ID   SYL_MAGMM               Reviewed;         859 AA.
AC   A0L4R4;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 97.
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=Mmc1_0432;
OS   Magnetococcus marinus (strain ATCC BAA-1437 / JCM 17883 / MC-1).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Magnetococcales;
OC   Magnetococcaceae; Magnetococcus.
OX   NCBI_TaxID=156889;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1437 / JCM 17883 / MC-1;
RX   PubMed=19465526; DOI=10.1128/aem.02874-08;
RA   Schubbe S., Williams T.J., Xie G., Kiss H.E., Brettin T.S., Martinez D.,
RA   Ross C.A., Schuler D., Cox B.L., Nealson K.H., Bazylinski D.A.;
RT   "Complete genome sequence of the chemolithoautotrophic marine magnetotactic
RT   coccus strain MC-1.";
RL   Appl. Environ. Microbiol. 75:4835-4852(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; CP000471; ABK42957.1; -; Genomic_DNA.
DR   RefSeq; WP_011712127.1; NC_008576.1.
DR   AlphaFoldDB; A0L4R4; -.
DR   SMR; A0L4R4; -.
DR   STRING; 156889.Mmc1_0432; -.
DR   EnsemblBacteria; ABK42957; ABK42957; Mmc1_0432.
DR   KEGG; mgm:Mmc1_0432; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002586; 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..859
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000071112"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           614..618
FT                   /note="'KMSKS' region"
FT   BINDING         617
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   859 AA;  96647 MW;  26A931CD311A35D7 CRC64;
     MDQKYNPQAI ESKWQKIWHQ QKTFATPENL GDKETFYLLV MFPYPSGRIH MGHVRNYAIG
     DVIARYQRMQ GKAVLHPMGW DAFGMPAENA AAQRKVHPRD WTYENIATMR EELKSMGLSY
     DWDREFATCD EDYAHAEQVL FLRLYEKGLV YRKHAFVNWD PVDHTVLANE QVIDGCGWRS
     GAPVEQRELN QWFFRITHYA DELLDNLQHM DGWPETVRTM QTNWIGKSHG VEFAFALEGY
     PGTLPVYTTR PDTLMGVTFC SVAAEHPIAA AVAENNPAAA AFIKTCQGVG TSEEALEKLE
     KKGFDTGIKA IHPITGESLP VYIANFVLMS YGTGAVMAVP AHDQRDFEFA KKHGIEIKVV
     IQPEGQTLHA EQLSEAYTGP GRLVNSGLFT GMDNEQAKQR VAEYFEAQGI GKGTINYRLR
     DWGISRQRYW GNPIPMVHCA ACGVVPVPVA QLPIQLPNEV DFSEPGNPLE RHPSWKTCDC
     PQCGQPARRE TDTMDTFMES SWYFLRYCSP HMGGVPLDKA AVDRWMPVNQ YVGGIEHAVL
     HLLYARFFHK ALRDIGEVSC DEPFARLLTQ GMVRKDTHRC AQHGWRYPKE VQERDGALYC
     IECGGAVTVG RNEKMSKSKH NVVDPNDLIA GYGADTARLF MLFAAPADRD LEWNDSGVDG
     AWRFLGRVWR LVLAAIERCG ERQACTTTPA DEQLKAFRSQ LHNTIVKVTE DLNRQSFNTA
     IAAVMEMSNG AIATFKGEDR LTGEASALLW ETAQVTVKLL HPYAPHMTEE LWQRMGEQSL
     LSDTPWPLAD AAALVKERVL IVIQVNGKLR SKLEVPVDMA QEAIEKLALA DEHVKVQTEG
     KTIRKVVVVP GRLVNIVAN