ID   SYL_GLOVI               Reviewed;         847 AA.
AC   Q7NE01;
DT   07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-2003, sequence version 1.
DT   27-MAR-2024, entry version 124.
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=gll4081;
OS   Gloeobacter violaceus (strain ATCC 29082 / PCC 7421).
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Gloeobacterales; Gloeobacteraceae;
OC   Gloeobacter.
OX   NCBI_TaxID=251221;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29082 / PCC 7421;
RX   PubMed=14621292; DOI=10.1093/dnares/10.4.137;
RA   Nakamura Y., Kaneko T., Sato S., Mimuro M., Miyashita H., Tsuchiya T.,
RA   Sasamoto S., Watanabe A., Kawashima K., Kishida Y., Kiyokawa C., Kohara M.,
RA   Matsumoto M., Matsuno A., Nakazaki N., Shimpo S., Takeuchi C., Yamada M.,
RA   Tabata S.;
RT   "Complete genome structure of Gloeobacter violaceus PCC 7421, a
RT   cyanobacterium that lacks thylakoids.";
RL   DNA Res. 10:137-145(2003).
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; BA000045; BAC92022.1; -; Genomic_DNA.
DR   RefSeq; NP_927027.1; NC_005125.1.
DR   RefSeq; WP_011144067.1; NC_005125.1.
DR   AlphaFoldDB; Q7NE01; -.
DR   SMR; Q7NE01; -.
DR   STRING; 251221.gene:10761599; -.
DR   EnsemblBacteria; BAC92022; BAC92022; BAC92022.
DR   KEGG; gvi:gll4081; -.
DR   PATRIC; fig|251221.4.peg.4113; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_3; -.
DR   InParanoid; Q7NE01; -.
DR   OrthoDB; 9810365at2; -.
DR   PhylomeDB; Q7NE01; -.
DR   Proteomes; UP000000557; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 2.
DR   Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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   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; 2.
DR   Pfam; PF13603; tRNA-synt_1_2; 1.
DR   Pfam; PF09334; tRNA-synt_1g; 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.
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..847
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_0000152021"
FT   MOTIF           39..49
FT                   /note="'HIGH' region"
FT   MOTIF           613..617
FT                   /note="'KMSKS' region"
FT   BINDING         616
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   847 AA;  95295 MW;  4C53540A83DA7029 CRC64;
     METRYNPHAI EPRRQKQWEE APHLAMDGRP KFYALSMFPY PSGALHMGHV RNYSITDVIS
     RYKRMRGFNV LHPIGWDAFG LPAENAAIDR GIHPAQWTEQ NIAQMREQLK RLGFAYAWER
     EVATCSPAYY RWTQKLFLEF WKAGLAYRKA GVVNWDPVDQ TVLANEQVDA EGRSWRSGAL
     VEKRPLEQWY LKITDYAEEL LQALGTLGDW PERVRVMQEN WIGKSVGAEL CFPINGEPEG
     IRVFTTRPDT VYGVTYLVLA PEHPLVERIT APERREAVRA FVAQVQSESE IERVSEDRPK
     QGVSTGAVAL NPFTGQAVPV WIADYVLFEY GTGAVMGVPG HDERDFVFAS QYELPIRLVV
     QAPDGSLTEP LRAAYTEVGV LVNSGPFNGL DSPTGKLKIV EYAEQQGWGK GRVQYRLRDW
     LISRQRYWGC PIPMVYCPEC GVVPVPDEQL PVALPGDVEF SGRGPSPLAK LEGWICVDCP
     QCGAPARRET DTMDTFIDSS WYFLRFADAR NGAEPFSREA VDYWLPVDQY VGGIEHAILH
     LLYSRFFTKV LRDRGLLSFD EPFKRLLTQG MVLSNAFVDP ATKKYYPPDQ VEERGGAFFA
     RPDGTPLVCA MEKMSKSKYN GIDPLTVRSE YGADTARLFV LFKAPPEKEL EWSDADVRGQ
     YSFLGRVWRT VYEFVSGEKP DRPVGEAQER DLRREVHRAI QQVGGDIEQY KFNTAIAALM
     KLNNAMADYP SGQSPAYKEG VYVIVKLLAP FAPHIGAELW QALGEAGDIH TSDWPALDES
     ALVEETIVLV IQVNGKKRDD IQVPAAASEG ELQELALASE AVRRHTDGKA IKKVIVVPGR
     LINLVVG
//