ID   SYL_RHOPT               Reviewed;         876 AA.
AC   B3Q8A1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   03-AUG-2022, entry version 80.
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=Rpal_0290;
OS   Rhodopseudomonas palustris (strain TIE-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=395960;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TIE-1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D.,
RA   Newman D.K., Roden E., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris TIE-1.";
RL   Submitted (MAY-2008) 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; CP001096; ACE98850.1; -; Genomic_DNA.
DR   RefSeq; WP_012494043.1; NC_011004.1.
DR   AlphaFoldDB; B3Q8A1; -.
DR   SMR; B3Q8A1; -.
DR   EnsemblBacteria; ACE98850; ACE98850; Rpal_0290.
DR   KEGG; rpt:Rpal_0290; -.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   BioCyc; RPAL395960:RPAL_RS01455-MON; -.
DR   Proteomes; UP000001725; 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..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091353"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   876 AA;  97860 MW;  C9E925DFE57421B4 CRC64;
     MSNERYNARE SEPKWQAKWD EAKIFATRND DLRKKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARTMRAR GYNVLHPMGW DAFGLPAENA AIERKIAPKA WTYDNIAAMK KQLQTMGLSL
     DWAREFATCD PSYYKHQQKM FLDFLKVGLV EREKRKLNWD PVDMTVLANE QVIDGRGWRS
     GAVVELREMN QWVFKITKYA QELLDALDTL DRWPDKVRLM QRNWIGRSEG LMVRFALDSA
     TTPAGETELK IFTTRPDTLF GAKFMAIAAD HPLAQAAAAK DPKVAAFIDD CKKRGTAQAE
     IDTAEKQGID TGIRAMHPFD PSWKLPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYQ
     LGNTPVVCPE GQDPASFVIT DTAYDGDGRM INSRFLDGMT IVEAKEEVAK RLETAQLGGA
     PVGERKVNFR LRDWGISRQR YWGCPIPIIH CPTCDVVPVP DADLPVVLPE DVSFDKPGNA
     LDHHPTWKHV TCPKCGGKAV RETDTMDTFV DSSWYFARFT DPWNTEAPTT PDVVNRMMPV
     DQYIGGVEHA ILHLLYSRFF TRAMKAAGHI DIQHDEPFAG LFTQGMVVHE TYRKADGHFA
     SPAEISITVE GDTRRATLLD GGSPVEIGPI EKMSKSKRNT VDPDDIIGTY GADTARWFML
     SDSPPDRDVI WSEEGVKGAS RFVQRLWRMV NDAAPIAASA PAERPASFGA DALTLRKAAH
     GALDKVLSGI ERLAFNVSLA HIREFSNTLG DALARSQTPS PDLAWAIRES TVILVQLFHP
     MMPHLAEECW TVLGQTGLVS EALWPQIEPD LLVEDSITLP VQVNGKKRGE VTVPRDAPTS
     EIEAAVLALD AVKQALGDKP VRKVIVVPQR IVNVVG