ID   SYL_RHIE6               Reviewed;         876 AA.
AC   B3PS46;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 92.
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=RHECIAT_CH0004409;
OS   Rhizobium etli (strain CIAT 652).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=491916;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CIAT 652;
RX   PubMed=20048063; DOI=10.1128/aem.02039-09;
RA   Gonzalez V., Acosta J.L., Santamaria R.I., Bustos P., Fernandez J.L.,
RA   Hernandez Gonzalez I.L., Diaz R., Flores M., Palacios R., Mora J.,
RA   Davila G.;
RT   "Conserved symbiotic plasmid DNA sequences in the multireplicon pangenomic
RT   structure of Rhizobium etli.";
RL   Appl. Environ. Microbiol. 76:1604-1614(2010).
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; CP001074; ACE93336.1; -; Genomic_DNA.
DR   AlphaFoldDB; B3PS46; -.
DR   SMR; B3PS46; -.
DR   KEGG; rec:RHECIAT_CH0004409; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   Proteomes; UP000008817; 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   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091350"
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;  97751 MW;  486DEF4C54850C8F CRC64;
     MATERYNPRD AEPRWQQKWN EDKVFETDNA DPREKYYVLE MFPYPSGRIH MGHVRNYAMG
     DVVARYKRAR GYNVLHPMGW DAFGMPAENA AMERGVHPAS WTYQNIASMK AQLKAMGLSL
     DWSREFATCD VEYYQHQQHL FLDFLEKGLV YRKQSKVNWD PVDNTVLANE QVIDGRGWRS
     GALVEQRELT QWFFKITDFS QDLLDALDTL DQWPEKVRLM QKNWIGRSEG LTVRWEIVPE
     TAPAGETEIT VYTTRPDTLF GASFLAIAAD HPLAKDAAAK NVEIEAFCEE CRRAGTSLAA
     LETAEKKGLD TGIRVRHPLD PTWELPVYIA NFVLMDYGTG AIFGCPSGDQ RDLDFARKYG
     LPVVAVVMPS DGDAASFAVG DTAYDGDGVM INSRFLDGKT TEEAFNIVAD RLSAASLGNT
     PVAERKVNFR LRDWGISRQR YWGCPIPVIH CDACGVVPVP KTDLPVKLPE DVTFDQPGNP
     LDRHPTWRHV TCPHCGKDAR RETDTMDTFV DSSWYFTRFT APWEAKPTDP EAANRWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMRETGHVA ASEPFKGLFT QGMVVHETYS RKAGAGREWV
     APADIRIEEI DGKRRALLLA TGEEVAIGSI EKMSKSKKNV VDPDDIIASY GADTARFFVL
     SDSPPERDVI WSEAGVEGAH RFTQRLWRLI SEAAGVLSTV AAAPASEGEA LAISQAAHKT
     LKAVQNDYDK LWFNKAVARI YELVNALAAP LTKVAAGEGD IAYRAAVRDA AEILIQLVAP
     MTPHLAEECW ATLGNTGLLA RTGWPRFVEA LVVENDVVLP VQINGKKRAE LTISRDADQN
     AVTDAVLELD AVKNVLNGQA PKKIIVVPQR IVNIVV
//