SYL_SYNJA
ID SYL_SYNJA Reviewed; 873 AA.
AC Q2JV13;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 07-MAR-2006, sequence version 1.
DT 03-AUG-2022, entry version 106.
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=CYA_1256;
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus;
OC unclassified Synechococcus.
OX NCBI_TaxID=321327;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab;
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; CP000239; ABC99439.1; -; Genomic_DNA.
DR RefSeq; WP_011430119.1; NC_007775.1.
DR AlphaFoldDB; Q2JV13; -.
DR SMR; Q2JV13; -.
DR STRING; 321327.CYA_1256; -.
DR EnsemblBacteria; ABC99439; ABC99439; CYA_1256.
DR KEGG; cya:CYA_1256; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_3; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008818; 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; 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; 3.
DR Pfam; PF13603; tRNA-synt_1_2; 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..873
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009455"
FT MOTIF 43..53
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 873 AA; 98433 MW; 14D89A03BC66321F CRC64;
MDARYNPPAI ESKWQAHWRE LGLDRTPELT AESRKFYALS MFPYPSGSLH MGHVRNYTIT
DVIARHKRMQ GYAVLHPMGW DAFGLPAENA AIDRGIPPAK WTYQNIAQMR DQLQRLGLSY
DWEREITTCA PDYYKWTQWL FLQFFKAGLA YQKEAPVNWD PVDQTVLANE QVDAEGRSWR
SGALVEKRLL KQWFLKITAY ADQLLADLEK LSGWPERVLT MQENWIGQSV GARVVFKTET
GEELPVFTTR PDTLWGATFM VLAPEHPLVE KLTTPEQEVA VKAYRAEAAA RSEIERSAED
REKTGVWTGS YAINPVNQER IPIWIADYVL MGYGTGAIMA VPAHDQRDFE FARQFGLPIK
LVVQPPQGGV TSAEDLQAAW TGEGVLINSG PLNGIPVGKG PGQSVERAIA WLEEQGLGER
QVNYRLRDWL ISRQRYWGCP IPIIHCPHCG IVPVPEEDLP VLLPEDVELT GRGGSPLAQL
EDWVKVKCPA CGADARRETD TMDTFICSSW YFLRFSDPRN DREIFRKDLV NAWLPVDQYV
GGIEHAILHL LYSRFFTKVL RDLGLLNFDE PFSRLLTQGM VQARTYYNPN KSGKDRWIPT
ALVKDPNDPR DPETGEPLQV IYATMSKSKG NGVDPEEVLA NYGADTARMF ILFKAPPEKD
LEWDDADVEG QFRFLNRVWR QVYEFVVRGS GTESLQGKAA ELLQAKVEAG SLTKAERDLR
RAVHTAIKEV SEDLEEYQFN TAIAGLMKLS NALAEAEIPD SPVYAEGIRT LVLLLAPFAP
HMAEELWQAL GGTDSVHRQA WPTYDPAALV ADTVTIVVQV NGKLRGSFEA PADVTPQEQE
RLALQSEAAQ RYLQGMTPKR VIVVPKKLVN LVV
