ID   SYL_DESVH               Reviewed;         829 AA.
AC   Q72CT7;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=DVU_1196;
OS   Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS   B-1760 / Hildenborough).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC   Desulfovibrionaceae; Desulfovibrio.
OX   NCBI_TaxID=882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough;
RX   PubMed=15077118; DOI=10.1038/nbt959;
RA   Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA   Kolonay J.F., Eisen J.A., Ward N.L., Methe B.A., Brinkac L.M.,
RA   Daugherty S.C., DeBoy R.T., Dodson R.J., Durkin A.S., Madupu R.,
RA   Nelson W.C., Sullivan S.A., Fouts D.E., Haft D.H., Selengut J.,
RA   Peterson J.D., Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G.,
RA   Hance M., Tran K., Khouri H.M., Gill J., Utterback T.R., Feldblyum T.V.,
RA   Wall J.D., Voordouw G., Fraser C.M.;
RT   "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT   Desulfovibrio vulgaris Hildenborough.";
RL   Nat. Biotechnol. 22:554-559(2004).
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; AE017285; AAS95674.1; -; Genomic_DNA.
DR   RefSeq; WP_010938492.1; NC_002937.3.
DR   RefSeq; YP_010415.1; NC_002937.3.
DR   AlphaFoldDB; Q72CT7; -.
DR   SMR; Q72CT7; -.
DR   IntAct; Q72CT7; 2.
DR   STRING; 882.DVU_1196; -.
DR   PaxDb; Q72CT7; -.
DR   EnsemblBacteria; AAS95674; AAS95674; DVU_1196.
DR   KEGG; dvu:DVU_1196; -.
DR   PATRIC; fig|882.5.peg.1120; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; Q72CT7; -.
DR   Proteomes; UP000002194; 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; 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   PANTHER; PTHR43740; PTHR43740; 2.
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; 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..829
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152011"
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;  93980 MW;  075C5C6BED149142 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
     VIQPQGEALD PATMSAAWTE AGALVNSGAF 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