ID   SYL_RHOP5               Reviewed;         888 AA.
AC   Q07UN5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   31-OCT-2006, 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}; OrderedLocusNames=RPE_0390;
OS   Rhodopseudomonas palustris (strain BisA53).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316055;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisA53;
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., Kim E., Harwood C.S., Oda Y.,
RA   Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL   Submitted (SEP-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; CP000463; ABJ04349.1; -; Genomic_DNA.
DR   RefSeq; WP_011661843.1; NC_008435.1.
DR   AlphaFoldDB; Q07UN5; -.
DR   SMR; Q07UN5; -.
DR   STRING; 316055.RPE_0390; -.
DR   EnsemblBacteria; ABJ04349; ABJ04349; RPE_0390.
DR   KEGG; rpe:RPE_0390; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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..888
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009410"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           644..648
FT                   /note="'KMSKS' region"
FT   BINDING         647
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   888 AA;  99417 MW;  FFE5EA905AB360C3 CRC64;
     MTSERYNARE SEPKWQRRWD DDKIFATQND DPRPKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARTMRAR GFNVLHPMGW DAFGLPAENA AIERKVAPKA WTYDNIAAMK KQLQTMGLSL
     DWAREFATCD PSYYKHQQKM FLDFLKAGLA EREKRKINWD PVDMTVLANE QVIDGRGWRS
     GAVVEQREMN QWVFKITRYS QDLLDALDRL DRWPDKVRLM QRNWIGRSEG MLVRFALDAA
     TTPAGESELK IFTTRADTLF GAKFMAIAAD HPLALAAAPK NPKIKDFIDE CKKRGTAQAD
     IDTAEKQGID TGIRAVHPFD PEWKLPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYD
     LGNTPVVCPE GQDPASFVIT DVAYDGDGRL INSRFLDGLS IDQAKEEVAK RLETATRDGA
     PIGERKVNFR LRDWGISRQR YWGCPIPVIH CPKCDVVPVP DADLPVVLPE DVSFDKPGNA
     LDHHPTWKHV TCPKCGGKAV RETDTMDTFV DSSWYFARFT DPWNENAPTT PDVVNKMMPV
     DQYIGGVEHA ILHLLYSRFF TRAMKATGHV GLDEPFAGMF TQGMVVHETY RRKSGEWVSP
     AELDATMTIE SIATDASGEA KTTTKRKVWL RETGEELEIG PIEKMSKSKR NTVDPDDIIG
     TYGADTARWF MLSDSPPDRD VIWSEEGVKG ASRFVQRLWR IANDAAEIAK LAPADRPAEF
     GPDAIAVRKA AHGALHKVLN GIERLAFNVS LAHIREFANA LADSLGKADK PTPDLAFAIR
     EAAIILVQLV APMMPHLAEE CWEVLGQAGL VSEAGWPAVE PALLVEDTIT LPVQVNGKKR
     GDVTVARDAQ NPQIEAAVLA LDTVKQALDG KPVRKIIIVP QRIVNVVV