SYL_SHEDO
ID SYL_SHEDO Reviewed; 863 AA.
AC Q12R39;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 101.
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=Sden_0797;
OS Shewanella denitrificans (strain OS217 / ATCC BAA-1090 / DSM 15013).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=318161;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS217 / ATCC BAA-1090 / DSM 15013;
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 Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of Shewanella denitrificans OS217.";
RL Submitted (MAR-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=ABE54087.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000302; ABE54087.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041406041.1; NC_007954.1.
DR AlphaFoldDB; Q12R39; -.
DR SMR; Q12R39; -.
DR STRING; 318161.Sden_0797; -.
DR EnsemblBacteria; ABE54087; ABE54087; Sden_0797.
DR KEGG; sdn:Sden_0797; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001982; 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..863
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334816"
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; 97238 MW; 76F3AB92441C7F9A CRC64;
MQELYNPSEI EALVQKHWQE HKTFEVTEDE SKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARYQRLQG KNVLQPIGWD SFGLPAENAA INNKTSPAPW TYENIDYMKN QLKLLGFGYD
WSREIATCTP EYYRWEQWFF TKLYEKGMVY KKTSSVNWCP NDETVLANEQ VQDGCCWRCD
TPVIQKEIPQ WFIKITDYAE ELLNDIDTLD GWPEQVKAMQ RNWIGRSEGI EMTFKVKDSE
QSFDIYTTRP DTLMGVTYVA IAAGHPLAEQ AASTNPALAA FIEECKNADT TEAAMASMEK
KGVATGLEAV HPISGKLVPI WVANFVLMNY GTGAVMSVPA HDQRDYEFAK AYGLEMQAVI
KPADSEVDIS KEAYTEKGVL FNSGTAFPEL DGLEFQAAFD AIDARLTAEG KGKRQVNYRL
RDWGVSRQRY WGAPIPMVTL ADGTVMPTPE DQLPVILPED VVMDGIQSPI KADKAWAETT
VDGKPAFRET DTFDTFMESS WYYARYCSPH ADEMLDPAKA NYWLPVDQYI GGIEHACMHL
LYFRFFHKLL RDAGLVNSNE PAKRLLTQGM VLADAYYYTN DKGARVWVSP LEAEVVEKDD
KGRVVKAVDS QGNELVYTGM SKMSKSKNNG IDPQTMVEKY GADTVRLFMM FASPPELTLE
WQESGVEGAH RFIKRLWKLA SDHVAAGPTE ALDVSKLSSS QKALRRELHK TIAKVSDDIG
RRQMFNTAVA AVMELMNHLS KAPQDSAQDR ALLAEALSAV TRLLYPIIPH MSFTLWHELG
NSNNIEDSRW PDVDEAALVE DSKLIVVQVN GKVRAKITVA ADATKEAVEQ LGLDDEHVQK
HLEGLTVRKV IYVPGKLLSL VAN