SYL_PROA2
ID SYL_PROA2 Reviewed; 806 AA.
AC B4S5G4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, 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=Paes_0505;
OS Prosthecochloris aestuarii (strain DSM 271 / SK 413).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Prosthecochloris.
OX NCBI_TaxID=290512;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 271 / SK 413;
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., Anderson I., Liu Z., Li T., Zhao F., Overmann J.,
RA Bryant D.A., Richardson P.;
RT "Complete sequence of chromosome of Prosthecochloris aestuarii DSM 271.";
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; CP001108; ACF45561.1; -; Genomic_DNA.
DR RefSeq; WP_012505098.1; NC_011059.1.
DR AlphaFoldDB; B4S5G4; -.
DR SMR; B4S5G4; -.
DR STRING; 290512.Paes_0505; -.
DR EnsemblBacteria; ACF45561; ACF45561; Paes_0505.
DR KEGG; paa:Paes_0505; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_10; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002725; 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..806
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091344"
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 806 AA; 92200 MW; 080A408174850D76 CRC64;
MRYEFSTIEQ KWQKYWADNQ TFLTDDNPDK PKYYVLDMFP YPSGTGLHVG HLEGYTATDI
IARYKRSRGF NVLHPMGWDA FGLPAEQFAI KTGTHPTTTT QKNVSSFRQT LQNMGFSYDW
SREINTTDPN YFRWTQWIFL QLLDKGLAYM SEVDVNWCED LRVVLANEEV DEKIAAGHTV
VRKPLRQWVL KITAYAERLL GDLDELDWPE NVKQMQRNWI GRSEGVEIDF ELPCHRQKLT
VYTTRPDTLF GASYLVISPE HPLAEKLATA PQLVELKNYI REAKLKTELE RTGLQKEKTG
VFTGSYAINP ANGEALPVWV SDFVLTSYGT GAIMSVPAHD SRDWEFAKKF GLPIIEVIQS
PHDVQDEVFE GKESICVNSS NNEISLDGLD FTSAFKRMAD WIESSGKGRR KINYKLRDWI
FSRQRYWGEP IPVKHYDDGS LRPETDLPLT LPEVEAYHPS TTGESPLANI EDWLFGQDEH
GAFRRETNTM PQWAGSCWYY LRFIDPSNQQ QLVDPDKERY WMNVDLYIGG AEHAVLHLLY
ARFWHKVLYD LGVVSTKEPF QKLFNQGMIL GEDNEKMSKS RGNVIPADHV MQSYGADAVR
LYEMFLGPLE QVKPWNTNGI EGISRFLSRV WRIVYPEQEG PAMLTDTPLD DALTRRMHKT
IKKVTEDTEH LKFNTAIAEM MVFVNELHKA GCRNRKALET LLLLLAPYAP HICEELWQAA
GNNEPIARAP FPVFDPALAE DNELTIAVQV NGKLRGTFLA PAGLSKEAMI AGAREIESVK
KFLEGMTIIK EIAVPGKLVN FAVKPL
