ID   SYL_BRASB               Reviewed;         874 AA.
AC   A5E8H4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 93.
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=BBta_0171;
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Bradyrhizobium.
OX   NCBI_TaxID=288000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BTAi1 / ATCC BAA-1182;
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA   Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.-S., Saunders E.,
RA   Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA   Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CP000494; ABQ32468.1; -; Genomic_DNA.
DR   RefSeq; WP_011942689.1; NC_009485.1.
DR   AlphaFoldDB; A5E8H4; -.
DR   SMR; A5E8H4; -.
DR   STRING; 288000.BBta_0171; -.
DR   KEGG; bbt:BBta_0171; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000246; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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..874
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009300"
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;  97492 MW;  5AA7D708047FC63D CRC64;
     MTSERYNARE AEPRWQRQWD EKAIFATKND DPRPKYYVLE MFPYPSGRIH IGHVRNYTLG
     DVLARFMRAK GFNVLHPMGW DAFGLPAENA AIERKVAPKA WTYDNIAAMK KQLRSIGLSL
     DWAREFATCD PSYYKHQQKM FLDFMQAGLV EREQRKVNWD PVDMTVLANE QVIDGRGWRS
     GAVVEQREMN QWVFKITKYS QELLDALDGL DRWPDKVRLM QRNWIGRSEG LLIRFALDPQ
     TTPAGETELK IFTTRPDTLF GAKFMAISAD HPLAQAAAAK NPELAAFIAE IKRIGTAQEA
     IDTAEKQGFD TGIRAVHPFD PSWTLPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYG
     LGNTPVVCPE GQDPASFVIT DTAFDGDGRL INSRFLDGMT IAQAKDEVAK RLEAEQRGGA
     AVGERQVNFR LRDWGISRQR YWGCPIPVIH CPTCDVVPVP AKDLPVVLPD DVTFDKPGNA
     LDHHPTWKHV TCPKCGGKAT RETDTMDTFV DSSWYFARFT DPWNETAPTT PDVANRMMPV
     DQYIGGVEHA ILHLLYSRFF TRAMKATGHV AMDEPFAGMF TQGMVVHETY QKADGTYVNP
     AEVKIEVGGN GRRAVLTATG EDITIGPIEK MSKSKKNTVD PDDIIESYGA DVARWFMLSD
     SPPDRDVIWS DERVQGAARF VQRLWRLVNE SVAAGQEAPS SRPATFGPDA LALRKAAHGA
     LDKVTGGIER LHFNVCLAHI REFANALAEV LARPAKPAPD LAWAIREAAQ ILVQLFSPMM
     PHLAEECWQV LGQGGLISEA SWPQIERDLL VEDSVTLVVQ VNGKKRGEVT VASNAQNPEI
     ESAVLALDAV KLALDGKPVR KVIIVPKRIV NVVG
//