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Database: UniProt
Entry: A0A162N0E6_9BURK
LinkDB: A0A162N0E6_9BURK
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ID   A0A162N0E6_9BURK        Unreviewed;       920 AA.
AC   A0A162N0E6;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 40.
DE   RecName: Full=Leucine--tRNA ligase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            EC=6.1.1.4 {ECO:0000256|HAMAP-Rule:MF_00049};
DE   AltName: Full=Leucyl-tRNA synthetase {ECO:0000256|HAMAP-Rule:MF_00049};
DE            Short=LeuRS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   Name=leuS {ECO:0000256|HAMAP-Rule:MF_00049};
GN   ORFNames=LPB072_02430 {ECO:0000313|EMBL:AOW11892.1};
OS   Hydrogenophaga crassostreae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Hydrogenophaga.
OX   NCBI_TaxID=1763535 {ECO:0000313|EMBL:AOW11892.1, ECO:0000313|Proteomes:UP000185680};
RN   [1] {ECO:0000313|EMBL:AOW11892.1, ECO:0000313|Proteomes:UP000185680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LPB0072 {ECO:0000313|EMBL:AOW11892.1,
RC   ECO:0000313|Proteomes:UP000185680};
RA   Kim E., Yi H.;
RT   "Hydorgenophaga sp. LPB0072 isolated from gastropod.";
RL   Submitted (OCT-2016) 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:0000256|ARBA:ARBA00001372, ECO:0000256|HAMAP-
CC         Rule:MF_00049};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00049}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC       {ECO:0000256|ARBA:ARBA00005594, ECO:0000256|HAMAP-Rule:MF_00049,
CC       ECO:0000256|RuleBase:RU363035}.
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DR   EMBL; CP017476; AOW11892.1; -; Genomic_DNA.
DR   RefSeq; WP_066085060.1; NZ_LVWD01000002.1.
DR   AlphaFoldDB; A0A162N0E6; -.
DR   STRING; 1763535.LPB072_02430; -.
DR   KEGG; hyl:LPB072_02430; -.
DR   OrthoDB; 9810365at2; -.
DR   Proteomes; UP000185680; 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   CDD; cd07958; Anticodon_Ia_Leu_BEm; 1.
DR   Gene3D; 2.20.28.290; -; 1.
DR   Gene3D; 3.10.20.590; -; 1.
DR   Gene3D; 3.40.50.620; HUPs; 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   NCBIfam; TIGR00396; leuS_bact; 1.
DR   PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL-RELATED; 1.
DR   PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 1.
DR   Pfam; PF08264; Anticodon_1; 1.
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; Anticodon-binding domain of a subclass of class I aminoacyl-tRNA synthetases; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF50677; ValRS/IleRS/LeuRS editing domain; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146,
KW   ECO:0000256|HAMAP-Rule:MF_00049};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000256|HAMAP-Rule:MF_00049};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00049};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00049}; Reference proteome {ECO:0000313|Proteomes:UP000185680}.
FT   DOMAIN          38..120
FT                   /note="Methionyl/Leucyl tRNA synthetase"
FT                   /evidence="ECO:0000259|Pfam:PF09334"
FT   DOMAIN          245..437
FT                   /note="Leucyl-tRNA synthetase editing"
FT                   /evidence="ECO:0000259|Pfam:PF13603"
FT   DOMAIN          673..706
FT                   /note="Aminoacyl-tRNA synthetase class Ia"
FT                   /evidence="ECO:0000259|Pfam:PF00133"
FT   DOMAIN          759..884
FT                   /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT                   anticodon-binding"
FT                   /evidence="ECO:0000259|Pfam:PF08264"
FT   MOTIF           42..52
FT                   /note="'HIGH' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   MOTIF           673..677
FT                   /note="'KMSKS' region"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT   BINDING         676
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ   SEQUENCE   920 AA;  101490 MW;  48EE7122DF4841AB CRC64;
     MQSTYAHKDV ERAAHAHWNA TDAYRVTEDS GKKKFYACSM LPYPSGKLHM GHVRNYTIND
     MLTRYLRMNG HNVLMPMGWD AFGLPAENAA LKNGVPPAKW THENIAYMKK QMQAMGLAVD
     WSREIATCDP TYYKWNQWLF LQMLKMPVKG IDGHPLMDEQ GEPVTVAYRK TQVVNWDPVD
     QTVLANEQVI DGKGWRTGAV VEKREIPGYY LNITSYAEEL LEHVQLGNPK ATLNGWPDKV
     RLMQENWIGK SEGVRFAFPH EIKDASGALI GDGKMYVFTT RADTIMGVTF CAVAPEHPLA
     MHAAASNPEL VAFIEECKSG GTTEAELATQ EKKGMKTGLT VTHPLTGAAV DVWVGNYVLM
     SYGDGAVMGV PAHDERDFSF ALKYGIEIKQ VVAVEGEAFS LTEWADWYGD KQRGACVNSG
     ALNGLNTKAA VDKVAELMAA KDLGEKKTTF RLRDWGVSRQ RYWGTPIPII HCDEHGAVPV
     PEKDLPVVLP QDCIPDGSGN PLNKHEGFHA GVVCPVCGKA ARRETDTMDT FVDSSWYFMR
     YCDPSNSEKM VADGADYWMR DQDAAIGGSG MDQYIGGVEH AILHLLYARF WTKVMRDLGL
     VKIDEPFTKL LTQGMVLNHI YSRRTDKGGK DYFWPADVEH VLDDAGKVVG AKLVKAVGDL
     PVGTAIDYEG VGTMSKSKNN GVDPQDLIER YGADTARLYT MFTAPPEATL EWNDAAVEGS
     YRFLRRVWGF GHKLSTQSGL GEAAASVSKQ TLSKPAKALR LEIHTVLKQV DYDYQRMQYN
     TVVSGAMKML NALEDFKPDG SAGDTAAVAE CFGLLLRCIY PATPHLAHQL WRDLGYAPQW
     GDLLDAPWPQ PDDAALKREE LELVLQINGK LRGSITVPAS ADKAAIEAAA LASEAFVKQA
     DGAAPKKVIV VPGRLVNVVV
//
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