SYL_SHEON
ID SYL_SHEON Reviewed; 859 AA.
AC Q8EHP4;
DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
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=SO_1174;
OS Shewanella oneidensis (strain MR-1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=211586;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-1;
RX PubMed=12368813; DOI=10.1038/nbt749;
RA Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT Shewanella oneidensis.";
RL Nat. Biotechnol. 20:1118-1123(2002).
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; AE014299; AAN54244.1; -; Genomic_DNA.
DR RefSeq; NP_716799.1; NC_004347.2.
DR RefSeq; WP_011071405.1; NZ_CP053946.1.
DR AlphaFoldDB; Q8EHP4; -.
DR SMR; Q8EHP4; -.
DR STRING; 211586.SO_1174; -.
DR PaxDb; Q8EHP4; -.
DR PRIDE; Q8EHP4; -.
DR KEGG; son:SO_1174; -.
DR PATRIC; fig|211586.12.peg.1126; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR PhylomeDB; Q8EHP4; -.
DR BioCyc; SONE211586:G1GMP-1078-MON; -.
DR Proteomes; UP000008186; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central.
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_0000152079"
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; 96827 MW; C78D6209DFB6CA17 CRC64;
MQEQYNPSEI EALVQKHWHD TKTFEVTEDQ NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARFQRLQG KNVLQPIGWD SFGLPAENAA INNKTAPAPW TYQNIEYMKN QLKLLGFGYD
WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTASVNWCP NDETVLANEQ VQDGCCWRCD
TPVEQKEIPQ WFIKITAYAE ELLNDIDTLD GWPEQVKTMQ RNWIGRSEGV EMTFGVAGSD
KSFDIYTTRP DTLMGVTYVA IAAGHPLAEI AAQTNPELAA FIDECKNSTT SEAELATMEK
RGVATGLYAI HPITGKQVPI WAANFVLMNY GTGAVMSVPG HDQRDYEFAK KYHLPIEAVI
KPAEGDLDIS EAAYTEKGIL FNSGEFDGLD FDGAFNVIAN KLVAEGKGKR QVNYRLRDWG
VSRQRYWGAP IPMVTLADGT VIPTPEDQLP VILPEDVVMD GIQSPIKADK EWAKTQVNGQ
DALRETDTFD TFMESSWYYA RYCSPQAEQM LDPTKANYWL PVDQYIGGIE HACMHLLYFR
FFHKLLRDAG LVNTNEPAKQ LLTQGMVLAD AFYYTNDKGA RVWVSPLDVA TTEKDDKGRI
TKAIDKDGNE LVYTGMCKMS KSKNNGIDPQ VMVEKYGADT VRLFMMFASP PELTLEWQES
GVEGAHRFIK RLWKLASEYV AQDNSEALDV SKLTSEQKAL RREVHKTIAK VTDDIGRRQM
FNTAVAAVME LMNHLQKAPQ TTGQDRAIIG EALSAVVRLL YPIIPHVSFT LWNELGNTNS
IEDSQWPVVD ESALVEDSKL IVVQVNGKVR AKITVAADAD QASVEALGMA DEQVIKYLDG
VTVRKVIYVP GKLLSIVAN
