SYL_BACFR
ID SYL_BACFR Reviewed; 943 AA.
AC Q64MG4;
DT 01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-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=BF4586;
OS Bacteroides fragilis (strain YCH46).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=295405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YCH46;
RX PubMed=15466707; DOI=10.1073/pnas.0404172101;
RA Kuwahara T., Yamashita A., Hirakawa H., Nakayama H., Toh H., Okada N.,
RA Kuhara S., Hattori M., Hayashi T., Ohnishi Y.;
RT "Genomic analysis of Bacteroides fragilis reveals extensive DNA inversions
RT regulating cell surface adaptation.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14919-14924(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; AP006841; BAD51323.1; -; Genomic_DNA.
DR RefSeq; WP_011203753.1; NC_006347.1.
DR RefSeq; YP_101857.1; NC_006347.1.
DR AlphaFoldDB; Q64MG4; -.
DR SMR; Q64MG4; -.
DR STRING; 295405.BF4586; -.
DR EnsemblBacteria; BAD51323; BAD51323; BF4586.
DR KEGG; bfr:BF4586; -.
DR PATRIC; fig|295405.11.peg.4410; -.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002197; 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; -; 3.
DR HAMAP; MF_00049_B; Leu_tRNA_synth_B; 1.
DR InterPro; IPR001412; aa-tRNA-synth_I_CS.
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; 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..943
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000151968"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 717..721
FT /note="'KMSKS' region"
FT BINDING 720
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 943 AA; 107969 MW; 9F9A3355FAA30082 CRC64;
MEYNFREIEK KWQKIWVDNH TYQVNEDASK QKFYVLNMFP YPSGAGLHVG HPLGYIASDI
YARYKRLQGF NVLNPMGYDA YGLPAEQYAI QTGQHPAITT VNNINRYREQ LDKIGFSFDW
NREIRTCDPE YYHWTQWAFI KMFNSYYCND EKQARPIEEL IEAFSTNGTQ GMNVACGEEM
DFTADEWNAK SEKEQQEILM NYRIAYLGNT MVNWCPALGT VLANDEVVDG VSERGGYPVI
QKVMRQWCLR VSAYAQRLLD GLETVEWTDS LKETQRNWIG RSEGAEMNFK VKDSDIEFTI
FTTRADTVFG VTFMVLAPES ELVAKLTTPE QKAEVDAYLD RTKKRTERER IADRSVSGVF
SGSYAINPLT NEPIPVWISD YVLAGYGTGA IMAVPAHDSR DYAFAKHFNL EIRPLIEGCD
VSEESFDAKE GIMMNSPRPG APEGGLVLNG LTVKEAIAKT KEYIKATGLG RVKVNFRLRD
AIFSRQRYWG EPFPVYYKDG MPYMIDESCL PLELPEVAKF LPTETGEPPL GHATKWAWDT
VNKCVTDNEN IDNRTIFPLE LNTMPGFAGS SAYYLRYMDP RNHEALVSPA VDQYWKNVDL
YVGGTEHATG HLIYSRFWNK FLHDWGISVA EEPFQKLVNQ GMIQGRSNFV YRIKDTNTFV
SLNLKDQYEV TPIHVDVNIV SNDILDLEAF KAWRPEYETA EFILEDGKYI CGWAVEKMSK
SMFNVVNPDM IVEKYGADTL RMYEMFLGPV EQSKPWDTNG IDGVHRFIKK FWSLFYDRNG
EYLVKDEPAT KEELKALHKL IKKVTGDIEQ FSYNTSVSAF MICVNELSSL KCNKKEVLEQ
LIVVLAPFAP HVCEELWDTL GNTTSVCDAQ WPTFNEQYLV EDTVNYTISF NGKARFNMEF
PADAASDAIQ ATVLADERSL KWTEGKTPKK VIVVPKKIVN IVI
