SYL_ALIB4
ID SYL_ALIB4 Reviewed; 821 AA.
AC A8ERV3;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 87.
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=Abu_0402;
OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Aliarcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the Epsilonproteobacterium
RT Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV66677.1; -; Genomic_DNA.
DR RefSeq; WP_012012229.1; NC_009850.1.
DR AlphaFoldDB; A8ERV3; -.
DR SMR; A8ERV3; -.
DR STRING; 367737.Abu_0402; -.
DR EnsemblBacteria; ABV66677; ABV66677; Abu_0402.
DR KEGG; abu:Abu_0402; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_7; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000001136; 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; IPR015413; Methionyl/Leucyl_tRNA_Synth.
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; 2.
DR Pfam; PF00133; tRNA-synt_1; 1.
DR Pfam; PF13603; tRNA-synt_1_2; 1.
DR Pfam; PF09334; tRNA-synt_1g; 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..821
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000057341"
FT MOTIF 40..50
FT /note="'HIGH' region"
FT MOTIF 586..590
FT /note="'KMSKS' region"
FT BINDING 589
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 821 AA; 94469 MW; C1F899A1C28CB234 CRC64;
MEYISKDIEK KWQNFWSENQ SFEPSSSKTK EKKYILSMFP YPSGRIHMGH VRNYCIGDAF
ARHFRKSDFN VLHPIGWDSF GMPAENAAIK HKLHPKKWTY ENIDYMRDEL KSLGLSFSKN
REFATSDELY TKWEQEFIIK MYEAGIIYRK SATVNWCPHD QTVLANEQLE EGCCWRCGTE
VVQKEMPGYY IGITKYAQEL LDDLEKLKED WPSQVLTMQE NWIGRSEGLE FKFDLSKESR
AKLERAFTKY FVFTTRPDTI YGVSYSALAP EHPIVKYIVE KNLLPEKKIK AIKAMQKIPE
RDRATQEKEG IDLEIEVMHP LTGKTIPVWV ANFVLSSYGG GAVMAVPAHD QRDFEFAKKY
NLPIKQVIVG PDGIIENQTE AYTAEGRLIE SENFTGVTNI EAKKAIIYHF EQNSFGIKKV
NYKLRDWGVS RQRYWGAPIP FIHCEKCGLV PEKIENLPVA LPEDVEITGE GNPLDTHPTW
KHCTCPKCGE KATRETDTLD TFVQSSWYFL RYATDNKKWN EVGISKEDSD YWMDVDQYIG
GIEHAILHLL YARFFTKVLR DLGYTNSSEP FKKLLTQGMV LKDGAKMSKS KGNVVDPDLI
IDKYGADTAR LFILFAAPPT KELEWNDSAV EGAFRFIKKF FERAENVNQN GLDNFKSIDH
SALSKEEKEA RKKVYEALLK SNEVFTKTYT FNTLIASCME ALNALQTQKN DSIWAEGYYI
LTNILEPIIP HACWELSKKL FDLKNFDGKI ELKEEVFALE SIILAVTVNG KKRCEIEVAP
DTSKDEILVK AKIASAKWLE NSEILKEIVV PNKLVNFVIK G
