SYL_VIBPA
ID SYL_VIBPA Reviewed; 857 AA.
AC Q87RQ0;
DT 23-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-MAY-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
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=VP0727;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
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; BA000031; BAC58990.1; -; Genomic_DNA.
DR RefSeq; NP_797106.1; NC_004603.1.
DR RefSeq; WP_005454506.1; NC_004603.1.
DR AlphaFoldDB; Q87RQ0; -.
DR SMR; Q87RQ0; -.
DR STRING; 223926.28805713; -.
DR EnsemblBacteria; BAC58990; BAC58990; BAC58990.
DR GeneID; 1188202; -.
DR KEGG; vpa:VP0727; -.
DR PATRIC; fig|223926.6.peg.696; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR Proteomes; UP000002493; Chromosome 1.
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 Gene3D; 3.90.740.10; -; 1.
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..857
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000152114"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 617..621
FT /note="'KMSKS' region"
FT BINDING 620
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 857 AA; 96654 MW; D84628AA1E5EE5EB CRC64;
MQEQYNPQDI EQKVQKHWDD NKTFVVSEDP NKEKFYCLSM FPYPSGRLHM GHVRNYTIGD
VVSRFQRLQG KNVMQPIGWD AFGLPAENAA VKNNTAPAPW TYENIEYMKN QLKLLGFGYD
WNREFATCTP EYYRWEQEFF TKLYEKGLVY KKTSSVNWCP NDQTVLANEQ VEDGCCWRCD
TPVEQKEIPQ WFIKITEYAQ ELLDDLDKLE GWPEMVKTMQ RNWIGRSEGV ELKFEVKGQQ
DLEVYTTRPD TLMGVTYVGI AAGHPLATLA AENNPELAAF IEECKNTKVA EAELATMEKK
GMATGLTAIH PLNGREVPVY VANFVLMDYG TGAVMAVPAH DQRDFEFATK YGLDIIPVIK
PADGSELDIS EAAYTEKGVL FDSGEFDGLE FQAAFDAIAA KLEAEGKGTK TVNFRLRDWG
VSRQRYWGAP IPMVTTEDGE VHPVPADQLP VILPEDVVMD GVTSPIKADK EWAKTTFNGE
PALRETDTFD TFMESSWYYA RYCSPQADDI LDPEKANYWL PVDQYIGGIE HACMHLLYSR
FFHKLLRDAG YVTSDEPFKQ LLCQGMVLAD AFYFENEKGG KEWVAPTDVA VERDGKGRII
SAKDNEGRDV THSGMIKMSK SKNNGIDPQE MVDKYGADTV RLFMMFASPA DMTLEWQESG
VEGANRFLKR VWKLVKEHAE KGAAEAVDTA ALSGEQKALR RDVHKTIAKV TDDIARRQTF
NTAIAAIMEL MNKLAKAPQE SAQDRAILDE ALKAVVTMLY PITPHISYEL WTALGESDID
NAAWPTFDEK ALVEDEKTIV VQVNGKLRAK LTVAADATKE QVEELGLNDE NVTKFTDGLT
IRKVIYVPGK LLNIVAN