ID   SYL_CHLCH               Reviewed;         805 AA.
AC   Q3APY5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=Cag_1688;
OS   Chlorobium chlorochromatii (strain CaD3).
OC   Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC   Chlorobium/Pelodictyon group; Chlorobium.
OX   NCBI_TaxID=340177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CaD3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Bryant D., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Chlorobium chlorochromatii CaD3.";
RL   Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
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; CP000108; ABB28940.1; -; Genomic_DNA.
DR   RefSeq; WP_011362702.1; NC_007514.1.
DR   AlphaFoldDB; Q3APY5; -.
DR   SMR; Q3APY5; -.
DR   STRING; 340177.Cag_1688; -.
DR   EnsemblBacteria; ABB28940; ABB28940; Cag_1688.
DR   KEGG; cch:Cag_1688; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_10; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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   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; 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; 2.
DR   Pfam; PF08264; Anticodon_1; 1.
DR   Pfam; PF00133; tRNA-synt_1; 1.
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.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Nucleotide-binding; Protein biosynthesis.
FT   CHAIN           1..805
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009320"
FT   MOTIF           40..51
FT                   /note="'HIGH' region"
FT   MOTIF           576..580
FT                   /note="'KMSKS' region"
FT   BINDING         579
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   805 AA;  92007 MW;  A0C78B83732AF54C CRC64;
     MKYDFTSIEK KWQTRWQAEA TFATGTDHSK PKYYVLDMFP YPSGSGLHVG HLEGYTASDI
     IARYKRSSGY NVLHPMGWDA FGLPAEQFAI KTGTHPRITT EANVKNFKGT LQAMGFSYDW
     EREINTTDSG YFKWTQWIFL QLYDRGLAYM SEVDVNWCEE LKTVLANEEV DEKLADGYTV
     VRRPLRQWVL KITAYAERLL ADLEELDWPE NVKQMQRNWI GRSEGVEIDF ELRCHRTTLK
     AYTTRPDTLF GATYLVIAPE HPMAEKLATA PQLLVVKEYI TKAKLKSDLE RTGLQKEKSG
     VFTGSYAINP ATGQPLPIWI SDFVLISYGT GAIMSVPAHD SRDWAFAKQY NLPIIEVIKS
     PHDVQEAVFE EKNSTCVNSA NDEISLNGLD FATAFERMAT WLESKKVGKR KVNYKLRDWI
     FSRQRYWGEP IPIKHYEDGT IRPETNLPLE LPAVEAYHPT STGESPLANI TEWLIGNDEH
     GAFRRETNTM PQWAGSCWYY LRFIDPHNHA QVVDGNNERY WMNVDLYIGG AEHAVLHLLY
     SRFWHKVLYD LGVVSTKEPF QKLFNQGMIL GEDNEKMSKS RGNVIPADHV LQRYGADAVR
     LYEMFLGPLE QVKPWNTNGI EGISRFLGKV WRFVYPEHSE AATQPSNEPL PDELLRRMHK
     TIKKVGDDTS SLKFNTAIAE MMVFVNELTK TGCNNREAIE TLLKLLAPYA PHMTEELWEA
     LGHTNSISHE PFPTFNPALV EENMAIIAVQ VNGKLRGTFT VPAKSPKEML LEEARKVESV
     AKFLEGKTIV KEIVVPDKLV NFAVK