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   03-AUG-2022, entry version 89.
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; Proteobacteria; 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   EnsemblBacteria; ACA87962; ACA87962; Swoo_3702.
DR   KEGG; swd:Swoo_3702; -.
DR   eggNOG; COG0495; Bacteria.
DR   HOGENOM; CLU_004427_0_0_6; -.
DR   OMA; TFMVLAP; -.
DR   OrthoDB; 32262at2; -.
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   Gene3D; 3.40.50.620; -; 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; 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..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