SYL_NITHX
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 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=Nham_0098;
OS Nitrobacter hamburgensis (strain DSM 10229 / NCIMB 13809 / X14).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; 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 EnsemblBacteria; ABE60999; ABE60999; Nham_0098.
DR KEGG; nha:Nham_0098; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
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 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..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