SYL_AZOVD
ID SYL_AZOVD Reviewed; 870 AA.
AC C1DMV9;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 26-MAY-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=Avin_09000;
OS Azotobacter vinelandii (strain DJ / ATCC BAA-1303).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=322710;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DJ / ATCC BAA-1303;
RX PubMed=19429624; DOI=10.1128/jb.00504-09;
RA Setubal J.C., Dos Santos P., Goldman B.S., Ertesvaag H., Espin G.,
RA Rubio L.M., Valla S., Almeida N.F., Balasubramanian D., Cromes L.,
RA Curatti L., Du Z., Godsy E., Goodner B., Hellner-Burris K., Hernandez J.A.,
RA Houmiel K., Imperial J., Kennedy C., Larson T.J., Latreille P., Ligon L.S.,
RA Lu J., Maerk M., Miller N.M., Norton S., O'Carroll I.P., Paulsen I.,
RA Raulfs E.C., Roemer R., Rosser J., Segura D., Slater S., Stricklin S.L.,
RA Studholme D.J., Sun J., Viana C.J., Wallin E., Wang B., Wheeler C., Zhu H.,
RA Dean D.R., Dixon R., Wood D.;
RT "Genome sequence of Azotobacter vinelandii, an obligate aerobe specialized
RT to support diverse anaerobic metabolic processes.";
RL J. Bacteriol. 191:4534-4545(2009).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP001157; ACO77139.1; -; Genomic_DNA.
DR RefSeq; WP_012699564.1; NC_012560.1.
DR AlphaFoldDB; C1DMV9; -.
DR SMR; C1DMV9; -.
DR STRING; 322710.Avin_09000; -.
DR PRIDE; C1DMV9; -.
DR EnsemblBacteria; ACO77139; ACO77139; Avin_09000.
DR KEGG; avn:Avin_09000; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_6; -.
DR OMA; TFMVLAP; -.
DR OrthoDB; 32262at2; -.
DR Proteomes; UP000002424; 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; 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; 1.
DR Pfam; PF08264; Anticodon_1; 1.
DR Pfam; PF00133; tRNA-synt_1; 2.
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.
FT CHAIN 1..870
FT /note="Leucine--tRNA ligase"
FT /id="PRO_1000202216"
FT MOTIF 42..52
FT /note="'HIGH' region"
FT MOTIF 629..633
FT /note="'KMSKS' region"
FT BINDING 632
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 870 AA; 96892 MW; BD4A1F5526161760 CRC64;
MHEQYQPREI EAAAQSIWDA QKSFEVREQP GKDTFYCLSM FPYPSGKLHM GHVRNYTIGD
VIARYQRMQG RNVLQPMGWD AFGMPAENAA MKNRVAPAKW TYENIAYMKS QLKSLGLGID
WSREVTTCKP DYYRWEQWLF TRLFEKGVIY RKNGTVNWDP VDQTVLANEQ VIDGRGWRSG
ALVEKREIPM YYFRITAYAE ELLQSLDSLP GWPEQVKTMQ RNWIGKSYGA DIVFDYDQAS
VGEAGQLRVY STRPDTLMGA TYVAVAAEHP LAQRAAANDP ALAAFIAECK AGSVAEADMA
TMEKKGLATG QFVVHPLTGD RLPVFVANYV LWGYGEGAVM AVPAHDERDF EFANKYGLPI
RQVYAAEGRD FSASEWQAWY ADKEGLTTVD SGKYDGKSFT EAFDAIVADL EATGHGARKT
QFRLRDWGIS RQRYWGCPIP IIHCEACGDV PVPEEQLPVV LPEDVVPDGT GSPLAKMPEF
YECACPKCGK PAKRETDTMD TFVESSWYYA RYASPQYAGG MVDPQAADHW LPVDQYIGGI
EHAILHLLYA RFFHKLMRDE GLLSSDEPFE NLLTQGMVVA ETYYRTLENG GKDWFNPADV
EVERDARAKV IGARLKSDGL PVEIGGTEKM SKSKNNGVDP QAMIDAYGAD TCRLFMMFAA
PPELSLEWSD AGVEGASRFL RRVWRLAHAH VGAGLPGTLD KARLSDAQKE IRRAIHLAIR
QASQDVGQHH KFNTAIAQVM TLMNVLEKAP AADEQDRALL QEGLETVALL LAPITPHICH
ALWEALGKDG LIIDAAWPTV DETALVQDTL TLVVQVNGKL RGEIQVPAAA SREEIEAAAR
ANENVLRFTE GLAIRKVIVV PGKLVNIVAN
