SYL_SHEFN
ID SYL_SHEFN Reviewed; 863 AA.
AC Q087K2;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 96.
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=Sfri_0705;
OS Shewanella frigidimarina (strain NCIMB 400).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318167;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCIMB 400;
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., Dalin E., Tice H., Pitluck S.,
RA Fredrickson J.K., Kolker E., McCuel L.A., DiChristina T., Nealson K.H.,
RA Newman D., Tiedje J.M., Zhou J., Romine M.F., Culley D.E., Serres M.,
RA Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Richardson P.;
RT "Complete sequence of Shewanella frigidimarina NCIMB 400.";
RL Submitted (AUG-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABI70563.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000447; ABI70563.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041413368.1; NC_008345.1.
DR AlphaFoldDB; Q087K2; -.
DR SMR; Q087K2; -.
DR STRING; 318167.Sfri_0705; -.
DR EnsemblBacteria; ABI70563; ABI70563; Sfri_0705.
DR KEGG; sfr:Sfri_0705; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000000684; 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..863
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334817"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 622..626
FT /note="'KMSKS' region"
FT BINDING 625
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 863 AA; 97261 MW; 1675C3830AD8D792 CRC64;
MQELYNPSEI EALVQKHWHE HKTFEVTEDE SKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARYQRLQG KNVLQPIGWD SFGLPAENAA INNKASPAPW TYENIDYMKN QLKLLGFGYD
WSREIATCTP EYYRWEQWFF TQLYAKGLVY KKTSSVNWCP NDETVLANEQ VQDGCCWRCD
TEVIQKEIPQ WFIKITDYAE ELLNDIDTLD GWPEQVKAMQ RNWIGRSEGI EMTFAVADSD
ASFDIYTTRP DTLMGVTYVA IAAGHPLAEQ SAQNNPELAA FLEECKNADT TEAAMASMEK
KGVATGLQAI HPISGKLVPI WVANFVLMNY GTGAVMSVPA HDQRDYEFAT KYQLAIEAVI
KPVDGEVDVS KEAYTEKGVV FNSGDAFPEL DGLDFQAAFE AIDARLTAEG KGKRQVNYRL
RDWGVSRQRY WGAPIPMVTL ADGTVVPTPE DQLPVILPED VVMDGIQSPI KADKAWAETT
VNGQPATRET DTFDTFMESS WYYARYCSPH ADEMLDPAKA NYWLPVDQYI GGIEHACMHL
LYFRFFHKLL RDAGLVNSDE PAKQLLTQGM VLADAYYYTN EKGARVWVSP LEVTVVEKDD
KGRIIKAIDN QGHELVYTGM SKMSKSKNNG IDPQVMVEKY GADTVRLFMM FASPPELTLE
WQESGVEGAH RFIKRFWKLA SDHVAAGKTE ALDTSKLNAD QKALRRELHK TIAKVSDDIA
RRQMFNTAVA SVMELMNHLL KASQETAQDR ALLAEALSAV TRLLYPIVPH MTFTLWNELG
NEGDIEDSRW PEVDESALVE DSKLIVVQVN GKVRAKITVA ADASKEDVEA LGMSDEHVQK
HTEGLTVRKV IYVPGKLLSI VAN