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SYL_PSEAE
ID   SYL_PSEAE               Reviewed;         873 AA.
AC   Q9HX33;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=PA3987;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
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; AE004091; AAG07374.1; -; Genomic_DNA.
DR   PIR; E83148; E83148.
DR   RefSeq; NP_252676.1; NC_002516.2.
DR   RefSeq; WP_003100324.1; NZ_QZGE01000001.1.
DR   AlphaFoldDB; Q9HX33; -.
DR   SMR; Q9HX33; -.
DR   STRING; 287.DR97_3878; -.
DR   PaxDb; Q9HX33; -.
DR   PRIDE; Q9HX33; -.
DR   EnsemblBacteria; AAG07374; AAG07374; PA3987.
DR   GeneID; 878925; -.
DR   KEGG; pae:PA3987; -.
DR   PATRIC; fig|208964.12.peg.4180; -.
DR   PseudoCAP; PA3987; -.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   InParanoid; Q9HX33; -.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; Q9HX33; -.
DR   BioCyc; PAER208964:G1FZ6-4061-MON; -.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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..873
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152066"
FT   REGION          624..643
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   873 AA;  97648 MW;  A61D2FDD098E69DB CRC64;
     MHEQYQPLEI ETQAQNYWKE HQSFLVRELP DKEKFYCLSM FPYPSGKLHM GHVRNYTIGD
     VISRYHRMQG RNVLQPMGWD AFGMPAENAA MKNNVAPAAW TYDNIAYMKS QLDSLGLAID
     WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
     ALIEKREIPM YYFKITAYAE ELLESLDNLP GWPEQVKTMQ RNWIGKSRGM EIGFPYDQAS
     IGHAGQLKVF TTRPDTLMGA TYVAVAAEHP LATQAAQNDP QLQAFIDECK RGGVAEADIA
     TQEKKGMATS LFVEHPLTGD KLPVWVANYV LMNYGEGAVM AVPGHDERDF EFANKYGLPI
     RQVIAKVEGD NDFESSVWKE WYGAKDESVL TVNSGKYDNL GYQAAFDAIG ADLEAKGLGQ
     ARTQFRLRDW GISRQRYWGC PIPIIHCEAC GDVPVPADQL PVVLPEDVVP DGSGSPLAKM
     PEFYECNCPK CGQPAKRETD TMDTFVESSW YFARYACPQF EGGMLDRKAA DYWLPVDQYI
     GGIEHAILHL LYARFFHKLM RDEGLVGSDE PFKNLLTQGM VVADTYYRTT ANGGKDWFNP
     ADVEVERDAK AKVVGARLKS DGQPVEIGGT EKMSKSKNNG VDPQSMIDQY GADTCRLFMM
     FASPPDMSLE WSDAGVEGAN RFLRRVWRLA HAHVSAGLPG ALDVAALSDA QKQVRRAIHL
     AIRQASQDVG QHHKFNTAIA AVMTLMNVLE KAPNQDAQDR ALIQEGLETV VLLLAPITPH
     ICHVLWGQLG HAEAVIDARW PSVDESALVQ DTLQLVVQVN GKLRGHIDVA ASASREDVEA
     AARANENVLR FTEGLSIRKV IVVPGKLVNI VAN
 
 
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