ID SYL_SYNJB Reviewed; 882 AA.
AC Q2JHX0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 112.
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=CYB_2881;
OS Synechococcus sp. (strain JA-2-3B'a(2-13)) (Cyanobacteria bacterium
OS Yellowstone B-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-2-3B'a(2-13);
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(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; CP000240; ABD03801.1; -; Genomic_DNA.
DR AlphaFoldDB; Q2JHX0; -.
DR SMR; Q2JHX0; -.
DR STRING; 321332.CYB_2881; -.
DR KEGG; cyb:CYB_2881; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR Proteomes; UP000001938; 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 Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 1.
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; 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..882
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009456"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT MOTIF 632..636
FT /note="'KMSKS' region"
FT BINDING 635
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 882 AA; 99521 MW; 6ED220A8B591A861 CRC64;
MDARYNPQAI ESKWQAHWRE IGLDRTPELK DGSRKFYALS MFPYPSGNLH MGHVRNYTIT
DVIARHKRMQ GYAVLHPMGW DAFGLPAENA AIDRGIPPAK WTYQNIAQMR EQLQRLGLSY
DWEREITTCA PDYYKWTQWL FLQFFKAGLA YQKEAPVNWD PVDQTVLANE QVDAEGRSWR
SGALVEKRML KQWFFKITAY ADQLLADLEK LSGWPERVRT MQENWIGQSV GAKVIFKTEA
GDELAVFTTR PDTLWGATFM VMSPEHPLVD KLTTAEQLQA VRAYQAQAAA RSEIERSAED
REKTGVWTGS YAINPVNQER IPIWIADYVL MGYGTGAIMA VPAHDQRDFE FARKFGLPIK
RVVQPPEGSL SSTDRASGTE SSELQAAWTG EGVMINSGPL DGIPVGKGPG QSVERAIAWL
EAQGLGEKQI NYRLRDWLIS RQRYWGCPIP VIHCPHCGIV PVPEKDLPVL LPEDVELTGR
GGSPLAQLED WVKVKCPTCG AEARRETDTM DTFICSSWYF LRFSDARNDR EIFRKDRVNA
WLPVDQYVGG IEHAILHLLY SRFFTKVLRD RGLLDFDEPF LRLLTQGMVQ GRTYYNPNKS
GKDRWIPAAL VKDPDNPTDP ETGEPLEVIY ATMSKSKGNG VDPEEVLAHY GADTARMFIL
FKAPPEKDLE WDDADVEGQF RFLNRVWRQV YEFVVRGGGT ESWRGRVSEL LPAKVEVGSL
TKAEKDLRRA IHTAIKEVSE DLENDYQFNT AIAELMKLSN ALGEAGIPDS PVYAEGIRTL
VLLMAPFAPH IAEELWQALG GADSVHRQSW PSYDPAALVA DTVTIVIQVN GKLRGSFEAP
AEVTPEEQEQ LALRSEAAQK YLEGATPKKV VVVPKKLVNF VL
//
