ID   SYL_SINFN               Reviewed;         876 AA.
AC   C3MB60;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=NGR_c33390;
OS   Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX   NCBI_TaxID=394;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 101917 / NGR234;
RX   PubMed=19376903; DOI=10.1128/aem.00515-09;
RA   Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA   Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA   Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA   Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT   "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT   systems.";
RL   Appl. Environ. Microbiol. 75:4035-4045(2009).
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; CP001389; ACP27069.1; -; Genomic_DNA.
DR   RefSeq; WP_012709816.1; NC_012587.1.
DR   RefSeq; YP_002827822.1; NC_012587.1.
DR   AlphaFoldDB; C3MB60; -.
DR   SMR; C3MB60; -.
DR   STRING; 394.NGR_c33390; -.
DR   PRIDE; C3MB60; -.
DR   EnsemblBacteria; ACP27069; ACP27069; NGR_c33390.
DR   KEGG; rhi:NGR_c33390; -.
DR   PATRIC; fig|394.7.peg.6184; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001054; 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; Reference proteome.
FT   CHAIN           1..876
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199220"
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;  97961 MW;  247F386ACAF60FEF CRC64;
     MATERYNPRD TEPRWQQEWD ARKVFETEND DPREKYYVLE MFPYPSGRIH MGHVRNYTMG
     DVVARYKRAR GFNVLHPMGW DAFGMPAENA AMERGVHPAG WTYQNIAAMK AQLKVMGLSL
     DWSREFATCD PAYYQRQQYL FLDFLEKGLV YRRQSKVNWD PVDNTVLANE QVIDGRGWRS
     GALVEQRELT QWFFRITDFS QDLLDALDGL EQWPEKVRLM QKNWIGRSEG LALRWALDPA
     TVPGETKELT VYTTRPDTLF GASFLAISAD HPLAREAAAK DAAIDAFCEE CRRAGTSLAA
     LETAEKKGID TGIRARHPFD PEWELPVYVA NFVLMDYGTG AIFGCPSGDQ RDLDFARKYG
     LSVVPVVMPK DADAATFTIE DEAYGGDGVM INSRFLDGLS TEEAFEAVAS KLEQETLDGA
     PRAERKVNFR LRDWGISRQR YWGCPIPVIH CEDCGVVPVP KADLPVTLPP DVTFDKPGNP
     LDRHPTWRHV ACPQCGKDAR RETDTMDTFV DSSWYYARFT APWEDKPTDP KAANHWLPVD
     QYIGGIEHAI LHLLYSRFFT RAMKATGHVA MDEPFKGLFT QGMVVHETYS RGEGAQREWV
     TPAEIRIDEI DGRRRAVLIE TGEEVAIGSI EKMSKSKKNV VDPDDIIGSY GADTARFFVL
     SDSPPDRDVI WSEAGVEGAH RFVQRVWRLV GEAAESLRGA KASPAKEGEG LAISQAAHRT
     LRAVEADYDK LAFNKAVARI YELVNVLAAP LTQVAAGKAD QAVTAAVKDA TTILIDLIAP
     MMPHLAEECW REIGGEGLIA ERPWPTFDPA LVVENEITLP VQINGKKRAD LTIARDADQS
     AIESAVLALD AVKAALNGAS PRKIIVVPQR IVNVVV