ID   SYL_LEIXX               Reviewed;         866 AA.
AC   Q6AEW2;
DT   02-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2004, sequence version 1.
DT   27-MAR-2024, entry version 121.
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=Lxx12370;
OS   Leifsonia xyli subsp. xyli (strain CTCB07).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=281090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CTCB07;
RX   PubMed=15305603; DOI=10.1094/mpmi.2004.17.8.827;
RA   Monteiro-Vitorello C.B., Camargo L.E.A., Van Sluys M.A., Kitajima J.P.,
RA   Truffi D., do Amaral A.M., Harakava R., de Oliveira J.C.F., Wood D.,
RA   de Oliveira M.C., Miyaki C.Y., Takita M.A., da Silva A.C.R., Furlan L.R.,
RA   Carraro D.M., Camarotte G., Almeida N.F. Jr., Carrer H., Coutinho L.L.,
RA   El-Dorry H.A., Ferro M.I.T., Gagliardi P.R., Giglioti E., Goldman M.H.S.,
RA   Goldman G.H., Kimura E.T., Ferro E.S., Kuramae E.E., Lemos E.G.M.,
RA   Lemos M.V.F., Mauro S.M.Z., Machado M.A., Marino C.L., Menck C.F.,
RA   Nunes L.R., Oliveira R.C., Pereira G.G., Siqueira W., de Souza A.A.,
RA   Tsai S.M., Zanca A.S., Simpson A.J.G., Brumbley S.M., Setubal J.C.;
RT   "The genome sequence of the Gram-positive sugarcane pathogen Leifsonia xyli
RT   subsp. xyli.";
RL   Mol. Plant Microbe Interact. 17:827-836(2004).
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; AE016822; AAT89083.1; -; Genomic_DNA.
DR   RefSeq; WP_011186079.1; NC_006087.1.
DR   AlphaFoldDB; Q6AEW2; -.
DR   SMR; Q6AEW2; -.
DR   STRING; 281090.Lxx12370; -.
DR   KEGG; lxx:Lxx12370; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_11; -.
DR   Proteomes; UP000001306; 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; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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   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..866
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152034"
FT   REGION          393..421
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           59..69
FT                   /note="'HIGH' region"
FT   MOTIF           628..632
FT                   /note="'KMSKS' region"
FT   BINDING         631
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   866 AA;  96258 MW;  A550EF6D38634B63 CRC64;
     MAHQHDTGTA AAAAGKTAIH YDFAQIQAKW LPVWEKLKPF ATDDPEDNRP RKYVLDMFPY
     PSGDLHMGHA EAYALGDVIA RYWRHQGFSV LHPIGWDAFG LPAENAAIKR GLDPRGWTYD
     NIAQQKASMR RYAPSFDWDR VLQTCDPSYY KWNQWLFLKL YEKGLAYRKA SQVNWCPFDQ
     TVLANEQVVN GRCERCDNLV TKKKLTQWYF RITDYADRLL DDLNQLEGAW PAKVILMQRN
     WIGRSTGADV QFAIEGREEP VAVYTTRPDT LYGVTFMVVA PDSELAAELA EDARPEVKQR
     FEEYLAAVRG TTEMDRLSTE REKTGVFLER HAVNPLTGES IPIWAADYVL SDYGHGAIMA
     VPAHDQRDLD FARAFDLPVR VVVDTTQPAT GAVPVIKTDP QTGEPLLPES APLESPAETG
     QALTGEGRLI NSGPFDGLSK SNAIRRVTEA LQGSGLGAPA KNFRLRDWLI SRQRYWGTPI
     PIVHCEACGE VPVPESELPV LLPPAEGLDL QPKGRSPLGA ASDWVNVSCF SCGGPAQRDT
     DTMDTFVDSS WYFLRFLNPN DDTRAFDPRE AEKWAPVDQY VGGVTHAILH LLYSRFITKV
     LFDQGFVSFT EPFTVLLNQG MVLMDGSAMS KSRGNLVKLS DQLDAHGVDA VRLTMSFAGP
     PEDDIDWADV SPSGSAKFLA RAWRVAHDVT SAPDVVWKSG DPALRRVTHR FLADTPGLVE
     AFKFNVVVAR LMELVNATRK TIDSGAGPAD RAVREAAEVT TMALNLFAPY TAEDMWARLG
     YEPSVSLVPW RKPDPTLLIE EAVTAIVQVD GKVRDRVEVS PKISVDELEA LARSSEAVLR
     SVGDREIVTV IVRAPKLVNI ATRSRS
//