ID   SYL_RHOPS               Reviewed;         878 AA.
AC   Q13E15;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 99.
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}; OrderedLocusNames=RPD_0436;
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5;
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   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Pelletier D.A., Kyrpides N., Lykidis A., Oda Y., Harwood C.S.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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; CP000283; ABE37674.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q13E15; -.
DR   SMR; Q13E15; -.
DR   STRING; 316057.RPD_0436; -.
DR   EnsemblBacteria; ABE37674; ABE37674; RPD_0436.
DR   KEGG; rpd:RPD_0436; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; RPAL316057:RPD_RS02240-MON; -.
DR   Proteomes; UP000001818; 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   Gene3D; 3.40.50.620; -; 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   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..878
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009412"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           630..634
FT                   /note="'KMSKS' region"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   878 AA;  97773 MW;  49BF702776813E9F CRC64;
     MSNERYNARE SEPKWQAKWD EAKIFATRND DPRPKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARTMRAR GHNVLHPMGW DAFGLPAENA AIERKVAPKA WTYANIAAMK KQLQTMGLSL
     DWAREFATCD PTYYKHQQKM FLDFLKAGLA ERETRKLNWD PVDMTVLANE QVIDGRGWRS
     GAVVEQREMN QWVFKITRYA QELLDALETL DRWPDKVRLM QRNWIGRSEG LLVRFALDSA
     TTPAGETELK IFTTRPDTLF GAKFMAIAAD HPLAQAAAAK DPKIAAFVED CKKRGTAQAE
     IDTAEKLGID TGIRALHPFD PNWQIPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYQ
     LGNTPVVCPE GQDPSSFVIT DEAYDGDGRL INSRFLDGMS IAEAKEDVAK RLETATLGNA
     PVGERKVNFR LRDWGISRQR YWGCPIPVIH CEVCGVVPVP DKDLPVVLPE DVSFDKPGNA
     LDHHPTWKHT ACPQCGAKAT RETDTMDTFV DSSWYFARFT DPWNENAPTT PDVVNRMLPV
     DQYIGGVEHA ILHLLYSRFF TRAMKATGHV GLDEPFRGMF TQGMVVHETY RKADGMFASP
     AEVAIVAEGD GRRATLLDDG TPIEIGPIEK MSKSKRNTVD PDDIIGSYGA DTARWFMLSD
     SPPDRDVIWS EEGVKGASRF VQRLWRMIND AAEIAKAAPA ARPDAFGPEA LAVRKAAHGA
     LDKVLSGIER LAFNVSLAHI REFSNSLGEA LARPGAASPD VAPDLAWAIR EGAVILVQLF
     HPMMPHLAEE CWAALGQPGL VSEALWPQIE RDLLLEDSIT LPVQVNGKKR GEVTVARDAN
     NPEIEAAVLA LDAVRQALDG KPVRKVIVVP QRIVNVVG