ID   SYL_AZOPC               Reviewed;         918 AA.
AC   B6YRS4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-JAN-2009, sequence version 1.
DT   27-MAR-2024, entry version 83.
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=CFPG_633;
OS   Azobacteroides pseudotrichonymphae genomovar. CFP2.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales;
OC   Candidatus Azobacteroides.
OX   NCBI_TaxID=511995;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=19008447; DOI=10.1126/science.1165578;
RA   Hongoh Y., Sharma V.K., Prakash T., Noda S., Toh H., Taylor T.D., Kudo T.,
RA   Sakaki Y., Toyoda A., Hattori M., Ohkuma M.;
RT   "Genome of an endosymbiont coupling N2 fixation to cellulolysis within RT
RT   protist cells in termite gut.";
RL   Science 322:1108-1109(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; AP010656; BAG83896.1; -; Genomic_DNA.
DR   RefSeq; WP_012573656.1; NC_011565.1.
DR   AlphaFoldDB; B6YRS4; -.
DR   SMR; B6YRS4; -.
DR   STRING; 511995.CFPG_633; -.
DR   KEGG; aps:CFPG_633; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000000723; 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; 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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..918
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000091288"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           692..696
FT                   /note="'KMSKS' region"
FT   BINDING         695
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   918 AA;  106760 MW;  708D3B4BAD69121D CRC64;
     MKYDFDAIEK KWQKYWKENR TYQVNIDRNK PKYYVLDMFP YPSGVGLHVG HPLGYIASDI
     YARYKRLKGF NVLHPMGYDA YGLPAEQYAI QTGQHPSITT KENINRYRKQ LDKIGFCFDW
     DREIRTCDPK YYQWTQWVFI QMFNSYYCKE AQRARPITEL VKILENQGTG GLHLACTKEI
     HLTANEWQMK DEKSKQAILM NYRIAYLSDI VVNWCPALGT VLANDEISGG ISIRGGYTVE
     QRKMRQWCLR ISAYAKRLLE GLDKIEWTDS LKKMQRNWIG RSEGVELRFK IKDENIEFMI
     FTTRPETIFG VTFIVIAPES EWLTQTIISK KKDSVDSYLN LVKRRTERER ISNRKVTGVF
     TGSYAVHPIS GETIPIWISD YILADYGTGA VMAVPAHDSR DYAFAKHFDL PIIPLIEDID
     ISKESFDIKE GIMTNSDFLN GLSVKQAIQK VKEYIKDENL GKIKVNYRLR DAIFSRQRYW
     GEPFPIYYKN GIPYAVDEED LPIKLPEIDK FLPAETGKPP LGRAKNWTYK GYPLELTTMP
     GFAGSSAYYL RYEDPHNSEC LVSSEANEYW QNVDLYIGGI EHATGHLIYS RFWNKFLFDL
     GIVAKEEPFK KLINQGMIQG RSNFVYRIKN TNTFVSYGLK HQYDVTPIHV DINLVFDDVL
     NIESFRDWNS EYKNAEFILE NGKYVCGWAI EKMSKSMFNT VSPDNIVNRF GADAFRLYEM
     FLGPLEQSKP WDTKGIDGIA RFLKRLWNLF FENDVLKVSN SLPLDKELKS IHKLIKKVSW
     DIENFSFNTS VAAFMICINE LTLLKCSKHS ILSDLVIVLA PFAPHIAEEL WHLLGNEATI
     FDSQFPKCNE EYLKEENVKY TVSFNGKARF ILNFPKKISE ENVKDTVLKC ESSKKWLKNK
     IPKKIIIIPN KIVNIVFD
//