SYL_PSESM
ID SYL_PSESM Reviewed; 868 AA.
AC Q87VX3;
DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=PSPTO_4812;
OS Pseudomonas syringae pv. tomato (strain ATCC BAA-871 / DC3000).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=223283;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-871 / DC3000;
RX PubMed=12928499; DOI=10.1073/pnas.1731982100;
RA Buell C.R., Joardar V., Lindeberg M., Selengut J., Paulsen I.T.,
RA Gwinn M.L., Dodson R.J., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA Daugherty S.C., Brinkac L.M., Beanan M.J., Haft D.H., Nelson W.C.,
RA Davidsen T.M., Zafar N., Zhou L., Liu J., Yuan Q., Khouri H.M.,
RA Fedorova N.B., Tran B., Russell D., Berry K.J., Utterback T.R.,
RA Van Aken S.E., Feldblyum T.V., D'Ascenzo M., Deng W.-L., Ramos A.R.,
RA Alfano J.R., Cartinhour S., Chatterjee A.K., Delaney T.P., Lazarowitz S.G.,
RA Martin G.B., Schneider D.J., Tang X., Bender C.L., White O., Fraser C.M.,
RA Collmer A.;
RT "The complete genome sequence of the Arabidopsis and tomato pathogen
RT Pseudomonas syringae pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10181-10186(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE016853; AAO58241.1; -; Genomic_DNA.
DR RefSeq; NP_794546.1; NC_004578.1.
DR RefSeq; WP_011105190.1; NC_004578.1.
DR AlphaFoldDB; Q87VX3; -.
DR SMR; Q87VX3; -.
DR STRING; 223283.PSPTO_4812; -.
DR PRIDE; Q87VX3; -.
DR EnsemblBacteria; AAO58241; AAO58241; PSPTO_4812.
DR GeneID; 1186495; -.
DR KEGG; pst:PSPTO_4812; -.
DR PATRIC; fig|223283.9.peg.4922; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; Q87VX3; -.
DR Proteomes; UP000002515; 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; 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_0000152068"
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; 96968 MW; F1CC07F068D867A4 CRC64;
MHELYQPREI EAAAQTFWDE QKSFEVSEQP GKETFYCLSM FPYPSGKLHM GHVRNYTIGD
VISRYQRMLG KNVLQPLGWD AFGMPAENAA IDNNVAPAKW TYENIAYMKN QLKSLGLAVD
WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP IDQTVLANEQ VIDGRGWRSG
ALIEKREIPM YYFKITAYAD ELLESLDELP GWPEQVKTMQ RNWIGRSRGM EVQFPYDQAS
IGEAGALKVF TTRPDTLMGA TYVAVAAEHP LATLAAQGNP ALQAFIDECK GGSVAEADVA
TQEKKGQPTS LFVEHPLTGE KLPVWVANYV LMHYGDGAVM AVPAHDERDF EFASKYDLPI
KPVVRTSAGD ETPAPWQAEY NEQGPLINSG EFTGLHFQDA FDAIEAALVK KALGQSRTQF
RLRDWGISRQ RYWGCPIPIV HCDTCGDVPV PEDQLPVILP EDVVPDGAGS PLARMPQFYE
CSCPKCGAPA KRETDTMDTF VESSWYYARY ASPHYEGGLV EPNAANHWLP VDQYIGGIEH
AILHLLYARF FHKLMRDEGL VTSNEPFKNL LTQGMVNAET YFRMETSGKK TWINPADVTL
ERDAKAKVIS ATLTSDGLPV EIGGTEKMSK SKKNGIDPQT MIDQYGADTC RLFMMFASPP
DMSLEWSDSG VEGSHRFLRR VWRLAQAHVG QGASGSLDIA ALTDEQKAVR RSIHQAIKQA
SQDIGQNQKF NTAVAQVMTL MNVLEKAPQA TPQDRALLQE GLETVTLLLA PITPHISHEL
WTQLGHNEPV IDAGWPVFDA HALVQDSLQL VIQVNGKLRG HIEMPASASR EEVEAAARIN
ENVLRFTDGL TIRKVIVVPG KLVNIVAS
