SYL_PARL1
ID SYL_PARL1 Reviewed; 870 AA.
AC A7HSL7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-SEP-2007, sequence version 1.
DT 03-AUG-2022, entry version 85.
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=Plav_1280;
OS Parvibaculum lavamentivorans (strain DS-1 / DSM 13023 / NCIMB 13966).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Parvibaculaceae; Parvibaculum.
OX NCBI_TaxID=402881;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-1 / DSM 13023 / NCIMB 13966;
RX PubMed=22675581; DOI=10.4056/sigs.2215005;
RA Schleheck D., Weiss M., Pitluck S., Bruce D., Land M.L., Han S.,
RA Saunders E., Tapia R., Detter C., Brettin T., Han J., Woyke T., Goodwin L.,
RA Pennacchio L., Nolan M., Cook A.M., Kjelleberg S., Thomas T.;
RT "Complete genome sequence of Parvibaculum lavamentivorans type strain (DS-
RT 1(T)).";
RL Stand. Genomic Sci. 5:298-310(2011).
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; CP000774; ABS62900.1; -; Genomic_DNA.
DR RefSeq; WP_012110174.1; NC_009719.1.
DR AlphaFoldDB; A7HSL7; -.
DR SMR; A7HSL7; -.
DR STRING; 402881.Plav_1280; -.
DR PRIDE; A7HSL7; -.
DR EnsemblBacteria; ABS62900; ABS62900; Plav_1280.
DR KEGG; pla:Plav_1280; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_5; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000006377; 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 Gene3D; 3.90.740.10; -; 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; 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; Reference proteome.
FT CHAIN 1..870
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334788"
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 870 AA; 97257 MW; 45E0A439AAE78404 CRC64;
MSTRYNARAA EPKWQKIWEE RGDFLMRDDA DGKPKYYVLE MFPYPSGRIH MGHVRNYTMG
DVIARYKKAR GFNVLHPMGW DAFGMPAENA AMEKNVHPKG WTYDNIAAMR EQLKAIGLAI
DWSREFATCD PEYYGHEQAL FLDMLEAGLV SRKKSMVNWD PVDNTVLANE QVIDGRGWRS
GALVERRELT QWFLKISDFA DELLEGLDTL DRWPEKVRLM QKNWIGRSEG ARVFFELENA
PDGNTKLEIF TTRPDTLYGA SFCALSPHHP LTQSLAKDNP ALTDFIRECD RIGTSEEAIE
TADKMGFDTG LKARHPFIEG KTLPVYVANF VLMDYGTGAI FACPAHDQRD LDFARKYNLP
VIPVVAPKDK QGAELDAFAS GLAETGTDAY TGDGVAINSD FLNGLDVQSA KRAAIDRLEA
KGIGEGTVNY RLRDWGISRQ RYWGCPIPVI HCASCGTLPV PRDQLPVVLP DDVNFSEPGN
PLDRHPSWKH VDCPKCGKPA SRETDTFDTF VDSSWYFVRF TAPDAPTPTD KALADHWLPV
DQYIGGIEHA ILHLLYSRFF TRAMKATGHV SLDEPFAGLF TQGMVNHETY RDAEGRWVPP
AEVDIETVSG KRVAKRIADG EPVIIGSVEK MSKSKKNTVD PEDIIAKYGA DTARWFMLSD
SPPERDVQWT DQGAEGAWRF TQRLWRMVTE RQEDLAPTGT PMPTAFSEDE LTLRRAAHQA
LAAATEDFEN LRFNRAVARV YELANAVSGF TPGTPEGAFA KREALEILVQ IVGPMMPHIA
EECWEALGHG EPLTAAEWPV ADKALLVEDS VTIAVQVNGK RRDELTIARD ADRETVERAA
LALEKVGKAI DGKPVRKVIV VPGKIVNIVV