SYL_SHEB8
ID SYL_SHEB8 Reviewed; 859 AA.
AC A6WRJ9;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAY-2008, sequence version 2.
DT 03-AUG-2022, entry version 86.
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};
GN OrderedLocusNames=Shew185_3311;
OS Shewanella baltica (strain OS185).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=402882;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OS185;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome of Shewanella baltica OS185.";
RL Submitted (JUL-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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=ABS09438.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000753; ABS09438.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_041411254.1; NC_009665.1.
DR AlphaFoldDB; A6WRJ9; -.
DR SMR; A6WRJ9; -.
DR KEGG; sbm:Shew185_3311; -.
DR HOGENOM; CLU_004427_0_0_6; -.
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.
FT CHAIN 1..859
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334814"
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; 96609 MW; 3CCCE1B601C99608 CRC64;
MQEQYNPSEI EALVQKHWHD NKTFEVTEDA NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVARFQRLQG KNVLQPIGWD SFGLPAENAA INNKTAPAPW TYENIEYMKN QLKLLGFGYD
WSREIATCTP EYYRWEQWFF TKLYEKGLVY KKTASVNWCP NDETVLANEQ VQDGCCWRCD
TPVEQKEIPQ WFIKITAYAE ELLNDIDTLD GWPEQVKTMQ RNWIGRSEGV EMTFGVAGHD
KSFDIYTTRP DTLMGVTYVA IAAGHPLAEI AAQTNPELAA FIDECKNSTT SEAELATMEK
RGVATGLFAI HPITGKQVPI WAANFVLMNY GTGAVMSVPG HDQRDFEFAK KYGLAIEAVI
KPVDGDVDIS EAAYTEKGVL FNSGEFDGLD FEAGFNAIAN KLVAEGKGKR QVNYRLRDWG
VSRQRYWGAP IPMVTLADGT VIPTPADQLP VLLPEDVVMD GIQSPIKADK EWAKTQVNGQ
DALRETDTFD TFMESSWYYA RYCSPHADEM LDPAKANYWL PVDQYIGGIE HACMHLLYFR
FFHKLLRDAG LVNSNEPAKQ LLTQGMVLAD AFYYINEKGA RVWVSPLDVA TTEKDDKGRI
TKAIDKDGNE LVYTGMSKMS KSKNNGIDPQ VMVEKYGADT VRLFMMFASP PELTLEWQES
GVEGAHRFIK RLWKLANEHV NQANSEALDV STLTSDQKAL RREVHKTIAK VTDDIGRRQM
FNTAVAAVME LMNHLQKAPQ TTGQDRAIIG EALSAIVRLL YPIIPHVSFN LWNELGNASN
IEDSQWPVVD EAALVEDSKL IVVQVNGKVR AKITVAADAD KESVEALGMS DEHVIKYLDG
LTVRKVIYVP GKLLSIVAN