ID   SYL_MOOTA               Reviewed;         829 AA.
AC   Q2RKZ1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 125.
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=Moth_0568;
OS   Moorella thermoacetica (strain ATCC 39073 / JCM 9320).
OC   Bacteria; Bacillota; Clostridia; Moorellales; Moorellaceae; Moorella.
OX   NCBI_TaxID=264732;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39073 / JCM 9320;
RX   PubMed=18631365; DOI=10.1111/j.1462-2920.2008.01679.x;
RA   Pierce E., Xie G., Barabote R.D., Saunders E., Han C.S., Detter J.C.,
RA   Richardson P., Brettin T.S., Das A., Ljungdahl L.G., Ragsdale S.W.;
RT   "The complete genome sequence of Moorella thermoacetica (f. Clostridium
RT   thermoaceticum).";
RL   Environ. Microbiol. 10:2550-2573(2008).
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; CP000232; ABC18898.1; -; Genomic_DNA.
DR   RefSeq; YP_429441.1; NC_007644.1.
DR   AlphaFoldDB; Q2RKZ1; -.
DR   SMR; Q2RKZ1; -.
DR   STRING; 264732.Moth_0568; -.
DR   EnsemblBacteria; ABC18898; ABC18898; Moth_0568.
DR   KEGG; mta:Moth_0568; -.
DR   PATRIC; fig|264732.11.peg.611; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_9; -.
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; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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; 1.
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..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334772"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           582..586
FT                   /note="'KMSKS' region"
FT   BINDING         585
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   829 AA;  94798 MW;  61B06E2164BF6103 CRC64;
     MEARYNFKEI EPKWQRRWEA SDLYRVTEDP DKPKFYCLEM FPYPSGNLHM GHVRNYSIGD
     VVARVKRMRG YNVLHPMGWD AFGLPAENAA IHRGIPPAEW TWSNIANMRR QLHAMGISYD
     WDREVATCHP NYYRWTQWLF LQMYKHGLAY RKKAAVNWCP SCATVLANEQ VVDGACERCH
     TPVMRKDLEQ WFFRITDYAD RLLEDLKKLP GWPDKVKIMQ ENWIGKSSGA EVVFRVEGSG
     EEIPVFTTRP DTLYGVTYLV LAPEHPLVEK LTAGTPYEGP VEEFVQAARY LSALDRTATE
     KEKEGLFTGA YAINPVNNER VPIWIANYVL MEYGTGAVMG VPAHDQRDFE FARKYDLPVK
     VVIRPASSEL PAGELAAAYV EDGIMVNSGP FNGLPNREGI QKVTEYLESI GRGRARVNYR
     LRDWLISRQR YWGAPIPMIY CDQCGIVPVP EEDLPVILPE GVEFRPTGES PLTYCPEFVN
     TTCPRCGGPA RRETDTMDTF VCSSWYFLRY TSPHSQDRAF ERDKVDYWMN VDQYIGGVEH
     AILHLMYARF FTKALHDFGL VGVEEPFQNL LTQGMVLKDG SKMSKSKGNI VSPEEIINRY
     GADTARLFIL FAAPPERDLE WSDQGVEGCY RFLNRVWRLV GSYADAVRRA GGSLEIRSHA
     DRELWRLLHA TIKKVTEDVE ERFNFNTAIS AIMELVNGCY RYQDTVPEEE QNLVLMGEVL
     RKLVTLLAPF APHITEELWQ GLGGQESVHR ESWPQYDPEA LVEEEITLVI QINGKVKDRM
     QVPAGLAREK IEELVLNRDK VAALLAGQQV VKVIVVPDKL VNVVARRAS
//