ID   SYL_POLSJ               Reviewed;         886 AA.
AC   Q122Q4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   03-AUG-2022, entry version 100.
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=Bpro_4605;
OS   Polaromonas sp. (strain JS666 / ATCC BAA-500).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas; unclassified Polaromonas.
OX   NCBI_TaxID=296591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS666 / ATCC BAA-500;
RX   PubMed=18723656; DOI=10.1128/aem.00197-08;
RA   Mattes T.E., Alexander A.K., Richardson P.M., Munk A.C., Han C.S.,
RA   Stothard P., Coleman N.V.;
RT   "The genome of Polaromonas sp. strain JS666: insights into the evolution of
RT   a hydrocarbon- and xenobiotic-degrading bacterium, and features of
RT   relevance to biotechnology.";
RL   Appl. Environ. Microbiol. 74:6405-6416(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; CP000316; ABE46488.1; -; Genomic_DNA.
DR   RefSeq; WP_011485475.1; NC_007948.1.
DR   AlphaFoldDB; Q122Q4; -.
DR   SMR; Q122Q4; -.
DR   STRING; 296591.Bpro_4605; -.
DR   EnsemblBacteria; ABE46488; ABE46488; Bpro_4605.
DR   KEGG; pol:Bpro_4605; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001983; 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..886
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009391"
FT   MOTIF           46..56
FT                   /note="'HIGH' region"
FT   MOTIF           638..642
FT                   /note="'KMSKS' region"
FT   BINDING         641
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   886 AA;  98358 MW;  EB01FC528E1BC171 CRC64;
     MQDKYNHLDV ERSAQAQWIA ADAYRVTEDT SGKKPRGKYY ACSMLPYPSG KLHMGHVRNY
     TINDMLTRYL RMKGYNVLMP MGWDAFGLPA ENAAMKNGVP PAQWTYDNIA YMKKQMQAMG
     LAIDWSREVA TCDPSYYKWN QWLFLKMLEK GIAYRKTQVV NWDPVDQTVL ANEQVIDGKG
     WRTGATVEKR EIPGYYLKIT DYAEELLGHV QHQLPGWPER VRLMQENWIG KSEGVRFAFT
     HDIRDASGAL IGGGKMYVFT TRADTIMGVT FCAVAPEHPL ALHAAALNPQ LAAFIEECKA
     GGTTEAELAT QEKKGKPTGL FVTHPLTGEQ VEVWVGNYVL MSYGDGAVMG VPAHDERDFE
     FAKKYGLPIK QVTDVKGQAY SLEAWADWYG DKQQGVAINS DKYDGLGLKA CVDAVAADLA
     AKGLGEKKTT WRLRDWGVSR QRYWGTPIPI IHCDEHGAVP VPEKDLPVVL PQDCVPDGSG
     NPLHRHEGFH AGVVCPVCGK PARRETDTMD TFVDSSWYYM RYCDPKNDQQ MVAGGADYWM
     PMDQYIGGIE HAILHLLYAR FWTKVMRDLG LVKIDEPFTK LLTQGMVLNH IYSRKGDKGG
     IEYFWPSEVE DIHDAAGKVT GAKRKSDGLL VNYEGVGTMS KSKNNGVDPQ DLIERYGADT
     ARLYTMFTAP PEATLEWNDA AVEGSYRFLR RVWNFGVKLS AAKTAAAAAQ AAGFVAEYGK
     EAKELRREIH TVLKQIDYDY QRMQYNTVVS GNMKLLNALE NFTNDGAAGS HKALHESFGI
     LLRCLYPATP HLAHALWSEL GYAAQQGDLL DAPWPEVDSG ALQQDVIELV LQVNGKLRGS
     VTVPAGADKA TIEAAALASE AFLKQAAGAP AKKVIVVPGR LVNIVV