ID   SYL_CLOB8               Reviewed;         816 AA.
AC   A6M268;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 91.
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=Cbei_4590;
OS   Clostridium beijerinckii (strain ATCC 51743 / NCIMB 8052) (Clostridium
OS   acetobutylicum).
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=290402;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51743 / NCIMB 8052;
RG   US DOE Joint Genome Institute;
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   Sims D., Brettin T., Bruce D., Tapia R., Brainard J., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Bennet G.,
RA   Cann I., Chen J.-S., Contreras A.L., Jones D., Kashket E., Mitchell W.,
RA   Stoddard S., Schwarz W., Qureshi N., Young M., Shi Z., Ezeji T., White B.,
RA   Blaschek H., Richardson P.;
RT   "Complete sequence of Clostridium beijerinckii NCIMB 8052.";
RL   Submitted (JUN-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; CP000721; ABR36698.1; -; Genomic_DNA.
DR   RefSeq; WP_012060745.1; NC_009617.1.
DR   AlphaFoldDB; A6M268; -.
DR   SMR; A6M268; -.
DR   STRING; 290402.Cbei_4590; -.
DR   EnsemblBacteria; ABR36698; ABR36698; Cbei_4590.
DR   KEGG; cbe:Cbei_4590; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000565; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..816
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074828"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   816 AA;  92942 MW;  F6D655DD20488AA7 CRC64;
     MANYGTKIDE KWQKFWDENE VYKFNPENSG KKLYTLEMFS YPSGAQLHAG HWFNYGPTDS
     WARLKRMQGY NVFQPMGFDA FGLPAENYAI KTGIHPQDST LKNIETMEKQ LKSMGAMFNW
     ENEVVTCLPD YYKWTQWLFL KLYEKGLAYR KKAPVNWCPS CNTVLANEQV VDGVCERCST
     EVTKKDLTQW FFKITEYGDE LLDKLDGLDW PEKTKSMQKH WIGRSYGAEV TFKVKDSDLK
     FDVFTTRVDT LNGVTYVVLA PENKLVDELT IPEYKAAVEE YKEAAAKQSE IERQSVSKEK
     TGVFTGSYAI NPINGKVVPI WISDYVLATY GTGCVMAVPA HDERDFAFAT KFNLPIERVI
     TDKENTNPDL PYCEYGVLVN SGKFDGLTTD EAKKKIVEEL EKDELGAMKK NFRLRDWLVS
     RQRYWGAPIP VIYCDDCGIV PVPEKDLPVK LPYNVEFTPD GKSPLGKCED FVNTTCPHCG
     KPAKREADTL DTFVCSSFYY LRYVDNKNDD APFDSEKVNK MLPVDKYVGG PEHACMHLLY
     ARFITKALRD MGYLNFDEPF LSLTHQGLIL GPDGLKMSKS KGNTISPDDY IKEYGADVFR
     MYLMFGFGYT EGGAWSDDGI KSVGKFVDRI ERILENCRNI INSNESTKDS IDSAEKELNF
     WKHNTIKGVT EDGDKMQFNT AIARLMELTN ALNKYTQENI KNANFLKETI VDFIKLLAPF
     APHFAEEQWS LLGNNSTIFN EKWPEFNPAA LVKDEVEIAI QINGKIKAKI MVASNLDEEG
     IKAASLENET IKENTEGKTI VKVIVIKGRL VNIVVK