SYL_BLOFL
ID SYL_BLOFL Reviewed; 867 AA.
AC Q7VRA6;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=Bfl313;
OS Blochmannia floridanus.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX NCBI_TaxID=203907;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA Latorre A., Rausell C., Kamerbeek J., Gadau J., Hoelldobler B.,
RA van Ham R.C.H.J., Gross R., Moya A.;
RT "The genome sequence of Blochmannia floridanus: comparative analysis of
RT reduced genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
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; BX248583; CAD83383.1; -; Genomic_DNA.
DR RefSeq; WP_011126591.1; NC_005061.1.
DR AlphaFoldDB; Q7VRA6; -.
DR SMR; Q7VRA6; -.
DR STRING; 203907.Bfl313; -.
DR EnsemblBacteria; CAD83383; CAD83383; Bfl313.
DR KEGG; bfl:Bfl313; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002192; 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; 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; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 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..867
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000151994"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 625..629
FT /note="'KMSKS' region"
FT BINDING 628
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 867 AA; 101320 MW; B8A6FB76B78356C9 CRC64;
MKKLYFPHQI ERIVQQHWND NQTFSVTEDK NKQKFYCLSM LPYPSGNLHM GHVRNYTIGD
VISRYQRMLG KNVLQPIGWD AFGLPAEQAA IIHKKNPSDW TYSNIQYMKQ QLKSLGFAYD
WKRELITNDP QYYRWEQWFF IILYEKGLVY RKTTLVNWCP YHNTVLANEQ VINGGCWRCH
TKIQYKKIPQ WFIKITHYAD QLLNGLNQLQ YWPEQVKTMQ RNWIGQSTGT NVIFKILNSN
ITTITVYIAR LDTFMGISYL TISVDHPITL QIAKINPDLA NFISIYNTIS IQLHNKQFIC
HKKKGIFTNL YAVHPITFTK LPIWVANFIT PLEFDGQGAI ASCPAHDQHD WEFAHQYDLP
IKPVIKYADG ELPNITNQAM IEPGILFNSD NFDDLTSHTA INYISKKLID LKIAKTKIFY
HLQDWGVSRQ RYWGVPIPMI KLKNGIIQPV PKSELPVILP EIIYTKNNEN NILSKNFNWT
HTTYKNQDVI RDTDTFDTFM ESSWYYARYT CPHYHDGMLQ SDAANYWLPI DQYIGGIEHA
TMHLMYFRFY HKLMRDIGLI QSNEPAIRLL CQGMILADSF YYISNDGQKN WVSPNKVIST
RDKMGHIIKS IDADGNNVIY AGLCKMSKSK NNGIDPNAMI QKYGADAVRF FIMFAAPAHS
TLEWKESGIE GALRFLKRLW NITYQHIQNG LIHQLNMYKL ENKHKIIRQK VHETIIKVTD
DIDRRQSFNT ALAAIMKLFN DIQDIFPINN TQDRSVLHEA LSIIVKLLYP FTPHISYILW
KELGYTNTID DTTWPTPDLQ AIQTQEILII VQINGKKKKK IFVPINSDKN TIHEIAKQAI
YQDKNLESKY VHKIIYIPNK IINFITK