ID   SYL_DESVV               Reviewed;         829 AA.
AC   A1VEL2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 105.
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=Dvul_1861;
OS   Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC   Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC   Desulfovibrionaceae; Nitratidesulfovibrio.
OX   NCBI_TaxID=391774;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DP4;
RX   PubMed=19737303; DOI=10.1111/j.1462-2920.2009.01946.x;
RA   Walker C.B., Stolyar S., Chivian D., Pinel N., Gabster J.A., Dehal P.S.,
RA   He Z., Yang Z.K., Yen H.C., Zhou J., Wall J.D., Hazen T.C., Arkin A.P.,
RA   Stahl D.A.;
RT   "Contribution of mobile genetic elements to Desulfovibrio vulgaris genome
RT   plasticity.";
RL   Environ. Microbiol. 11:2244-2252(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; CP000527; ABM28878.1; -; Genomic_DNA.
DR   RefSeq; WP_011792507.1; NC_008751.1.
DR   AlphaFoldDB; A1VEL2; -.
DR   SMR; A1VEL2; -.
DR   KEGG; dvl:Dvul_1861; -.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   Proteomes; UP000009173; 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; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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; 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; 1.
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..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009335"
FT   MOTIF           40..50
FT                   /note="'HIGH' region"
FT   MOTIF           581..585
FT                   /note="'KMSKS' region"
FT   BINDING         584
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   829 AA;  94053 MW;  B8342F1120C5FFF0 CRC64;
     MKYDHQSIET RWQKKWEDSG IFQCDTEADK PKYYVLEMFP YPSGNIHMGH VRNYSIGDVV
     ARFKRMQGFN VLHPMGWDAF GLPAENAAIK NGTHPAKWTF ANIDNMRSQL KRLGYSYDWQ
     REVATCTPEY YRWEQLFFLR FLEKGLVYRK KAAQNWCPKC HTVLANEQVI EGLCWRCDSA
     VEQKELTQWF LRITDYAEEL LADLSKLENG WPERVLSMQR NWIGKSTGAE IRFALDGRDD
     SITVFTTRPD TIFGATFMSI APEHPLVEEL IDGKPQADDV RAFVERIRNM DRIDRQSDTL
     EKEGVFTGAY CVNPFTGRKM PIWVANFVLA EYGTGAVMAV PAHDQRDFEF ARKYDLPMQV
     VIQPQGETLD PATMSAAWTE AGALVNSGNF DGLANEDAKQ RIADDLETTG NGRRTINYRL
     RDWNISRQRY WGAPIPVIYC DACGVVPEKE ENLPVVLPLD VKTHDDGRSP LPHTPAFYEC
     TCPVCGGKAR RETDTMDTFV ESSWYFARYT DATNDKAPFT PDALRYWLPV DQYIGGVEHA
     ILHLLYSRFF TKALRDCGFI ELDEPFANLL TQGMVLMDGS KMSKSKGNVV DPTEMIARYG
     ADTVRLFCLF AAPPERDFDW SESGIEGSYR FVGRVWRLVE ELREHLLAVG ACSSTAEDAK
     TPVARELRLK EHATVRKAGD DLNDRFQFNT AIAAVMELVN ALYLAKDELV ADESGRKVLS
     SAVSTVLTLL SPFTPHLSEE LWALLGHTES VSTLPWPRWK EDALVRDTVT LVVQVNGKLR
     GKLDIPADAS REEVETLALN EPNVLRYLEG VTVRKVVVIP GKLVNVVVS
//