ID   SYL_CERS5               Reviewed;         873 AA.
AC   A4WXA5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 104.
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=Rsph17025_3135;
OS   Cereibacter sphaeroides (strain ATCC 17025 / ATH 2.4.3) (Rhodobacter
OS   sphaeroides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Cereibacter.
OX   NCBI_TaxID=349102;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17025 / ATH 2.4.3;
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   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Kim E., Richardson P., Mackenzie C., Choudhary M.,
RA   Donohue T.J., Kaplan S.;
RT   "Complete sequence of chromosome of Rhodobacter sphaeroides ATCC 17025.";
RL   Submitted (APR-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; CP000661; ABP72019.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4WXA5; -.
DR   SMR; A4WXA5; -.
DR   STRING; 349102.Rsph17025_3135; -.
DR   KEGG; rsq:Rsph17025_3135; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   BioCyc; RSPH349102:G1G8M-3238-MONOMER; -.
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   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; 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.
FT   CHAIN           1..873
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009415"
FT   MOTIF           41..51
FT                   /note="'HIGH' region"
FT   MOTIF           645..649
FT                   /note="'KMSKS' region"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   873 AA;  97366 MW;  9625CE7AD78EB108 CRC64;
     MSRYDPAATE SRWQAAWDEA GVFTARHDPS RPKYYVLEMF PYPSGRIHMG HVRNYTMGDV
     VARQKAAAGY SVLHPMGWDA FGMPAENAAM ERGGHPKDWT YGNIADMRAQ MKPLGLSIDW
     SREFATCDPE YYGQQQAMFI DMLEAGLIYR KNAVVNWDPV DMTVLANEQV IDGKGWRSNA
     PVERRELTQW FFRISDYAGE LLEALDRLKD WPEKVRLMQA NWIGQSRGLQ FAFSTVNAPE
     GFDRLEVYTT RPDTLLGASF AAISPDHPLA KHLERHDAGV AEFVAECRRV GTSEEALEKA
     EKKGFDTGIR VRHPFDTALE LPVYIANFIL MDYGTGAIFG CPAHDQRDFE FASKYGLPIP
     PVFVAEGTEE APLTEAFVPM KSERVAYVRG FAGAEIQTGE EAVAAAIDFC ESKGVGRGVT
     NYRLRDWGIS RQRYWGCPIP VIHCETCGVV PEAKENLPVR LPDDVTFDVP GNPLDRHPTW
     RDCTCPKCGA KARRETDTMD TFVDSSWYYA RFTAPRATTP TDPEEAEYWM NVDQYIGGIE
     HAILHLLYSR FFARAMQKTG HLPAKAIEPF NALFTQGMVT HEAYYSEEAK QEPVWQGMLE
     PGESPDTQMT VRHITYHFPE EVERTEDGAI LKTTGQKLKV IPSTKMSKSK KNVVDPMNII
     SQFGADTARW FVMSDSPPER DVEWTASGAE AAFKHLGRVW RLADEIARAE GAPTAEDVAL
     DRATAKAIAE VTQGIEGFAF NKAIAKLYEF TNTLSRSGAG AEAKRRAMRT MAQLMSPMVP
     HLAEEVWSML GGEGLVAQAP WPKADPALLV DDMVTLPIQI NGKRRAEVTV PKDMAASEVE
     KLVLADEAVQ RALSGGAPKK LIVVPGRIVN VVI
//