ID   SYL_SYNC1               Reviewed;         851 AA.
AC   Q3A4P8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=Pcar_1413;
OS   Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS   (Pelobacter carbinolicus).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC   Syntrophotaleaceae; Syntrophotalea.
OX   NCBI_TaxID=338963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA   Land M., Kyrpides N., Ivanova N., Richardson P.;
RT   "Complete sequence of Pelobacter carbinolicus DSM 2380.";
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000142; ABA88659.1; -; Genomic_DNA.
DR   RefSeq; WP_011341142.1; NC_007498.2.
DR   AlphaFoldDB; Q3A4P8; -.
DR   SMR; Q3A4P8; -.
DR   STRING; 338963.Pcar_1413; -.
DR   EnsemblBacteria; ABA88659; ABA88659; Pcar_1413.
DR   KEGG; pca:Pcar_1413; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_7; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000002534; 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..851
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009387"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           612..616
FT                   /note="'KMSKS' region"
FT   BINDING         615
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   851 AA;  96220 MW;  4066676129891262 CRC64;
     MEERYDAGGI EGKWQKRWEQ DRTFKAKEKD AREKYYLLEM FPYPSGRIHM GHVRNYSIGD
     VVARFKRLQG YNVLHPMGWD AFGMPAENAA IQHKTHPGKW TYENIDNMRA QLKKMGFSYD
     WDREVATCHP EYYRWEQLIF LKMLEKGLAY KKSSFVNWCS ECQTVLANEQ VENDACWRCG
     TVVEQKELEQ WFFKITDYAQ ELLDDTSKLS GWPEPVLTMQ RNWIGRSTGC EIDFPVADSD
     LKIKVFTTRQ DTLYGATFMS LAAEHPLAME LVSAECKAEV EAFIARVRTQ DKAKRTSDDF
     VKEGVFTGSY GINPVNGRRI PIYLANFVLM DYGTGAVMAV PTHDQRDFDF ARKYDIPMIV
     VIQPEDQTLD PATMTEAWTA PGVLVNSAPF DGLDNESAKE KIAAHLEEQG VGRKTVNYRL
     RDWGVSRQRY WGTPIPIIYC PACGIVPVPE EDLPVLLPMD VEISGEGGSP LARHQEFLKV
     TCPTCGGDAR RETDTFDTFV ESSWYFARYT CPRFEQGPVD RATVDHWLPV DQYIGGIEHA
     VMHLLYARFF TKVMRDLGMM AHDEPFKNLL TQGMVCMETA SCPEHGWLFP EQVVEGKCVL
     CGATAQTGRN EKMSKSKKNV VDPDKLILSY GADTARLFSL FAAPPEKDLE WNEQGVEGCY
     RFLHRVWRAV YDNLEMISGV AVPASVDGAA RNLRRQVHAT IKKVTGDIDG RFHFNTAIAS
     VMELVNAIYG FEAKAQYPGV MREALEATVR LLAPFVPHVC EELWACLGHE GGLEAAGWPA
     WDEEALVEDE KTIVVQVNGK VRGKLTIAAD ADNDTVQQAA LKADNVVRFL EGKTVRKVVV
     VPGRLVNIVV S