ID   SYL_RHILO               Reviewed;         875 AA.
AC   Q98EU7;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   03-AUG-2022, entry version 115.
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=mll4077;
OS   Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS   (Mesorhizobium loti (strain MAFF 303099)).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=266835;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX   PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA   Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA   Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB50820.1; -; Genomic_DNA.
DR   RefSeq; WP_010912163.1; NC_002678.2.
DR   AlphaFoldDB; Q98EU7; -.
DR   SMR; Q98EU7; -.
DR   STRING; 266835.14024216; -.
DR   PRIDE; Q98EU7; -.
DR   EnsemblBacteria; BAB50820; BAB50820; BAB50820.
DR   KEGG; mlo:mll4077; -.
DR   PATRIC; fig|266835.9.peg.3225; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000000552; 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; 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; 3.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..875
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152070"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           631..635
FT                   /note="'KMSKS' region"
FT   BINDING         634
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   875 AA;  98134 MW;  3A2F64BC5199FF20 CRC64;
     MATERYNPRA SEPKWQKAWA EKKLFEARND DPKPKYYVLE MFPYPSGRIH IGHTRNYTMG
     DVVARYKRAK GFNVLHPMGW DAFGMPAENA AMQNKVHPKE WTYQNIATMR EQLKVMGLSL
     DWAREFATCD VDYYHRQQML FLDFVEKGLV TRKSSKVNWD PEDMTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITDFA QDLLDSLEGL DEWPEKVKLM QQNWIGRSEG LLIRWPLASD
     VAGEHELEVY TTRPDTIFGA SFMAVAADHP LAKKAAETNP ALAKFIDEVR HMGTSVAALE
     TAEKKGFDTG IRVVHPFDDS WTLPVYVANF VLMEYGTGAI FGCPSGDQRD LDFANKYGLP
     VIPVVMPEGG DAKSFQITEE AYVDDGVMIN SRFLDGMKPD RAFDEVAKLL EQKTIGNRPM
     AERKVNFRLR DWGISRQRYW GCPIPMIHCE DCGVVPVPKA DLPVKLPDDV DFDRPGNPLD
     RHPTWRHVKC PQCGRDARRE TDTMDTFVDS SWYFARFTAP WAYEPTDPRA ANEWLPVDQY
     IGGIEHAILH LLYSRFFTRA MRATGHVDLA EPFKGLFTQG MVVHETYRVG GASNNGRWLS
     PAEVRIEDAE GKRRAIEIAT GEEAAIGSLE KMSKSKKNTV SPEDITDGYG ADTARWLMLS
     DSPPEGDVEW TDDGAAGAHR FMQRIWRLVS TAAETLAGVK PAAADSGEAG AVRKATHKIL
     KAVGEDIEKL GFNRAIARIY ELANVLTTPL NQVAEGKADP ALQGACREAV EILVHLIAPV
     MPHLAEECWE TLGGTDLVAE RPWPAFDPAL VVDNEVTYPV QVNGKKRGDL TIARDADQGA
     VEKAVLALDF VQKALEGKAP RKVIIVPQRI VNVVA