SYL_CHLPD
ID SYL_CHLPD Reviewed; 816 AA.
AC A1BDY0;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
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};
GN OrderedLocusNames=Cpha266_0551;
OS Chlorobium phaeobacteroides (strain DSM 266).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=290317;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 266;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Goltsman E.,
RA Schmutz J., Larimer F., Land M., Hauser L., Mikhailova N., Li T.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides DSM 266.";
RL Submitted (DEC-2006) 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; CP000492; ABL64607.1; -; Genomic_DNA.
DR RefSeq; WP_011744440.1; NC_008639.1.
DR AlphaFoldDB; A1BDY0; -.
DR SMR; A1BDY0; -.
DR STRING; 290317.Cpha266_0551; -.
DR EnsemblBacteria; ABL64607; ABL64607; Cpha266_0551.
DR KEGG; cph:Cpha266_0551; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000008701; 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; 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; 2.
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..816
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000009322"
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 816 AA; 93335 MW; 6770B1DAC50560F1 CRC64;
MRYDFSTIEK KWQSFWLKNN SFSSGESTDK PKYYVLDMFP YPSGSGLHVG HLEGYTATDI
VARYKRSCGY NVLHPMGWDA FGLPAEQFAI KTGTHPKNTT EKNISSFRET LQAMGFSYDW
SREINTTSPD YFRWTQWIFI KLYELGLAYV SEVDINWCEE LKTVLANEEV EEKVKEGYTV
IRKPLRQWVL KITAYAERLL DDLDELDWPE NVKQMQRNWI GRSEGMEIDF ELRCHNRKLR
VYTTRPDTLF GATFLVISPE HPLALKLATA QQLVAVTQYI KEAKLKSELE RTGLQKDKTG
IFTGSFAINP ATGDPLPVWI SDFVLTSYGT GAIMSVPAHD SRDWEFAKKF GLPIIEVIKS
PDGVDDAAFE GKESVSINSS NPEISIDGLH FSEAFQIMAH WLETKGLGER KVTYKLRDWI
FSRQRYWGEP IPVKHYEDGS IRTESNLPLQ LPEVEAYQPS ETGESPLATM HDWLYGADEF
GSFRRETNTM PQWAGSCWYY LRFIDPENNA QLIDPAKEKY WMNVDLYIGG AEHAVLHLLY
ARFWHKVLYD LGVVSSREPF KKLFNQGMIL GEDNEKMSKS RGNVIPADQV LKDYGADAVR
LYEMFLGPLE QVKPWNTNGI EGISRFLGKV WRLVYPDSEN PDQRDQAAVL DENPLPEILQ
RRMHKTIKKV TEDTDHLKFN TAISEMMVFV NELQKNGCRQ KSAVENLLLM LAPYAPHITA
ELWQAIGHTS PISAEPFPVF DPAIAEDPVV TIAVQVNGKL RGRFTAPAKS PEESLVDMAK
HVDTVIKFLE GQTIVKEIVI QDKLVNFAVK QSIPNH