ID SYL_SHEWM Reviewed; 859 AA.
AC B1KDW0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, 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=Swoo_3702;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-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; CP000961; ACA87962.1; -; Genomic_DNA.
DR RefSeq; WP_012326294.1; NC_010506.1.
DR AlphaFoldDB; B1KDW0; -.
DR SMR; B1KDW0; -.
DR STRING; 392500.Swoo_3702; -.
DR KEGG; swd:Swoo_3702; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR Proteomes; UP000002168; 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 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..859
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000091363"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 618..622
FT /note="'KMSKS' region"
FT BINDING 621
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 859 AA; 97372 MW; F83A898A01DEE481 CRC64;
MQEQYQPSEI EAKVQQHWQD TKTFEVTEDE NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARYQRLQG KNVLQPIGWD SFGLPAENAA IKNSSAPAPW TYENIDYMKN QLKMLGFGYD
WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTASVNWCP NDETVLANEQ VQDGCCWRCD
TEVVQKEIPQ WFIKITDYAD ELLSDIDQLD EWPEQVKTMQ RNWIGRSEGI EMTFQVADSD
ESFDIYTTRP DTVMGVTYVA IAAGHPLAEK AAANSPELAA FIEECKNADT TEAAMAAMEK
KGVATGLYAI HPLTGKQVPI WAANFVLMNY GTGAVMSVPA HDQRDYEFAI KYGLAIEGVI
KPEDAELDIS EEAYTEKGVL FNSAEFDGLD FQAAFDAIDA KLTAEGKGKR QVNFRLRDWG
VSRQRYWGAP IPMVTLADGT VVPTPEDQLP VILPEDVVMD GIQSPIKADK EWAKTQINGE
DALRETDTFD TFMESSWYYA RYCSPHADEM LDPAKANYWL PVDQYIGGIE HACMHLLYFR
FFHKLLRDIG LVNSDEPAKR LLTQGMVLAD AYYYTNEKGA RVWVSPADVT VQETDDKGRT
VKAVDSHGNE LVYTGMSKMS KSKNNGIDPQ EMVDKYGADT VRLFMMFAAP PELTLEWQES
SVEGAHRFIK RLWKVAHDHV AKGTTVSLDV KSLDAKQKEL RRELHKTIAK VGDDIERRQM
FNTAIASVME LMNRLQKAPT ETEQDRALMQ EALSAVVRLL YPIIPHTSFS LWKELGNEEN
IEDVRWPEAD ESALVEDSKL IIVQVNGKLR AKITVPADAT KEAVEAQGFA EEGVIKHTEG
KTVRKVIYVP GKLLNIVAN
//
