ID   SYL_MAGSA               Reviewed;         862 AA.
AC   Q2WBE4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JAN-2006, 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=amb0027;
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Magnetospirillum.
OX   NCBI_TaxID=342108;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264;
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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; AP007255; BAE48831.1; -; Genomic_DNA.
DR   RefSeq; WP_011382475.1; NC_007626.1.
DR   AlphaFoldDB; Q2WBE4; -.
DR   SMR; Q2WBE4; -.
DR   STRING; 342108.amb0027; -.
DR   EnsemblBacteria; BAE48831; BAE48831; amb0027.
DR   KEGG; mag:amb0027; -.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000007058; 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..862
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334769"
FT   MOTIF           49..59
FT                   /note="'HIGH' region"
FT   MOTIF           625..629
FT                   /note="'KMSKS' region"
FT   BINDING         628
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   862 AA;  95889 MW;  06D761D800A3D176 CRC64;
     MSRPDGISGD RYNVKETEAR WQQAWEAKRC FEAEIAPGKP KYYVLEMFPY PSGRIHMGHV
     RNYTLGDVVA RYKRAKGFNV LHPMGWDAFG LPAENAAIQN NVHPAKWTRE NIAAMREQLK
     SMGLSYDWRR EVATCEPEYY RHEQKMFLDF LKAGLVYRKE SWVNWDPVEN TVLANEQVID
     GRGWRSGALV EKRLLSQWFL KITAYAQDLL DSLATLERWP ERVRLMQENW IGRSEGARLM
     FDLDGRSDRL EIFTTRPDTL FGAKFVAIAA NHPLAAELAA GNPALAEFVA ECNRMGTSEA
     AIETAEKKGF DTGLRAVHPF DSTWTLPIYV ANFVLMDYGS GAIFGCPAHD QRDLDFANKY
     GLGWTQVVEP ASDGQAVLAA IAKGEAYTGD GVAVNSQFLD GLAVDEAKAE AIRRIEEMGR
     GERTINYRLR DWGVSRQRYW GCPIPVIHCE ACGTVPVPAE QLPVVLPEDV SFDKPGNPLD
     HHPTWKHVDC PCCGKPARRE TDTFDTFFES SWYFARYTSP DRTDVAFDRV AADYWMSVDQ
     YIGGIEHAVL HLLYSRFFTR ALKDCGYLNV KEPFAGLLTQ GMICHETYKS EDGAWLFPTE
     VVPGADGKLV HAETGAPVTG GRSEKMSKSK KNVVDPAGII DGYGADTARL FMLSDSPPER
     DLDWTEAGID GAWRYVNRLW RMVATAELPP AGAPMPELSP EAAKIRRLLH KTIAQVGEDL
     ERFHFNKAVA RIREMTNGLG ELPAGDSGAA WVLREGLEAT ARLIGPMMPH LAEEMWLALG
     GSGLLAEAAW PEADPALLVE DSVTVAVQVN GKLRATIELP KDVDAALAEQ TALAQPQVIS
     AMSGKPARKV VVVPNRIVNV VV