SYL_PELPB
ID SYL_PELPB Reviewed; 807 AA.
AC B4SDX3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 83.
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=Ppha_0665;
OS Pelodictyon phaeoclathratiforme (strain DSM 5477 / BU-1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Pelodictyon.
OX NCBI_TaxID=324925;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5477 / BU-1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of Pelodictyon phaeoclathratiforme BU-1.";
RL Submitted (JUN-2008) 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; CP001110; ACF42964.1; -; Genomic_DNA.
DR RefSeq; WP_012507459.1; NC_011060.1.
DR AlphaFoldDB; B4SDX3; -.
DR SMR; B4SDX3; -.
DR STRING; 324925.Ppha_0665; -.
DR EnsemblBacteria; ACF42964; ACF42964; Ppha_0665.
DR KEGG; pph:Ppha_0665; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002724; 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; 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.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..807
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091341"
FT MOTIF 40..51
FT /note="'HIGH' region"
FT MOTIF 576..580
FT /note="'KMSKS' region"
FT BINDING 579
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 807 AA; 93181 MW; 37E6878C5B71A15B CRC64;
MRYEFSKTEA KWQAWWKEQN TFKTGDDADK PKYYVLDMFP YPSGTGLHVG HLEGYTASDI
TARYKRSCGY NVLHPMGWDA FGLPAEQFAI KTGTHPKTTT EENIRNFKGT LQAMGFSYDW
SREINTTDPH YFKWTQWIFL KLYERGLAYM SEVDVNWCEE LKTVLANEEV DEKIADGYTV
VRRPLRQWVL KITAYADRLL ADLDELNWPE NVKQMQRNWI GRSEGVEIDF ELRCHNKKLR
VYTTRPDTLF GATYLVISPE HPLAEKLATA QQLVEVKNYI SKAKLKTELE RTGLQKEKTG
VFTGSYAINP ATGEPLPVWI SDFVLISYGT GAIMSVPAHD SRDWEFAKQY NLPIIEVIQS
PHDVQERVFE EKESICVNSA NNEITLNGLP FCEAFERMAS WLETKKAGER KVNYKLRDWI
FSRQRYWGEP IPIKHYHDGT LRLETALPLV LPEVEAYHPS STGESPLANI PHWLYGSDEH
GSFRRETNTM PQWAGSCWYY LRFIDPENQE KLVDPEKERY WMNVDLYIGG AEHAVLHLLY
ARFWHKVLFD LGVVSSREPF KKLFNQGMIL GEDNEKMSKS RGNVIPADHV LERYGADAVR
LYEMFLGPLE QVKPWNTNGI EGISRFLSKV WRLVYGEHEE SATLLSEEAM PEELLRRMHK
SIKKVGEDTE QLKFNTAISE MMVFVNELQK SGCKNRSAIE TLLVLLSPYA PHITEELWES
IGHNYSISQA PFPSFDPKLV EESILTIAVQ INGKLRGTFL APAKSPKELL LQEAKKTESV
FKFLDGQTIL REIVVVDKLV NFVVKKE
