ID   SYL_GEOUR               Reviewed;         824 AA.
AC   A5G677;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 95.
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=Gura_3134;
OS   Geotalea uraniireducens (strain Rf4) (Geobacter uraniireducens).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geotalea.
OX   NCBI_TaxID=351605;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1134 / JCM 13001 / Rf4;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chertkov O., Brettin T., Bruce D., Han C., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Shelobolina E., Aklujkar M.,
RA   Lovley D., Richardson P.;
RT   "Complete sequence of Geobacter uraniireducens Rf4.";
RL   Submitted (MAY-2007) 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; CP000698; ABQ27295.1; -; Genomic_DNA.
DR   RefSeq; WP_011939961.1; NC_009483.1.
DR   AlphaFoldDB; A5G677; -.
DR   SMR; A5G677; -.
DR   STRING; 351605.Gura_3134; -.
DR   PRIDE; A5G677; -.
DR   EnsemblBacteria; ABQ27295; ABQ27295; Gura_3134.
DR   KEGG; gur:Gura_3134; -.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000006695; 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; 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.
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..824
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000074835"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           581..585
FT                   /note="'KMSKS' region"
FT   BINDING         584
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   824 AA;  93456 MW;  5AA28FA742CB2ABA CRC64;
     MEEKYLPSRV EEKWQKFWEA NKSFRATEDK TREKYYLLEM FPYPSGRIHM GHVRNYSIGD
     VIARFKRMKG FNVLHPMGWD AFGMPAENAA IQNKSHPAKW TYENIAYMRG QLKKMGLSYD
     WDRELATCDV DYYKWEQLIF LQMYKKGLAY KKISSVNWCP KCETVLANEQ VEDGCCWRCD
     SNVDQKELEQ WSFRITDYAE ELLEYTYKLP GWPERVLTMQ RNWIGRSTGC EIDFPIEGQM
     DKIKVFTTRQ DTLFGATFMS LAPEHPMALE LTTPENMATV AAFIEKVKKT DRIRRTAEDF
     EKEGVFTGSY CINPVTNRRM PVYLANFVLT DYGTGAVMAV PTHDQRDFEF ARKYDIPMGV
     VIQPEGEALD PQTMAEAFTA EGIMVNSGRF DGLKSGAAKE QIADYLEKEG IGKKTVNYRL
     RDWGISRQRY WGNPIPMIYC DLCGAVPVPE TDLPVVLPMD ATFTGEGGNP LDKVDSFVNT
     TCPQCGEAAR RETDTMDTFV ESSWYFLRYC CPDFVSGPLD KEKTEYWMSV DQYIGGIEHA
     VMHLLYARFF TKVLRDLGYC DIDEPFTNLL TQGMVIKDGA KMSKSKGNVV DPNALIDKYG
     ADTARLFSLF AAPPEKDLDW SDQGVDGSFR FLNRVWKLVY DTLPIIGGAG ALDPAGLTNE
     GKGLRRQVHK TIRKVTEDIE ERFHFNTAIA ATMELVNTIQ SFEPKNSPQN APVLKEAIES
     VVMLLAPFVP HFTEELWAQL GNNKSLEQAG WPAFDSAAAI DEELLVVVQV NGKLRGKLTV
     AVTASEDDVK GAALADERVK PFIEGKSVKK IVYVPGKLVN IVVG