ID   SYL_GEOSL               Reviewed;         824 AA.
AC   Q74AZ0;
DT   01-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=GSU2209;
OS   Geobacter sulfurreducens (strain ATCC 51573 / DSM 12127 / PCA).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Geobacteraceae; Geobacter.
OX   NCBI_TaxID=243231;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51573 / DSM 12127 / PCA;
RX   PubMed=14671304; DOI=10.1126/science.1088727;
RA   Methe B.A., Nelson K.E., Eisen J.A., Paulsen I.T., Nelson W.C.,
RA   Heidelberg J.F., Wu D., Wu M., Ward N.L., Beanan M.J., Dodson R.J.,
RA   Madupu R., Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S.,
RA   Gwinn M.L., Kolonay J.F., Sullivan S.A., Haft D.H., Selengut J.,
RA   Davidsen T.M., Zafar N., White O., Tran B., Romero C., Forberger H.A.,
RA   Weidman J.F., Khouri H.M., Feldblyum T.V., Utterback T.R., Van Aken S.E.,
RA   Lovley D.R., Fraser C.M.;
RT   "Genome of Geobacter sulfurreducens: metal reduction in subsurface
RT   environments.";
RL   Science 302:1967-1969(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; AE017180; AAR35585.1; -; Genomic_DNA.
DR   RefSeq; NP_953258.1; NC_002939.5.
DR   RefSeq; WP_010942849.1; NC_002939.5.
DR   AlphaFoldDB; Q74AZ0; -.
DR   SMR; Q74AZ0; -.
DR   STRING; 243231.GSU2209; -.
DR   EnsemblBacteria; AAR35585; AAR35585; GSU2209.
DR   KEGG; gsu:GSU2209; -.
DR   PATRIC; fig|243231.5.peg.2241; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   InParanoid; Q74AZ0; -.
DR   OMA; TFMVLAP; -.
DR   Proteomes; UP000000577; 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   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_0000152020"
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;  93367 MW;  5D5B9DB48DFCED55 CRC64;
     MQERYIPKNV EGKWQEIWEE NKTFTVTEDP SKPKYYLLEM FPYPSGRIHM GHVRNYSIGD
     VVGRFKRMRG FNVLHPMGWD AFGMPAENAA IKHGSHPAKW TYENIDYMRS QLKKMGLSYD
     WGRELATCDV DYYKWEQKMF LEMYEKGLVY KKSSFVNWCP ACETVLANEQ VEDGCCWRCD
     SDVTQKELDQ WFFRITRYAE ELLEDTWNLP GWPERVLVMQ RNWIGKSFGC EIDFPVEGKV
     EKVKVFTTRQ DTLYGATFMS LAPEHPQALE LTTPERRAEV EAFIDKVKKT DKIKRTAEDF
     EKEGVFTGAY CINPVTNLRM PVYLANFVLL DYGTGAVMAV PTHDQRDFEF ARTYDLPLQV
     VIQPEGETLD PAAMTAAYTE VGTMVNSGPF NGMKSDEAKE KIADYLEQEG VGTKTVNYRL
     RDWGISRQRY WGNPIPVINC DICGVVPVPD KDLPVVLPMD AEFTGEGGNP LARVESFVNV
     TCPQCGAEAR RETDTMDTFV QSSWYFLRYC CPDFACGPID RARAGYWMPV DQYIGGIEHA
     VLHLLYSRFF TKALRDLGYV TVAEPFKNLL TQGMVIKDGA KMSKSKGNVV DPDALIERYG
     ADTARLFTLF AAPPEKDLDW SDQGVEGSFR FLNRVWRLVF EVLPFIGSAG KPDPAALGDG
     ARDLRRTVHK TIRKVTDDLD ERFHFNTAIS AVMELVNAIQ SFEPKNAPEN APVLREAVES
     VVQLLAPFVP HVAEELWESL GHQGGVEASG WPSYDPEATV EEELLIVVQV NGKLRGKVTV
     AVDAGEEQVK AAAFADDKVK PWLDGKQIRK AIYVPGKLLN IVVG