ID   SYL_CERS1               Reviewed;         847 AA.
AC   A3PMN4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Rsph17029_2498;
OS   Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Cereibacter.
OX   NCBI_TaxID=349101;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17029 / ATH 2.4.9;
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., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.,
RA   Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL   Submitted (FEB-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; CP000577; ABN77600.1; -; Genomic_DNA.
DR   RefSeq; WP_011841711.1; NC_009049.1.
DR   AlphaFoldDB; A3PMN4; -.
DR   SMR; A3PMN4; -.
DR   EnsemblBacteria; ABN77600; ABN77600; Rsph17029_2498.
DR   GeneID; 57471169; -.
DR   KEGG; rsh:Rsph17029_2498; -.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
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   Gene3D; 3.90.740.10; -; 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; 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; 2.
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..847
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009413"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           619..623
FT                   /note="'KMSKS' region"
FT   BINDING         622
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   847 AA;  94165 MW;  33C63C56B841C53B CRC64;
     MSRYDPAATE SRWQAAWDAA GVFTARHDPA RPKYYVLEMF PYPSGRIHMG HVRNYTMGDV
     VARQKAAAGF SVLHPMGWDA FGMPAENAAM ERGGHPKDWT YGNIADMRAQ MKPLGLSIDW
     SREFATCDPE YYGQQQAMFI DMMEAGLVYR KNAVVNWDPV DMTVLANEQV IDGKGWRSGA
     PVVRRELTQW FFRISDYAGE LLEALDTLKD WPEKVRLMQA NWIGQSRGLQ FAFSMAGAPE
     GFDRLEVYTT RPDTLMGASF AAISPDHPLA RHLERHDAEV AEFVAECRRV GTSEEALEKA
     EKKGFDTGLR VRHPFDTAWE LPVYIANFIL MDYGTGAIFG CPAHDQRDFE FATKYGLPIR
     PVFLPEDTEE TALAEAFVPM KSERVHYIRG FAGAEVQTGE EGVAAAIDFC ESQGVGRGVT
     NYRLRDWGIS RQRYWGCPIP VIHCETCGVV PEAKENLPVR LPDDVSFDVP GNPLDRHPTW
     RDCTCPKCGA KARRETDTMD TFVDSSWYYA RFTAPRAATP TDAEEADYWM NVDQYIGGIE
     HAILHLLYSR FFARAMQKTG HLPAKAIEPF NALFTQGMVT HEIYLTRDAA GRPVYHLPED
     VTDGRLADGT PVEIIPSAKM SKSKKNVVDP MNIIRQFGAD TARWFVMSDS PPERDVEWTA
     SGAEAASKHL HRVWRLADEI SRADGEANAE DGALDKATAR AIAEVTQGVE GFAFNKAIAK
     LYEFTNTLSR SGAGAEAKKR AMRTMAQLMS PMVPHLAEEV WAMLGGEGLV AQAAWPKADP
     ALLIDDTVTL PIQVNGKRRG EITVPKEMAA SEVEKLVLAD EAVQRALGGA APKKLIVVPG
     RIVNVVI