ID   SYL_SYNY3               Reviewed;         869 AA.
AC   P73274;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 139.
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=sll1074;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BA000022; BAA17302.1; -; Genomic_DNA.
DR   PIR; S77455; S77455.
DR   AlphaFoldDB; P73274; -.
DR   SMR; P73274; -.
DR   STRING; 1148.1652380; -.
DR   PaxDb; P73274; -.
DR   EnsemblBacteria; BAA17302; BAA17302; BAA17302.
DR   KEGG; syn:sll1074; -.
DR   eggNOG; COG0495; Bacteria.
DR   InParanoid; P73274; -.
DR   OMA; TFMVLAP; -.
DR   PhylomeDB; P73274; -.
DR   Proteomes; UP000001425; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 2.
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; Reference proteome.
FT   CHAIN           1..869
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152105"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           622..626
FT                   /note="'KMSKS' region"
FT   BINDING         625
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   869 AA;  98295 MW;  09D9380506F08D16 CRC64;
     MASPYNAGEI EQKWQQRWAE WGLDKTPIAS DLPKFYALSM FPYPSGNLHM GHVRNYTITD
     VIARLKRMQG YQVLHPMGWD AFGLPAENAA IERGIPPKQW TEKNIAQMRA QLQQLGLSID
     WEREVATCAP DYYRWTQWLF LEFFQAGLAY QKEATVNWDP IDQTVLANEQ VDSEGRSWRS
     GAMVERKLLR QWFLKITDYA EALLNDLEQL TGWPERVKLM QSHWIGKSVG AYLEFPIKDS
     QEKIAVFTTR PDTVYGVTYV VLAPEHPLTK VVTTAEQQGT VDEFVAMVAK ESEIERTAED
     KPKRGVKTGG IAINPFNGEE IPILIADYVL YEYGTGAVMG VPAHDQRDFK FAQDNNLPMQ
     VVIIPDDADN SDVNLTVAYT EAGVMVNSAQ FTGMASPKAK QAIIKFAEDN DYGRAKVQYR
     LRDWLISRQR YWGCPIPIIH CDDCGAVPVP TKDLPVELPD NVEFSGRGPS PLAKLEDWIN
     VPCPSCGKPA RRETDTMDTF IDSSWYFLRY ADAQNTELPF DGEKVAHWLP VDQYVGGIEH
     AILHLLYSRF FTKVLADRQL IPVKEPFQKL LTQGMVQGIT YKNPTTGKYV PAKDLQTGQQ
     VIDPKDPKDP DSGEPLQVFY EKMSKSKFNG VDPQEVLAKY GADTARMFIL FKAPPEKDLE
     WDDADVEGQF RFLNRVWRLV TDYIGDPAGI RFAVRPETLV TNEPLTKAEK DLRRAIHGAI
     KEVAEDLNDD YQFNTAISEM MKLSNALIAA TDLISFPVYQ EGIETLLLLL APFAPHLTEE
     LWHRLGRTDS IHQQAWLQVD PTALVLDEIT LVIQVLGKTR GTITVPASAD KTQLEELARN
     SDLAQRYLEG KTIKKVIVVP GKLVNFVIT