ID   SYL_GEOMG               Reviewed;         824 AA.
AC   Q39T99;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   27-MAR-2024, entry version 122.
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=Gmet_2300;
OS   Geobacter metallireducens (strain ATCC 53774 / DSM 7210 / GS-15).
OC   Bacteria; Thermodesulfobacteriota; Desulfuromonadia; Geobacterales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=269799;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53774 / DSM 7210 / GS-15;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Geobacter metallireducens GS-15.";
RL   Submitted (OCT-2005) 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; CP000148; ABB32525.1; -; Genomic_DNA.
DR   RefSeq; WP_004514498.1; NC_007517.1.
DR   AlphaFoldDB; Q39T99; -.
DR   SMR; Q39T99; -.
DR   STRING; 269799.Gmet_2300; -.
DR   KEGG; gme:Gmet_2300; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   Proteomes; UP000007073; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   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; 1.
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..824
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009346"
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;  93514 MW;  63EB85F98765DD2D CRC64;
     MEEKYIPRNV EEKWQKIWEE NKTYKVTEDP SKPKYYLLEM FPYPSGRIHM GHVRNYSIGD
     VVGRFKRLRG FNVLHPMGWD AFGMPAENAA IQHKSHPAKW TYENIAYMRS QLKKMGLSYD
     WDRELATCDL DYYKWEQKVF LEMYEKGLAY KKTSYVNWCP KCETVLANEQ VEDGACWRCD
     SEVTQKELEQ WFFRITDYAE ELLEYTEKLP GWPERVLTMQ RNWIGKSYGC EIDFPVEGSL
     AKIKVFTTRQ DTLYGATFMS LAPEHPMALE LTTPDRRAEV EAFIDKVKKT DKIKRTAEDF
     EKEGVFTGSY CINPVTNRRM PVFLANFVLL DYGTGAVMAV PTHDQRDFEF ARKYDLPLQV
     VIQPEGETLD PAAMATAYTE VGTMVNSGTF DGLRSDEAKE KIADYLAKEG IGTKTVNFRL
     RDWGISRQRY WGNPIPVIYC DICGVVPVPE KDLPVVLPMD VEFTGEGGSP LKKLDSFVNV
     PCPQCGQMAR RETDTMDTFV QSSWYFLRYC CPDFAAGPID KARAEYWMSV DQYIGGIEHA
     VLHLLYARFF TKALRDLGYV TVDEPFTNLL TQGMVIKDGA KMSKSKGNVV DPDALINRYG
     ADTARLFSLF AAPPEKDLDW SDQGVDGSYR FLSRVWRLVC DLLPFVGKGG AVDSASLSDD
     ARGLRRAVHK TIRKVTDDID ERFHFNTAIA AIMELVNAIY AFEPKNAPEN GPVLTEAIES
     VVIMLSPFVP HVTEELWEAL GHQGGVEAAG WPSFDPSAAV DEEFLIVVQV NGKLRGKVTV
     ATDATEEQVK AAAFADEKVK PWIEGKQLRK AIYVPGKLLN IVVG
//