ID   SYL_SYNPW               Reviewed;         878 AA.
AC   A5GL71;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 88.
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=SynWH7803_1260;
OS   Synechococcus sp. (strain WH7803).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC   unclassified Synechococcus.
OX   NCBI_TaxID=32051;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH7803;
RG   Genoscope;
RL   Submitted (MAY-2006) 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; CT971583; CAK23686.1; -; Genomic_DNA.
DR   RefSeq; WP_011933166.1; NC_009481.1.
DR   AlphaFoldDB; A5GL71; -.
DR   SMR; A5GL71; -.
DR   STRING; 32051.SynWH7803_1260; -.
DR   EnsemblBacteria; CAK23686; CAK23686; SynWH7803_1260.
DR   KEGG; syx:SynWH7803_1260; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001566; 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; Reference proteome.
FT   CHAIN           1..878
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000334832"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           58..68
FT                   /note="'HIGH' region"
FT   MOTIF           632..636
FT                   /note="'KMSKS' region"
FT   BINDING         635
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   878 AA;  98170 MW;  26816D443AA013D4 CRC64;
     MTASKSSSAT ASASDRPDRY DPIALEQRWQ SQWQQDDLYA TRSPEPGQNA FYALSMFPYP
     SGSLHMGHVR NYVITDVIAR AQRMRGDSVL HPMGWDAFGL PAENAAIERQ VDPGVWTDRN
     IEQMKAQLAR LGLSIDWSRE QATCHADYYR WTQWLFLELM DQGLAYQKDA TVNWDPVDQT
     VLANEQVDSE GRSWRSGALV EQKNLRQWFL RITNYADALL DDLDLLKGWP ERVRTMQANW
     IGRSIGAEID FRVSDHDDAV ITVFTTRADT LHGVSYVVLA PEHPLVATLT AEHQRESVAA
     FRDLVGELSA DERTADDRPK RGVPIGATAV NPANGESIPI WIADYVLAGY GTGAVMGVPA
     HDERDFLFAR TYELPVKRVI QAAGTSDHLS DGEAWTGPGI LLNSGRFDGQ SSEEARQEIT
     AHGQELGWAR PKRQYRLRDW LISRQRYWGC PIPVIHCDHC GAVPVPADQL PVTLPKDVDL
     QGKGGSPLAS LQSWVNVKCP SCGRDARRET DTMDTFMCSS WYFLRFADPH NTERAFDADA
     VERWLPVQQY VGGIEHAILH LLYSRFFTKA LRDRGLLNIR EPFERLLTQG MVQGVTYRNP
     RTGRYVAPSE VSDENAPKDP VDGGELEVLF EKMSKSKYNG VDPAAVIDRY GADTARMFIL
     FKAPPEKDLE WDDADVEGQF RFLQRLWRLI ESVRSDDQDQ LLGDPVDPPE GSGLSDKEGE
     IRRAVHTAIE AVSDDLKGDF QFNTAISELM KLSNTLSGAL PEASRAVQAE AVSALIRLLA
     PFAPHLAEEF WFSLGGQDSV HKQPWPLHDP AALVRDTVDL VIQVKGKVRG TITVPADCSK
     ETLEELALAS DVAERWLEGK PPRRVIVVPG KLVNLVPS