ID   SYL_POLAQ               Reviewed;         890 AA.
AC   A4SVD9;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 94.
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=Pnuc_0232;
OS   Polynucleobacter asymbioticus (strain DSM 18221 / CIP 109841 /
OS   QLW-P1DMWA-1) (Polynucleobacter necessarius subsp. asymbioticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Polynucleobacter.
OX   NCBI_TaxID=312153;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18221 / CIP 109841 / QLW-P1DMWA-1;
RX   PubMed=22675600; DOI=10.4056/sigs.2395367;
RA   Meincke L., Copeland A., Lapidus A., Lucas S., Berry K.W., Del Rio T.G.,
RA   Hammon N., Dalin E., Tice H., Pitluck S., Richardson P., Bruce D.,
RA   Goodwin L., Han C., Tapia R., Detter J.C., Schmutz J., Brettin T.,
RA   Larimer F., Land M., Hauser L., Kyrpides N.C., Ivanova N., Goker M.,
RA   Woyke T., Wu Q.L., Pockl M., Hahn M.W., Klenk H.P.;
RT   "Complete genome sequence of Polynucleobacter necessarius subsp.
RT   asymbioticus type strain (QLW-P1DMWA-1(T)).";
RL   Stand. Genomic Sci. 6:74-83(2012).
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; CP000655; ABP33453.1; -; Genomic_DNA.
DR   RefSeq; WP_011902078.1; NC_009379.1.
DR   AlphaFoldDB; A4SVD9; -.
DR   SMR; A4SVD9; -.
DR   STRING; 312153.Pnuc_0232; -.
DR   EnsemblBacteria; ABP33453; ABP33453; Pnuc_0232.
DR   GeneID; 31480582; -.
DR   KEGG; pnu:Pnuc_0232; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000231; 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   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.
FT   CHAIN           1..890
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074838"
FT   MOTIF           48..58
FT                   /note="'HIGH' region"
FT   MOTIF           645..649
FT                   /note="'KMSKS' region"
FT   BINDING         648
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   890 AA;  99554 MW;  B9ED38A7A3BF2954 CRC64;
     MSKDYDHRGI EAAAQADWER TQVYRVTENA VNASGKKKPK YYACSMLPYP SGKLHMGHVR
     NYTINDVMAR QLRMQGYNVL MPMGWDAFGM PAENAAIQNK VPPAKWTYDN IAYMKKQMAA
     MGLAIDWSRE VATCSPDYYR WNQWLFLKML EKGVAYRKTQ VVNWDPIDQT VLANEQVIDG
     RGWRSGALVE KREIPGYYFN ITAYAEQLLS GLDGLGWPER VKTMQQNWIG KSRGVRFAFK
     HEIADAHGNF IQDGLLYVFT TRADTIMGVT FCAVAAEHPL ASKAAENNPT LAAFIEKCKT
     GSVIEADLAT QEKEGMFTGL YVTHPLTNES VPVWVGNYVL MSYGDGAVMG VPAHDERDFA
     FALKYELPIK QVIALKDESP MFNGTHWQDW YAQKENVVCF NSGKFDGLSH EEAVNTVASD
     LEKMGIGELK TTYRLRDWGI SRQRYWGTPI PIIHCGDEGN PGCGAVPVPE ADLPVVLPED
     CVPDGSGNPL NKRADFLNVK CPQCGKPARR ETDTMDTFVD SSWYFMRYTG PDATSMVDGR
     NEYWMPMDQY IGGIEHAILH LLYARFWTKV MRDLDLITFD EPFQNLLTQG MVLNETYYSE
     EASGKKTWLN PLDVELDLDE KGRPQGAKLK GDSSGTPVII GGVEKMSKSK NNGVDPQALI
     DQYGADTARL FVMFAAPPEQ QLEWSGAGVD GASRFLRRVW MYSSSQASAI KDAQDALPST
     LNDAEKELRR EVHAILKQAN FDYQRRQYNT VVSAAMKMLN VLEPIKLGQD SPISASVLRE
     CLSILLRVLY PVVPHLTHVL WKDMGYSENF GSLLDAPWPT VDETALIQTE ITLMLQINGK
     LRGELKVPAD ASKEQIEAIA LQSEPATKAL NGGAPKKVIV VPGRLINIVA