ID   SYL_PARD8               Reviewed;         946 AA.
AC   A6LGA2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   27-MAR-2024, entry version 103.
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=BDI_3008;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR44716.1; -; Genomic_DNA.
DR   RefSeq; WP_011967101.1; NC_009615.1.
DR   AlphaFoldDB; A6LGA2; -.
DR   SMR; A6LGA2; -.
DR   STRING; 435591.BDI_3008; -.
DR   PaxDb; 435591-BDI_3008; -.
DR   KEGG; pdi:BDI_3008; -.
DR   PATRIC; fig|435591.13.peg.2967; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   BioCyc; PDIS435591:G1G5A-3085-MONOMER; -.
DR   Proteomes; UP000000566; 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   Gene3D; 3.40.50.620; HUPs; 3.
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; 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; 1.
DR   Pfam; PF13603; tRNA-synt_1_2; 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..946
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009385"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           719..723
FT                   /note="'KMSKS' region"
FT   BINDING         722
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   946 AA;  108495 MW;  735FA3BCA5F4A5AE CRC64;
     MEYNFREIEK KWHDYWIAEK VYKVEKDTNK PKYYVLDMFP YPSGAGLHVG HPLGYIASDI
     YSRFKRLQGF NVLHPMGYDA YGLPAEQYAI QTGQHPEITT KNNIARYREQ LEKIGFCYDW
     SREIRTCDPE YYKWTQWAFI RMFNSYYCND EKQARPISEL IQAFETSGTE GLNVACGEEL
     SFTAEEWKAK SDKEKQEILL NYRIAYRGET MVNWCAALGT VLANDEVVNG VSERGGYPVE
     QKIMRQWCLR VSAYAQRLLD GLDTIDWTDS LKETQKNWIG RSEGAEVRFK VKDSDKEFTI
     FTTRADTMFG VTFMVLAPES ELVQQLTTAD QKAEVDAYLD RTKKRTERER IADRQVTGVF
     SGSYAINPFT GEAVPIWISD YVLAGYGTGA IMAVPAHDSR DYAFAKHFGL EIRPLVEGCD
     VSKESFDAKE GIVCNSPRTG VTPYCDLSLN GLTIKEAIAA TKKYVKDHDL GRVKINYRLR
     DAIFSRQRYW GEPFPVYYDA DSMPQMLPEE CLPLLLPEVD KFLPTETGEP PLGHAVKWAW
     DTVNQKVTEV SKIDNQTIFP LELCTMPGFA GSSAYYLRYM DPHNDKALVA KDVDEYWRNV
     DLYIGGTEHA TGHLIYSRFW NKFLFDLGIV CEEEPFKKLI NQGMIQGRSN FVYRINGTNK
     FVSLNLKDQY EVTPIHVDVN IVSNDLLDIE AFKNWRPEYN DAEFVLEDGK YICGWAVEKM
     SKSMFNVVNP DMIVEKYGAD TLRLYEMFLG PLEQSKPWDT NGIDGVHRFL KKLWGLFFGN
     TDTLQVTDAE PTADELKSLH KLIKKVTFDI EHFSYNTSIS AFMICVNELT SLKCSKRAIL
     EPLITLLAPF APHIAEELWH QLGHDTTICD ARWPKHNEEY LKEKSVVYAI SFNGKARYNL
     ELPADISKED AEKAALNHEN SAKWMEGKTV KKVIVVPGKI VNIVVG
//