ID SYL_NITSB Reviewed; 815 AA.
AC A6Q512;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=NIS_1464;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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; AP009178; BAF70571.1; -; Genomic_DNA.
DR RefSeq; WP_012082834.1; NC_009662.1.
DR AlphaFoldDB; A6Q512; -.
DR SMR; A6Q512; -.
DR STRING; 387092.NIS_1464; -.
DR KEGG; nis:NIS_1464; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR InParanoid; A6Q512; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000001118; 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; 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; 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; 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..815
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009382"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 583..587
FT /note="'KMSKS' region"
FT BINDING 586
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 815 AA; 94146 MW; 48FB5009F2996E89 CRC64;
MQYDPKAIEQ KWQNEWKEKN AFEPQENYSK EKMYVLSMFP YPSGRIHMGH VRNYTIGDAI
ARYYRKTGAN VLHPIGWDAF GMPAENAAIK HKVHPKKWTY ENIDYMRKEL DALGLSFSHD
REFATCDPLY SKWEQSFIID MWNRGLLYRK KAAVNWCPHD KTVLANEQVI EGRCWRCDTE
VVQKEIEQYF LKITDYAQEL LEDLKKLEGN WPNQVIAMQR NWIGRSEGLE FRLHFDETSA
KKAGIDGFEV FTTRPDTIYG VTYTALAPEH PVVKHLIETK QLSDEAVQKI CTMQNQNART
RQQAEKEGLF LDLYVIHPLT KQKIPVWVAN FVLAEYGSGA VMAVPAHDER DFEFAHKYNL
PIKYIIKPKE GELDTTKAYT EPGILFDSGE FSGFESSEAK QKIIEYFEEN GIGKRSVNYK
LKDWLVSRQR YWGTPIPLIK CPKCGIVPEK KENLPVTLPE DVEITGEGNP LELHPTWKKT
TCPKCGGEAE RETDTLDTFV ESSWYFLRYT TPRKYWEEVP FRKEDTDYWM PVDQYIGGIE
HAILHLLYAR FFTKVLRDLG YVNLDEPFKR LLTQGMVLKD GAKMSKSKGN TVDPDEIVAK
FGADTARLFI LFAAPPAKEL EWSDSAVEGA YRFIKRFFER SQNAYKTKSL PKIDQKSLSK
EEKEARKKVY EALQKSTDVY TKSFSFNTLI AASMEALNAL NGQNNPDIWT EGYWVLTNIL
EPIIPHTCWE ISHNLFERNN FTRLQLDPAA LEEDSVTLAV TVNGKRRAEI EVPKDASKEE
ILAKAKEIAK KWIDGKTIVK EIVVPGRLVN IVVKG
//
