SYL_ACIET
ID SYL_ACIET Reviewed; 910 AA.
AC B9MH67;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
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=Dtpsy_3266;
OS Acidovorax ebreus (strain TPSY) (Diaphorobacter sp. (strain TPSY)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Diaphorobacter.
OX NCBI_TaxID=535289;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TPSY;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Coates J.D.;
RT "Complete sequence of Diaphorobacter sp. TPSY.";
RL Submitted (JAN-2009) 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; CP001392; ACM34695.1; -; Genomic_DNA.
DR RefSeq; WP_015914504.1; NC_011992.1.
DR AlphaFoldDB; B9MH67; -.
DR SMR; B9MH67; -.
DR STRING; 535289.Dtpsy_3266; -.
DR EnsemblBacteria; ACM34695; ACM34695; Dtpsy_3266.
DR KEGG; dia:Dtpsy_3266; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_4; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000450; 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; 1.
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.
FT CHAIN 1..910
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000199198"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 658..662
FT /note="'KMSKS' region"
FT BINDING 661
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 910 AA; 101266 MW; A75017841E67CA7E CRC64;
MQDKYNHTEV ERAAHAHWNA NDAYRVTEDQ AKPKFYACSM LPYPSGKLHM GHVRNYTIND
MLTRSLRMKG HNVLMPMGWD AFGLPAENAA LKNGVPPAQW TYDNIAYMKK QMQAMGLAID
WSREVATCDP DYYKWNQWLF LKMLDKGIAY RKTQVVNWDP VDQTVLANEQ VIDGRGWRTG
ALVEKREIPG YYLKITDYAQ ELLDHVQIGN EKATLTGWPD KVRLMQENWI GKSAGVRFAF
PHDIRNAAGE RIQDGKLYVF TTRADTIMGV TFCAVAPEHP LAQHAAASNA PLAAFIEECK
KGGTTEAELA LKEKEGMPTG LFVTHPLTGE QVEVWVGNYV LMSYGDGAVM GVPAHDERDF
AFALKYQLPI KQVVLVDGET FDFHQWQDWY GDKERGVTIN SDNFSGLSYQ DAVAAVAHAL
AEKGLGELKT TWRLRDWGIS RQRYWGTPIP IIHCESCGAV PVPEKDLPVV LPQDLVPDGS
GNPLAKCEAF LKVDCPCCGK PARRETDTMD TFVDSSWYFM RYCDPKNRDA MVAGGTDYWM
RDQKAATGGS GMDQYIGGIE HAILHLLYAR FWTKVMRDLG LVKVDEPFTK LLTQGMVLNH
IYSRRTAKGA KDYFWPHDVE HVYDEAGKIV GAKLKNPAES GDGLLPVGTP IDYEGVGTMS
KSKNNGVDPQ QLIEKYGADT ARLYTMFTAP PELTLEWNDA AVEGSYRFLR RVWNFGVKLS
AIDKDAALAS VAGAASLKDV QFGKEAKALR LEIHTVLKQV DYDYQRMQYN TVVSGAMKMI
NALEDFKATD SAGAQVALIE GFGILLRVLY PATPHIAHVL WDELGYAGTL GDLLDAAWPQ
VAPDALVQDE LELMLQVNGK LRGAIRVAAS ADKAAIEQAA LASEDFQKFA EGKAPKKVII
VPGRLVNVVV
