ID   SYL_SYNP6               Reviewed;         865 AA.
AC   Q5N006;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
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=syc2174_d;
OS   Synechococcus sp. (strain ATCC 27144 / PCC 6301 / SAUG 1402/1) (Anacystis
OS   nidulans).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX   NCBI_TaxID=269084;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27144 / PCC 6301 / SAUG 1402/1;
RX   PubMed=17211581; DOI=10.1007/s11120-006-9122-4;
RA   Sugita C., Ogata K., Shikata M., Jikuya H., Takano J., Furumichi M.,
RA   Kanehisa M., Omata T., Sugiura M., Sugita M.;
RT   "Complete nucleotide sequence of the freshwater unicellular cyanobacterium
RT   Synechococcus elongatus PCC 6301 chromosome: gene content and
RT   organization.";
RL   Photosyn. Res. 93:55-67(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}.
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; AP008231; BAD80364.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5N006; -.
DR   SMR; Q5N006; -.
DR   STRING; 269084.syc2174_d; -.
DR   EnsemblBacteria; BAD80364; BAD80364; syc2174_d.
DR   KEGG; syc:syc2174_d; -.
DR   eggNOG; COG0495; Bacteria.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000001175; 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   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..865
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152103"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT   MOTIF           629..633
FT                   /note="'KMSKS' region"
FT   BINDING         632
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   865 AA;  97356 MW;  707E35820B4B5539 CRC64;
     MQNGANSRSQ EYQGVSVDSR YDPQAIETKW QQSWAAAQLD RTPEADDRPK FYALSMFPYP
     SGNLHMGHVR NYTITDAIAR VKRRQGFRVL HAMGWDAFGL PAENAAIDRG VQPADWTYQN
     VAQMREQLKQ LGLSYDWDRE VTTCSPDYYR WTQWLFLQFF EAGLAYQKEA TVNWDPIDQT
     VLANEQVDSE GRSWRSGAKV ERRQLKQWFL KITDYAEELL QDLDQLTGWP ERVRLMQANW
     IGKSTGAYLE FPIVNSSDRV KVFTTRPDTV YGVSYVVLAP EHPLVTQVTT PEQQTAVAAF
     AAEVSQTSEL ERTAEDRPKR GVPTGGFVTN PFTGQAVPIW IADYVLVEYG TGAVMGVPAH
     DSRDFAFAQR YGLPVQPVIQ PTEGAIAEPW PAPFTEAGVM VNSGQFDGLS STEAKAKIIA
     FAEEQGWGQA HVQYRLRDWL ISRQRYWGCP IPIVHCPDCG PVAAADLPVQ LPDSVQFSGR
     GPSPLAQLED WVTTTCPSCG KPARRETDTM DTFMCSSWYY LRYSDASNPE IAFTKDKVND
     WLPVDQYVGG IEHAILHLLY SRFFTKVLRD RGLLSFDEPF KRLLTQGMVQ GLTYKNPKTG
     KYVPSDRISD PSQPVDPDTG DRLEVFFEKM SKSKYNGVDP ARVLDRYGAD TARMFILFKA
     PPEKDLEWDD ADVEGQFRFL NRVWRLVQTA SQVEATTAAD DKAEKDLRRA VHTAIQAFTE
     DLEEDYQLNT AIAELMKLTN ALNDAPMPGS PAYLKGVQTL VLLLAPFAPH IAEELWQQLG
     GERSVHLEGW PVLDESALIV DEIPLVIQIM GKTRGTITVP ASADRDQLQQ LAKNSEIAQR
     WLDGQTIRKV IVVPGKLVNF VIASP