ID   SYL_CALS8               Reviewed;         817 AA.
AC   A4XKG9;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=Csac_1819;
OS   Caldicellulosiruptor saccharolyticus (strain ATCC 43494 / DSM 8903 / Tp8T
OS   6331).
OC   Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacterales Family III. Incertae Sedis; Caldicellulosiruptor.
OX   NCBI_TaxID=351627;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43494 / DSM 8903 / Tp8T 6331;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Kiss H., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., van de Werken H.J.G., Verhaart M.R.A.,
RA   VanFossen A.L., Lewis D.L., Nichols J.D., Goorissen H.P., van Niel E.W.J.,
RA   Stams F.J.M., Willquist K.U., Ward D.E., van der Oost J., Kelly R.M.,
RA   Kengen S.M.W., Richardson P.;
RT   "Genome sequence of the thermophilic hydrogen-producing bacterium
RT   Caldicellulosiruptor saccharolyticus DSM 8903.";
RL   Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000679; ABP67404.1; -; Genomic_DNA.
DR   RefSeq; WP_011917338.1; NC_009437.1.
DR   AlphaFoldDB; A4XKG9; -.
DR   SMR; A4XKG9; -.
DR   STRING; 351627.Csac_1819; -.
DR   PRIDE; A4XKG9; -.
DR   EnsemblBacteria; ABP67404; ABP67404; Csac_1819.
DR   KEGG; csc:Csac_1819; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000256; 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; 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; 1.
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..817
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009315"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           578..582
FT                   /note="'KMSKS' region"
FT   BINDING         581
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   817 AA;  95200 MW;  01C44C1BC39859F1 CRC64;
     MEYNFREIEK KWQQKWFSQN KYKVTEDSPK PKYYVLEMFP YPSGKLHMGH VRNYSIGDVF
     ARFMRLKGYN VLHPMGWDAF GLPAENAAIK HGIHPSDWTW SNIENMKRQL KELGISYDWD
     REVATCHPDY YKWTQWMFLQ FYKAGLAYRK RSYVNWCPSC ETVLANEQVV NGRCERCKSL
     VGKKDLEQWF FRITKYAERL LRDIDKLDGW PEKVKIMQKN WIGRSEGAEI EFEIDGLGKR
     IKVFTTRPDT LFGVTYLVLA PEHPLTKEII AGKPQEKECL EFIEKMQYLN EIERTSTETE
     KEGRFTGGYA IHPLTGKKVP IYIANYVLVD YGTGAVMGVP AHDQRDFEFA KKYNLPIKVV
     IKGDGVDIQN LQSAYEGEGV LINSGEFNGL KNTEAMKKIT EYLEKNGYGK ACVTYKLRDW
     LISRQRYWGA PIPIVYCDDC GIVPVPEEEL PVLLPYNVEF KPTGQSPLAY CEEFVNTTCP
     KCGKPARRET DTMDTFICSS WYYFRYTDPK NSEKPFEKSL VDYWLPVDQY IGGVEHAILH
     LLYSRFFTKV LYDLGYISFE EPFKNLLTQG MVLKDGAKMS KSLGNIVSPE EIVEKYGADT
     ARLFILFAAP PERDLEWSDQ GVEGCFRFLN RLWRLYIELK DKLSDSSLPG QSELDDELNY
     RLNYTIKKVT EDIGERFNFN TAISSIMELL NFLYDYKEKG SLNRELILKT LKNFLILIYP
     FTPHIACELW EIMGFEGDIE DVSWPEYDES ALVRKNVEIA VQINGKVRAR FDVPVDISEE
     ELKQKIMNNE KIKTLLEGKE IVKFIYVKNR LVNIVIK