SYL_PSEPK
ID SYL_PSEPK Reviewed; 868 AA.
AC Q88DN1;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 114.
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=PP_4794;
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
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; AE015451; AAN70363.1; -; Genomic_DNA.
DR RefSeq; NP_746899.1; NC_002947.4.
DR RefSeq; WP_010955412.1; NC_002947.4.
DR AlphaFoldDB; Q88DN1; -.
DR SMR; Q88DN1; -.
DR STRING; 160488.PP_4794; -.
DR EnsemblBacteria; AAN70363; AAN70363; PP_4794.
DR KEGG; ppu:PP_4794; -.
DR PATRIC; fig|160488.4.peg.5116; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR PhylomeDB; Q88DN1; -.
DR BioCyc; PPUT160488:G1G01-5131-MON; -.
DR Proteomes; UP000000556; 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 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..868
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152067"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 627..631
FT /note="'KMSKS' region"
FT BINDING 630
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 868 AA; 96698 MW; 0C543398AA3F6FFC CRC64;
MHEQYTPRDI EAAAQKFWDE QQSFAVTEQP GKDTYYCLSM FPYPSGKLHM GHVRNYTIGD
VIARYQRMLG KNVLQPMGWD AFGMPAENAA MKNNVAPAKW TYENIDYMKT QLKSLGLAID
WAREVTTCKP DYYRWEQWLF TRLFEKGIIY RKNGTVNWDP ADQTVLANEQ VIDGRGWRSG
ALIEKREIPM YYFRITDYAD ELLESLDELP GWPEQVKTMQ RNWIGKSRGM EVQFPYDKAS
IGHEGTLKVF TTRPDTLMGA TYVAVAAEHP LATQAAQGNP ALQAFIDECK SGSVAEADMA
TQEKKGMATS LLVEHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFAHKYNLPV
KAVVRTSAGD EVGSEWQAAY GEHGQLINSA EFDGLDFAGA FDAIEAALIR KELGKSRTQF
RLRDWGISRQ RYWGCPIPII HCPSCGDVPV PEDQLPVTLP ENVVPDGAGS PLARMPEFYE
CSCPKCGAAA KRETDTMDTF VESSWYFARY ASPNYDKGLV DPKAANHWLP VDQYIGGIEH
AILHLLYARF FHKLMRDEGL VTSNEPFKNL LTQGMVVAET YYRVASNGGK DWFNPADVEI
ERDAKAKIIG ARLKTDGLPV EIGGTEKMSK SKNNGVDPQS MIEAYGADTC RLFMMFASPP
DMSLEWSDSG VEGASRFLRR VWRLAQAHVS QGLPGKLDVA ALDDAQKVIR RAIHAAIKQA
STDVGQFHKF NTAIAQVMTV MNVLEKAPQA TEQDRALLQE GLEAVTLLLA PITPHISHAL
WQHLGHAGSV IDAAWPSVDE QALVQDSITL VVQVNGKLRG QVEMPAAASR EEVEAAARSN
ENVLRFIDGL TIRKVIVVPG KLVNIVAN
