ID   SYL_POLNA               Reviewed;         888 AA.
AC   A1VTV4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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};
GN   OrderedLocusNames=Pnap_3786;
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2;
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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; CP000529; ABM39082.1; -; Genomic_DNA.
DR   RefSeq; WP_011803148.1; NC_008781.1.
DR   AlphaFoldDB; A1VTV4; -.
DR   SMR; A1VTV4; -.
DR   STRING; 365044.Pnap_3786; -.
DR   KEGG; pna:Pnap_3786; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000644; 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; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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   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; 2.
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..888
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009390"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           640..644
FT                   /note="'KMSKS' region"
FT   BINDING         643
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   888 AA;  98298 MW;  FB63D4C5260D8D59 CRC64;
     MQDKYNHLDV ERSAQTHWNA ADAYRVTEDA SRKKYYACSM LPYPSGKLHM GHVRNYTIND
     MLSRYLRMKG YNVLMPMGWD AFGLPAENAA LKNGVPPAQW TYDNIAYMKK QMQAMGLAVD
     WSREIATCDP SYYKWNQWLF LKMLEKGIAY RKTQVVNWDP VDQTVLANEQ VIDGKGWRTG
     ATVEKREIPG YYLKITDYAE ELLGSVQHKL PGWPERVKLM QENWIGKSEG VRFAFLHDIK
     DASGALIGDG QMYVFTTRAD TIMGVTFCAV APEHPLAVHA AASNPALAAF VEECKSGGTT
     EAELATQEKK GQPTGLFVTH PLTGDKVEVW VGNYVLMSYG DGAVMGVPAH DERDFEFAKK
     YGLPIKQVTD VKGQAYSLDA WADWYGDKQH GIAINSGKYD GLAFKAAVDA IAADLAALGL
     GEKKTTWRLR DWGVSRQRYW GTPIPIIHCD EHGAVPVPEK DLPVVLPMDC IPDGSGNPLH
     KHEGFHAGVV CPVCGKPARR ETDTMDTFVD SSWYFMRYCD PKNSEAMVAG GADYWMPMDQ
     YIGGIEHAIL HLLYARFWTK VMRDLGLVKV DEPFTKLLTQ GMVLNHIYSR RTDKGGKEYF
     WPHDVEHVLD DTGKIAGARL KNAVGDLPVG TAIDYEGVGT MSKSKNNGVD PQDIIEKYGA
     DTARLYTMFT APPEATLEWN DAGVEGSYRF LRRVWNFGVK LNAMNSGANG ADAACAKGLF
     DKETKALRLE VHTLLKQVDY DYQRMQYNTV VSGGMKLLNA LEDFKGEISA ASLAALREGF
     SVLLRCLYPA APHLTHALWS ELGYAAEAGD LLDTPWPEVD ASALQQDEIE LMLQINGKLR
     GSVTVPAGAD KAVIEAAALA SEAFVKQAAG APAKKVIVVP GRLVNIVV
//