ID   SYL_DESVM               Reviewed;         834 AA.
AC   B8DJF0;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=DvMF_3090;
OS   Desulfovibrio vulgaris (strain DSM 19637 / Miyazaki F).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=883;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19637 / Miyazaki F;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Hazen T.C.,
RA   Richardson P.;
RT   "Complete sequence of Desulfovibrio vulgaris str. 'Miyazaki F'.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001197; ACL10027.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8DJF0; -.
DR   SMR; B8DJF0; -.
DR   STRING; 883.DvMF_3090; -.
DR   EnsemblBacteria; ACL10027; ACL10027; DvMF_3090.
DR   KEGG; dvm:DvMF_3090; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 2.
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..834
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000199197"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           586..590
FT                   /note="'KMSKS' region"
FT   BINDING         589
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   834 AA;  93505 MW;  F3DE26FD5DD02836 CRC64;
     MKYDHQSIEI KWQRTWEESG AFHCDHHSDK PKYYVLEMFP YPSGNIHMGH VRNYSIGDVV
     ARFKRMQGFN VLHPMGWDAF GLPAENAAIK HGTHPAKWTF SNIDNMRTQL RRLGYSYDWR
     RELATCTPEY YRWEQQFFLR FFEKGLVYRK QAPQNWCPKC HTVLANEQVI EGLCWRCDSA
     VEQKNLTQWF LRITDYAEEL LADLDKLEAG WPERVVSMQR NWIGKSIGAE IVFPLEGPGG
     SGNDDSITVF TTRQDTVFGA TFMSLAPEHP LVEQLIDGKP EAPAVRAFVE RIRNMDRIVR
     QSDDLEKEGV FTGAYCVNPF TGRRMPIWVA NFVLAEYGTG AVMAVPAHDQ RDFEFARKYD
     LPMQVVIQPE GDALDTAAMQ AAWTEAGLLV NSGEFDGLPN EAAKQKIADS LETSGKGRRT
     VNYRLRDWNI SRQRYWGAPI PVVYCDACGV VAEKDENLPV LLPLEVRTHE DGRSPLPDTP
     EFAECACPKC GGKARRETDT MDTFVESSWY FARYTSASKD DGAFDPAALK YWMPVDQYIG
     GVEHAILHLL YSRFFVKALR DCGYMDLDEP FANLLTQGMV LKEGAKMSKS KGNVVDPTEM
     IARYGADTVR LFCLFAAPPE RDFDWSDSGI EGSYRFIGRI WRLAEELSGV LLPVKACSAT
     AADAATPQGK DLRNKEHATV RKAGADISDR FQFNTAIAAV MELVNALYLA KDELSGDEGG
     RKVLSSAVAT VLTLLSPITP HIAEELWASI GNAGRITDEP WPQWSEEALA RDEETIVVQI
     NGKLRGRVSV PAGADAKAIE AAALSEPNVA RHLEDVTVRK VVVIPGKLVN VVVG