SYL_DESVV
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 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=Dvul_1861;
OS Desulfovibrio vulgaris subsp. vulgaris (strain DP4).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Desulfovibrio.
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 PRIDE; A1VEL2; -.
DR EnsemblBacteria; ABM28878; ABM28878; Dvul_1861.
DR KEGG; dvl:Dvul_1861; -.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
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 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.
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
