ID   SYL_BRADU               Reviewed;         874 AA.
AC   Q89WQ1;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 114.
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=blr0627;
OS   Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS   NBRC 14792 / USDA 110).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=224911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX   PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA   Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA   Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT   "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT   Bradyrhizobium japonicum USDA110.";
RL   DNA Res. 9:189-197(2002).
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; BA000040; BAC45892.1; -; Genomic_DNA.
DR   RefSeq; NP_767267.1; NC_004463.1.
DR   RefSeq; WP_011083454.1; NZ_CP011360.1.
DR   AlphaFoldDB; Q89WQ1; -.
DR   SMR; Q89WQ1; -.
DR   STRING; 224911.27348876; -.
DR   PRIDE; Q89WQ1; -.
DR   EnsemblBacteria; BAC45892; BAC45892; BAC45892.
DR   GeneID; 64020489; -.
DR   KEGG; bja:blr0627; -.
DR   PATRIC; fig|224911.44.peg.9167; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   InParanoid; Q89WQ1; -.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; Q89WQ1; -.
DR   Proteomes; UP000002526; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..874
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000151984"
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   874 AA;  97908 MW;  570F8A8F96A3663B CRC64;
     MTSERYNARD SEPRWQAAWD EKAIFVSKND DSRPKYYVLE MFPYPSGRIH IGHVRNYTLG
     DVLARFMRAK GFNVLHPMGW DAFGLPAENA AIERKVAPKA WTYDNIAAMK KQLRSIGLSL
     DWSREIATCD PSYYKHQQKM FLDFLRAGLA EREKRKVNWD PVDMTVLANE QVIDGKGWRS
     GAIVEQREMN QWVFKITKYS QELLSALDTL DRWPDKVRLM QRNWIGRSEG LLVRFALDQA
     TTPAGESELK IFTTRPDTLF GAKFMAISAD HPLATAAAAK DPKLAEFIAE IKKIGTAQEI
     IDTAEKQGFD TGIRAIHPFD PSWKLPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYN
     LGNTPVVCPE GQDPKSFVIT DTAYDGDGRM INSRFLDGMT IEQAKDEVAK RLESELRGNA
     PVGERQVNFR LRDWGISRQR YWGCPIPVIH CPTCDVVPVP DADLPVKLPD DATFDKPGNA
     LDHHPTWKHV TCPQCGGKAQ RETDTMDTFV DSSWYFARFT DPWNENAPTT PAVANRMLPI
     DQYIGGVEHA ILHLLYSRFF TRAMKATGHV ALDEPFAGMF TQGMVVHETY QKADGSYVQP
     AEVKIELGGN GRRATLLTTG EDIQIGAIEK MSKSKKNTVD PDDIIETYGA DVARWFMLSD
     SPPDRDVIWS DERVQGASRF VQRLWRLVND SVELGKAAPA ARPASFGADA TALRKAAHGA
     LDKVTTEIER LHFNVCLAHI REFTNAFSEV LQRPGQPAAD LAWAIREASQ ILVQLFSPMM
     PHLAEECWQV LGQKGLVSEA NWPQIERDLL VEDSVTLVVQ VNGKKRGEVT VATAAQNPEI
     EAAVLALDAV KLALDGKPVR KVIIVPKRIV NVVG