ID   SYL_SYNAS               Reviewed;         862 AA.
AC   Q2LQK5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
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=SYNAS_01790; ORFNames=SYN_02374;
OS   Syntrophus aciditrophicus (strain SB).
OC   Bacteria; Thermodesulfobacteriota; Syntrophia; Syntrophales; Syntrophaceae;
OC   Syntrophus.
OX   NCBI_TaxID=56780;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SB;
RX   PubMed=17442750; DOI=10.1073/pnas.0610456104;
RA   McInerney M.J., Rohlin L., Mouttaki H., Kim U., Krupp R.S.,
RA   Rios-Hernandez L., Sieber J., Struchtemeyer C.G., Bhattacharyya A.,
RA   Campbell J.W., Gunsalus R.P.;
RT   "The genome of Syntrophus aciditrophicus: life at the thermodynamic limit
RT   of microbial growth.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:7600-7605(2007).
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; CP000252; ABC76058.1; -; Genomic_DNA.
DR   RefSeq; WP_011416093.1; NC_007759.1.
DR   AlphaFoldDB; Q2LQK5; -.
DR   SMR; Q2LQK5; -.
DR   STRING; 56780.SYN_02374; -.
DR   KEGG; sat:SYN_02374; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   InParanoid; Q2LQK5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001933; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 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; 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; Reference proteome.
FT   CHAIN           1..862
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009453"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           614..618
FT                   /note="'KMSKS' region"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   862 AA;  98777 MW;  E81B3D4E8454F1A9 CRC64;
     MNRKYVPQEI EEKWQRYWEE KNTFKVTEDP SKKKYYLLEM FPYPSGKIHI GHVRNYTIGD
     VVARYKRMEG YNVLHPMGWD SFGMPAENAA IERGIHPSLW TNENITHMRK QLKRMGFSYD
     WDREVSTCEP VYYRWEQLFF LWMYEKGLAY KKTSSVNWCP RCQTVLANEQ VEAGLCWRCG
     SEVVEKILDQ WFFRITAYID ELLAGCDRLT GWPERVLTMQ RNWIGKSYGC EVSFPMADGN
     GDIKVFTTRQ DTLFGATFML IAAEHPLVME LIKGKPVEKD ARTFAEEVKK QDKLMRTSDY
     YEKQGLFLDC YCLNPLTGWE MPIFATNFVL ADYGTGCVMA VPTHDQRDFE FAEKFGLRKV
     VVISPPDKTL DPETMTEAYV EEGILVNSGP FNGMENLKAL DAIADHLIAL GRGKRTIQYR
     LRDWGISRQR YWGAPIPMIM CPKCGTVPVP EAELPVVLPR DVDFSGEGGS PLAKHPEFLN
     TTCPSCGGPA KRESDTMDTF VESSWYFERY CCPHFAEKPG LNRQQVDYWM PVDQYIGGIE
     HAILHLLYAR FYTRMLRDFG LVGVDEPFTN LLTQGMVCKE TTRCPDHGYL YPEEVREGRC
     IHCLAEVIVG KTEKMSKSLK NVVDPDYLVR QYGADTARMF CLFAAPPEKD LEWSDQGVEG
     SFRFIGRTWR IVVDYLDDLQ GIAPFAGDGE LEGELKSLRR KTHQTIRKVR DDMGERFHFN
     TAISAIMELV NTLYGLPRPP REDRTALAVI RETIEAIILL LAPIVPHLTE ELWQMLGHQG
     TCLADTPLPV YDPTVAAEDE MTIVIQVNGK VRSRVIVAAD EAEDKIKALA MGDEKVSRFL
     EGKSVIKQVY VPKKLVNIVV KG
//