ID   SYL_NITHX               Reviewed;         878 AA.
AC   Q1QRZ8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   27-MAR-2024, entry version 105.
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};
GN   OrderedLocusNames=Nham_0098;
OS   Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Nitrobacter.
OX   NCBI_TaxID=323097;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10229 / NCIMB 13809 / X14;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L.,
RA   O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T.,
RA   Gentry M.E., Bruce D., Richardson P.;
RT   "Complete sequence of chromosome of Nitrobacter hamburgensis X14.";
RL   Submitted (MAR-2006) 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; CP000319; ABE60999.1; -; Genomic_DNA.
DR   RefSeq; WP_011508706.1; NC_007964.1.
DR   AlphaFoldDB; Q1QRZ8; -.
DR   SMR; Q1QRZ8; -.
DR   STRING; 323097.Nham_0098; -.
DR   KEGG; nha:Nham_0098; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_5; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000001953; 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; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   CDD; cd00812; LeuRS_core; 1.
DR   Gene3D; 2.20.28.290; -; 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; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; 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..878
FT                   /note="Leucine--tRNA ligase"
FT                   /id="PRO_1000009379"
FT   MOTIF           43..53
FT                   /note="'HIGH' region"
FT   MOTIF           630..634
FT                   /note="'KMSKS' region"
FT   BINDING         633
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   878 AA;  98481 MW;  E201CAD309F8241A CRC64;
     MTSDRYNARD AEPRWQAAWD QQAIFATKND DPREKYYVLE MFPYPSGRIH IGHVRNYTLG
     DVIARYMRAK GYNVLHPMGW DAFGLPAENA AIERKVAPKA WTYDNIKAMK KQLRSIGLSL
     DWAREFATCD PSYYKHQQKM FLDFLRAGLA EREKRKINWD PVDMTVLANE QVIDGRGWRS
     GAVVEQREMN QWVFKITKYS QELLEALDTL DRWPDKVRLM QRNWIGRSEG LLLRFALDPA
     TTPNGEGELK IFTTRPDTLF GAKFMAIAPD HPLAQAAAKD NPALAEFIAE CKRRGTAQAE
     IDTAEKMGFD TGIRAIHPFD PDWTLPVYVA NFILMEYGTG AIFGCPAHDQ RDLDFVNKYG
     LGNTPVVCPE GQDPKTLVIT DTAYDGDGRM INSRFLDGMT AEAAKKEVAK RLESEMRGNM
     PVGERKVNFR LRDWGISRQR YWGCPIPVIH CPKCDVVPVP ENDLPVTLPE DVTFDKPGNA
     LDHHPTWKHV TCPQCGARAT RETDTMDTFV DSSWYFARFT DPWNETAPTT PEIANRMMPV
     DQYIGGVEHA ILHLLYSRFF TRAMKATGHL SMDEPFKGMF TQGMVVHETY RKADGGWASP
     DEVGIEAVGN GRRATLISTG EPVEIGAVEK MSKSKRNTVD PDDIIGSYGA DTARWFMLSD
     SPPDRDVIWS EEGVQGASRF MQRLWRLVNE SAEAGKAAPR DKPATFGTDA LALRKAAHGA
     LDKVSTGIER LHFNVCLANI REFANTLAET LARFGTRTSD LAPDIAWSLR EAATILVQLF
     SPMMPHLSEE CWHALGHTGL VSEARWPQIE RDLLVEDTVT LPVQVNGKKR GEVTVASSAP
     NPEIETAVLA LDAVRQALGG KPARKIIIVP QRIVNVVG
//