ID SYL_FUSNN Reviewed; 859 AA.
AC Q8RIQ3;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 27-MAR-2024, entry version 126.
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=FN1517;
OS Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 /
OS BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355).
OC Bacteria; Fusobacteriota; Fusobacteriia; Fusobacteriales; Fusobacteriaceae;
OC Fusobacterium.
OX NCBI_TaxID=190304;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC
RC 2640 / LMG 13131 / VPI 4355;
RX PubMed=11889109; DOI=10.1128/jb.184.7.2005-2018.2002;
RA Kapatral V., Anderson I., Ivanova N., Reznik G., Los T., Lykidis A.,
RA Bhattacharyya A., Bartman A., Gardner W., Grechkin G., Zhu L., Vasieva O.,
RA Chu L., Kogan Y., Chaga O., Goltsman E., Bernal A., Larsen N., D'Souza M.,
RA Walunas T., Pusch G., Haselkorn R., Fonstein M., Kyrpides N.C.,
RA Overbeek R.;
RT "Genome sequence and analysis of the oral bacterium Fusobacterium nucleatum
RT strain ATCC 25586.";
RL J. Bacteriol. 184:2005-2018(2002).
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; AE009951; AAL93643.1; -; Genomic_DNA.
DR RefSeq; NP_602344.1; NC_003454.1.
DR RefSeq; WP_011015646.1; NZ_CP028101.1.
DR AlphaFoldDB; Q8RIQ3; -.
DR SMR; Q8RIQ3; -.
DR STRING; 190304.FN1517; -.
DR PaxDb; 190304-FN1517; -.
DR EnsemblBacteria; AAL93643; AAL93643; FN1517.
DR GeneID; 79782458; -.
DR KEGG; fnu:FN1517; -.
DR PATRIC; fig|190304.8.peg.20; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_0; -.
DR InParanoid; Q8RIQ3; -.
DR BioCyc; FNUC190304:G1FZS-21-MONOMER; -.
DR Proteomes; UP000002521; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 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..859
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152018"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 611..615
FT /note="'KMSKS' region"
FT BINDING 614
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 859 AA; 99129 MW; 1F081E6B36C46E0C CRC64;
MRDYEFKEIE KKWQERWSKD NIFKTENQVE GKENYYVLSM LPYPSGKLHV GHARNYTIGD
VISRYKRMKG YNVLQPMGWD SFGLPAENAA IQNGTHPAIW TKSNIENMRR QLKLMGFSYD
WEREIASYTP EYYKWNQWLF KRMYEKGLIY KKKSLVNWCP DCQTVLANEQ VEDGMCWRHS
KTHVIQKELE QWFFKITDYA DELLEGHEEI KDGWPEKVLT MQKNWIGKSF GTELKLKVVE
TGEDLPIFTT RIDTIYGVSY AVVAPEHPIV EKILKDNPSI KDKVTEMKNT DIIERGAEGR
EKNGIDSGWH IENPVNKEIV PLWIADYVLM NYGTGAVMGV PAHDERDFVF AGKYNLPVKQ
VITSKKSDEK VQLPYIEEGV MINSGEFNGL SSKDALVKIA EYVEEKGYGK RTYKYRLKDW
GISRQRYWGT PIPALYCEKC GEVLEKDENL PVLLPDDIEF SGNGNPLETS NKFKEATCPC
CGGKARRDTD TMDTFVDSSW YFLRYCDPKN LNLPFSKEIV DKWTPVDQYI GGVEHAVMHL
LYARFFHKVL RDLGLLSSNE PFKRLLTQGM VLGPSYYSEK ENKYLLQKAA IIKGDKAYSQ
SGEELQVKVE KMSKSKNNGV DPEEMLDKYG ADTTRLFIMF AAPPEKELEW NENGLAGAYR
FLTRVWRLVF ENSELVKNAN DEIDYNKLSK EDKTLLIKLN QTIKKVTDAI ENNYHFNTAI
AANMELINEV QTYVSSSMNS EQAAKILGYT LKKIIIMLSP FVPHFCDEIW EELGEKGYLF
NEKWPEYDEK MLSSDETTIA VQVNGKVRGS FEIAKDSEQA LVEKTALKLP NVAKHLEGMN
VVKIIVIPNK IVNIVVKPQ
//
