MW;  792609177FB4A315 CRC64;
     MQEKYLPSEI ERAGQARWTA DQTYRAADAS DRPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLARYHALRG FNVMQPMGWD AFGLPAENAA IANGVPPAQW TYANIDHMRT QLQALGFAID
     WSRELATCKP DYYRWEQWLF TRLFEKGVIY KKMATVNWDP VDQTVLANEQ VIDGRGWRSG
     ALVEKRDIPM YFFRITQYAD ELLSGLDTLP GWPERVKTMQ ANWIGKSTGV RLAFPYELDG
     SQEKLWVFTT RADTLMGVTF VAVAAEHPLA ARAAENNPEL AAFVAECKQG SVAEADMATM
     EKKGMDTGFK VTHPLTGEEV PVWVGNYVLM SYGEGAVMAV PAHDERDFGF AKKYDLPIKQ
     VIGVDGETFS LDAWAEWYGD KTRGQCVNSG KYDRLGYEAA VDAIAADLAA KGLGEKKTQF
     RLRDWGISRQ RYWGCPIPII HCETCGDVPV PAEQLPVVLP EDVVPDGSGN PLNKRADFVN
     CTCPACGAPA RRETDTMDTF VESSWYYARY ACPDYADGML DARADQWLPV DQYIGGIEHA
     ILHLLYARFF HKLMRDEGLV ASDEPFANLL TQGMVVADTY YREDAGGKKT WFNPADVETK
     DGVATLRADG KPVVVGGTEK MSKSKNNGVD PQALIDQYGA DTARLFTMFA APPEQSLEWS
     DAGVEGAHRF LRRLWKTVYE HVQAGPVVTR AGGALPEPLK ALRRQLHQTI QKVGDDIERR
     KQFNTAIAAV MELMNALAKL DGMDADTRAV RQETLEAVAV LLAPIVPHVG EAIHAELRPG
     AAMRWPEVDA AALVQDEIEL MLQVNGKLRG QIRVAAGADK PAIEAAALAS EAVQKYLAGQ
     TPKKVVVVPG RLVNIVA