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}; 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
//
