ID SYL_SHELP Reviewed; 863 AA.
AC A3QH47;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 118.
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=Shew_2929;
OS Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=323850;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1088 / PV-4;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA Fredrickson J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella loihica PV-4.";
RL Submitted (MAR-2007) 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; CP000606; ABO24795.1; -; Genomic_DNA.
DR RefSeq; WP_011866726.1; NC_009092.1.
DR AlphaFoldDB; A3QH47; -.
DR SMR; A3QH47; -.
DR STRING; 323850.Shew_2929; -.
DR KEGG; slo:Shew_2929; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000001558; 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 CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 1.
DR PRINTS; PR00985; TRNASYNTHLEU.
DR SUPFAM; SSF47323; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 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_1000009424"
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; 97736 MW; 8CD8A85373777D84 CRC64;
MQEQYLPSEI EAKVQQHWQD TKTFEVTEDE SKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARYQRLQG KNVLQPIGWD SFGLPAENAA INNKTAPAPW TYENIDYMKN QLKMLGFGYD
WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTASVNWCP NDETVLANEQ VQDGCCWRCD
TQVVQKEIPQ WFIKITDYAE ELLNDIDQLD EWPEQVKTMQ RNWIGRSEGI EMTFQVEGSD
QSFDIYTTRP DTVMGVTYVA IAAGHPLAQQ AAENNPVLAE FIEECKNADT TEAAMAAMEK
KGVDTGLKAI HPLTGKLVPI WAANFVLMNY GTGAVMSVPG HDQRDYEFAT KYGLPIVGVI
KPADGELDIS EEAYTEKGIL FNSGDSFPEL DGLDFQAAFD AIDAKLSSEG KGKRQVNYRL
RDWGVSRQRY WGAPIPMVTL ADGTVMPTPE DQLPVILPED VVMDGIQSPI KADKEWAKTQ
VNGQEAFRET DTFDTFMESS WYYARYCSPK ADQMLDPAKA NYWLPVDQYI GGIEHACMHL
LYFRFFHKLL RDIGLVNSDE PAKRLLTQGM VLADAFYYTD DKGARVWVSP NDAKVTETDD
KGRIVKAVDS QGHELVYTGM SKMSKSKNNG IDPQEMVDKY GADTVRLFMM FASPPELTLE
WQESSVEGAH RFIKRLWKLA HDHVSQGPTV ALNVASLDSA QKELRRELHK TIAKVGDDIE
RRQMFNTAIA SVMELMNRLQ KAPMESEQDR ALMQEALCAV VRLLYPIIPH TSFELWQALG
HEETIENVLW PVVDESALVE DSKLIIVQVN GKLRAKVTVA ADADKDTVEA AGMAEEGVIK
HTEGKTVRKV IYVPGKLLNI VAN
//
