ID SYL_ANOFW Reviewed; 805 AA.
AC B7GK53;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, 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=Aflv_0425;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ32809.1; -; Genomic_DNA.
DR RefSeq; WP_012574132.1; NC_011567.1.
DR AlphaFoldDB; B7GK53; -.
DR SMR; B7GK53; -.
DR STRING; 491915.Aflv_0425; -.
DR GeneID; 7036682; -.
DR KEGG; afl:Aflv_0425; -.
DR PATRIC; fig|491915.6.peg.435; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR Proteomes; UP000000742; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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..805
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199172"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 805 AA; 92398 MW; A208849E5C1DC81C CRC64;
MSFNHREIEK KWQKYWEENK TFKTTEDDGK RKFYALDMFP YPSGAGLHVG HPEGYTATDI
LARMKRMQGY NVLHPMGWDA FGLPAEQYAL DTGNDPAEFT EKNINNFRRQ IKSLGFSYDW
DREVNTTDPN YYKWTQWIFL KLYEKGLAYM DEVPVNWCPA LGTVLANEEV IDGKSERGGH
PVIRKPMKQW MLRITAYADR LLEDLEELDW PESIKEMQRN WIGRSEGANI HFQVDGHDET
FTVFTTRPDT LFGATYAVLA PEHPLVEKIT TPEQKEAVEA YLKQIQSKSD LERTDLAKEK
TGVFTGAYAI NPANGEKLPI WIADYVLMSY GTGAIMAVPA HDERDYEFAK KFNLPIKQVV
AGGDISKEAY TGDGEHINSD FLNGLNKEEA TKKMIEWLEA NGKGEKKVSY RLRDWLFSRQ
RYWGEPIPII HWEDGTMTPV PEEELPLVLP KTDEIKPSGT GESPLANIEE WVSVVDPKTG
KKGRRETNTM PQWAGSCWYY LRYIDPHNDK QLADPEKLEK WLPVDIYIGG AEHAVLHLLY
ARFWHKFLYD IGVVPTKEPF QKLFNQGMIL GENNEKMSKS KGNVVNPDDI VESHGADTLR
LYEMFMGPLE ASIAWSTKGL DGARRFLDRV WRLFVEENGE LNPKIVDNPE TDTLERVYHQ
TVKKVTEDYE ALRFNTAISQ LMVFINEAYK APILPKAYME GFVKLLSPVC PHIAEELWEK
LGYSNTIAYE AWPAYDEAKL VEDEVEIVIQ VNGKVRAKLH VPADATKEQL EQLAMEDEKI
KEQIEGKTVR KVIAVPGKLV NIVAN
//
