SYL_BRUA4
ID SYL_BRUA4 Reviewed; 877 AA.
AC A6WXW1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
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=Oant_1095;
OS Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=439375;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC 15819 / NCTC 12168 / Alc 37;
RX PubMed=21685287; DOI=10.1128/jb.05335-11;
RA Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA Ugalde R.A., Garcia E., Tolmasky M.E.;
RT "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT pathogen and symbiont of several eukaryotic hosts.";
RL J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS13815.1; -; Genomic_DNA.
DR RefSeq; WP_012091253.1; NC_009667.1.
DR AlphaFoldDB; A6WXW1; -.
DR SMR; A6WXW1; -.
DR STRING; 439375.Oant_1095; -.
DR PRIDE; A6WXW1; -.
DR EnsemblBacteria; ABS13815; ABS13815; Oant_1095.
DR KEGG; oan:Oant_1095; -.
DR PATRIC; fig|439375.7.peg.1145; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; A6WXW1; -.
DR Proteomes; UP000002301; Chromosome 1.
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; Reference proteome.
FT CHAIN 1..877
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009384"
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; 98210 MW; 29A56EA8E314F5F4 CRC64;
MAAERYNPRV AEAHWQKVWE EDRTFETDNS DSREKYYVLE MFPYPSGRIH MGHVRNYAMG
DVVARYKRAK GFNVLHPMGW DAFGMPAENA AMQNKVHPKE WTYQNIATMR SQLKSMGLSL
DWAREFATCD VEYYHRQQML FIDLFEKGLV TRKTSKVNWD PVDNTVLANE QVVDGRGWRS
GALVEQRELT QWFFKITDFS EELLAGLDTL DQWPEKVRLM QRNWIGKSEG LQVRFTLDGK
TAPEGFSEVE VYTTRPDTLF GAAFVGISAD HPLAKKLAEN NASLTGFIEE CHQHGTSLAA
LETAEKKGFD TGVKVKHPFD ENWELPVYVA NFVLMEYGTG AVFGCPAHDQ RDLDFANKYK
LKVTPVVMPK GEDAAGFSIG ETAYTDDGVM INSRFLDGMT PEAAFNEVAN RLEQTSLGNS
PQASRKVQFR LRDWGISRQR YWGCPIPMIH CESCGVNPVP RADLPVKLPD DVEFDRPGNP
LDRHATWRHV KCPKCGADAR RETDTMDTFV DSSWYYARFT APWENEPTDR KVADHWLPVD
QYIGGIEHAI LHLLYSRFFT RAMKVAGHVG IDEPFKGLFT QGMVVHETYK ANGQWVAPAD
IRIEETDGKR SAALLSTGEP VEIGSIEKMS KSKKNVVDPD DIIASYGADT ARWFMLSDSP
PERDVIWTEA GAEGAHRFVQ RVWRLVAEAA EHLKDVAPKT GTQGEALVVS KAAHKAVKAV
GDDIEKLAFN RGVARLYELV NTAAASLQQV ASGNADDELK SAVRDVTEKL ILMLAPMMPH
LAEQCLAVLG GKIAGRETLV ARSAWPEFDP ALVVENEIVM PVQINGKKRG DLTIARDADQ
ASIQQAVLEL DFVKAALNGS SPKKVIVVPQ RIVNVVA