ID   SYL_NITEC               Reviewed;         868 AA.
AC   Q0AG57;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Neut_1429;
OS   Nitrosomonas eutropha (strain DSM 101675 / C91 / Nm57).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosomonas.
OX   NCBI_TaxID=335283;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 101675 / C91 / Nm57;
RX   PubMed=17991028; DOI=10.1111/j.1462-2920.2007.01409.x;
RA   Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S.,
RA   Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.;
RT   "Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas
RT   eutropha C91: implications for niche adaptation.";
RL   Environ. Microbiol. 9:2993-3007(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; CP000450; ABI59675.1; -; Genomic_DNA.
DR   RefSeq; WP_011634481.1; NC_008344.1.
DR   AlphaFoldDB; Q0AG57; -.
DR   SMR; Q0AG57; -.
DR   STRING; 335283.Neut_1429; -.
DR   EnsemblBacteria; ABI59675; ABI59675; Neut_1429.
DR   KEGG; net:Neut_1429; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_4; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
DR   Proteomes; UP000001966; 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.
FT   CHAIN           1..868
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009378"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT   MOTIF           624..628
FT                   /note="'KMSKS' region"
FT   BINDING         627
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   868 AA;  98169 MW;  91196E00FCE9842F CRC64;
     MQEKYHPQEI EQQARQSWQE TGIFNTTEIP DKPKYYCLSM FPYPSGKLHM GHVRNYTIGD
     VLSRYRRMQG YNVMQPMGWD AFGLPAENAA IQKGVPPAKW TYDNIAYMRS QLQSLGLAID
     WKRELATCDP EYYRWNQWLF LRMLEKGIAY QKTQVVNWDP VDQTVLANEQ VIDGCGWRTG
     AVVEKREIPG YYLAITRYAD ELLAGLENLP GWPERVKAMQ ANWIGKSYGV DIIFSPDIAS
     GMPQALKVFT TRADTLMGAT YVAVAAEHPV ALYAAQNQPK LAAFIESCRQ GATMEAELAL
     QEKKGMATGL YVLHPLTGER LPVWVANYVL MSYGEGAVMA VPAHDERDFD FARQYALPIR
     PVIKPEDGEL PAPLAQAFTG YGVTFDSGEF SSLKSMDAVD AIATKLKLEE QGEKRVRYRL
     RDWGISRQRY WGCPIPLVHC DQCGVVPVPD DQLPVTLPED LVPDGSGNPL TKTPSFYECT
     CPRCGQQAHR ETDTMDTFVD SSWYFIRYAC QDQQAAMTDQ RANYWLPVDQ YIGGIEHAIL
     HLLYSRFWSK VMRDLGLVSF DEPFANLLTQ GMVLNEIFFR KTGNGRIQYF NPVEVDVQYD
     AEGKKIGAVL QADGQPVESG GIGTMSKSKN NGIDPQEIIE QYGADTARLF MMFASPPTQT
     LEWSDAGVEG AFRFLKRLWR QVYLHRQQGS DMSATDAIPH LEYPADLRDL RCQLHQTIVK
     VTDDLERRHT FNTAIAAVME LMNKLAGVQD ISPAARQLMQ EALENSVLLL SPIVPHICHI
     LWRELRPGTE LLDQPWPQAD EQALIQDEIE IVVQINGKLR GQIRIAREAD QATIERIALE
     HEHVQRNIAG QPIRKVVIVP GRLVNIVV