SYL_BRUO2
ID SYL_BRUO2 Reviewed; 877 AA.
AC A5VSE9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 87.
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=BOV_1740;
OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=444178;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512;
RX PubMed=19436743; DOI=10.1371/journal.pone.0005519;
RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M.,
RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T.,
RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S.,
RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.;
RT "Genome degradation in Brucella ovis corresponds with narrowing of its host
RT range and tissue tropism.";
RL PLoS ONE 4:E5519-E5519(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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABQ61550.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000708; ABQ61550.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_002967933.1; NC_009505.1.
DR AlphaFoldDB; A5VSE9; -.
DR SMR; A5VSE9; -.
DR EnsemblBacteria; ABQ61550; ABQ61550; BOV_1740.
DR GeneID; 45125090; -.
DR KEGG; bov:BOV_1740; -.
DR HOGENOM; CLU_004427_0_0_5; -.
DR PhylomeDB; A5VSE9; -.
DR Proteomes; UP000006383; Chromosome I.
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 Gene3D; 3.90.740.10; -; 1.
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; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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..877
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334734"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 628..632
FT /note="'KMSKS' region"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 877 AA; 97863 MW; 56D2AAA6E29FFD95 CRC64;
MAAERYNPRV AEAHWQKVWE ENRTFETDNS DSREKYYVLE MFPYPSGRIH MGHVRNYAMG
DVVARYKRAK GFNVLHPMGW DAFGMPAENA AMQNKVHPKE WTYQNIATMK RQLKSMGLSL
DWSREFATCD VEYYHRQQML FIDLYEKGLV TRKTSKVNWD PVDNTVLANE QVVDGRGWRS
GALVEQRELT QWFFKITDFS EELLAGLDTL DQWPEKVRLM QRNWIGKSEG LQVRFALAAG
TAPAGFSEVE VYTTRPDTLF GAAFVAISAD HPLAKKLSEG NAALSSFIEE CHQQGTSLAA
LETAEKKGFD TGIKVKHPFD DNWELPVYVA NFVLMEYGTG AVFGCPAHDQ RDLDFANKYK
LKVTPVVLPK GEDAASFSIG ETAYTDDGVM INSRFLDGMT PEAAFNEVAS RLEKTDLVGR
PQAVRKVQFR LRDWGISRQR YWGCPIPMIH CESCGVNPVP RADLPVKLPD DVEFDRPGNP
LDRHATWRHV KCPKCGGDAR RETDTMDTFV DSSWYYTRFT APWENEPTDR KAADHWLPVD
QYIGGIEHAI LHLLYSRFFT RAMKVAGHVG VDEPFKGLFT QGMVVHETYK ANGQWVSPAD
IRIEEIDGKR VATMLDSGAP VEIGSIEKMS KSKKNVVDPD DIIASYGADT ARWFVLSDSP
PERDVIWTEA GAEGAHRFVQ RIWRLVAEAA PALKDVAPKA GTQGEALGVS KAAHKAVKAV
GDDIEKLAFN RGVARLYELV NTLSGALQQA ADGKADAEMK GALREATEML VLMTAPMMPH
LAEQCLAELG GKVAGKETLV ARAPWPVFDP ALVVENEIVL PVQINGKKRG DLTIARDADQ
ASIQQAVLEL DFVKAALNGG SPKKIIVVPQ RIVNVVA