SYL_NATTJ
ID SYL_NATTJ Reviewed; 826 AA.
AC B2A6C2;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Nther_0537;
OS Natranaerobius thermophilus (strain ATCC BAA-1301 / DSM 18059 /
OS JW/NM-WN-LF).
OC Bacteria; Firmicutes; Clostridia; Natranaerobiales; Natranaerobiaceae;
OC Natranaerobius.
OX NCBI_TaxID=457570;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1301 / DSM 18059 / JW/NM-WN-LF;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Lykidis A., Mesbah N.M., Wiegel J.;
RT "Complete sequence of chromosome of Natranaerobius thermophilus JW/NM-WN-
RT LF.";
RL Submitted (APR-2008) 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; CP001034; ACB84133.1; -; Genomic_DNA.
DR RefSeq; WP_012447019.1; NC_010718.1.
DR AlphaFoldDB; B2A6C2; -.
DR SMR; B2A6C2; -.
DR STRING; 457570.Nther_0537; -.
DR PRIDE; B2A6C2; -.
DR EnsemblBacteria; ACB84133; ACB84133; Nther_0537.
DR KEGG; nth:Nther_0537; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_9; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001683; 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..826
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091337"
FT MOTIF 41..51
FT /note="'HIGH' region"
FT MOTIF 586..590
FT /note="'KMSKS' region"
FT BINDING 589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 826 AA; 95481 MW; 7FE2F0098DB072CC CRC64;
MKEYQPQKIE SKWQKRWQDE ISYETEVDHN KDKYYVLEMF PYPSGKLHMG HMRVYSIGDV
LARFQRMRGY NVLHPMGWDA FGLPAENAAI ENQDLPSRWT YANIDNMKDQ LQALGTSYDW
KREVSTCSPD YYKWTQWMFL QLYKNGLAYK KKAPVNWCPE CETVLANEQV ENGACWRCDS
MVEQKQLSQW FFKITEYADR LDQDLELLEE WPDRVKTMQK NWIGKSQGTE IDFPVKGSRE
KIRAFTTRPD TIFGATYMVL APEHPMTEQL VQGTDQEKEV MDFIKGVHEM GKEAREAEDL
EKEGVFTGRW AINPLNGEEI PILVGNYVLM EYGTGAIMAV PAHDQRDFQF AHKYNLPIKE
VVTPPEGEGK TESETHDELK KAYTDHGILI NSPGYNGMTS EQAIEQITRD IENKGIGAGV
TTYRLRDWLV SRQRYWGAPI PVLYCDQCGI LPVPEDELPV QLPEDVDFSQ GSRNVLAARQ
DFVETSCPQC GGSAQRETDT MDTFVCSSWY FLRYTTPWDN EVPFRQEDVN YWMPVDQYIG
GIEHAVLHLL YARFFTKVMY DQGYTNFKEP FSRLLAQGMV NKDGAKMSKS KGNVVSPDEI
LRTYGADTGR LFILFAAPPE KDLDWNDEGV EGCYRFLQRL YRLVNDNQNL VDLQLDDTKF
TKEDKEYHRL IHKTIKKVTD DISERHNFNT AISAIMELTN ASSKYKEQKE VNESLLRTGL
ETIVMLLAPF TPHIAEELWE TLGYQDSVHK LNWPSYDEKA MVAEEAEMVV QVNGKVRDHL
TVPADSSEET IKEKALEREK VQKYISGAEI KKVIVIPQKL VNIVCK