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
//