ID A0A0C4Y682_9BURK Unreviewed; 899 AA.
AC A0A0C4Y682;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=RR42_m3571 {ECO:0000313|EMBL:AJG20937.1};
OS Cupriavidus basilensis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=68895 {ECO:0000313|EMBL:AJG20937.1, ECO:0000313|Proteomes:UP000031843};
RN [1] {ECO:0000313|EMBL:AJG20937.1, ECO:0000313|Proteomes:UP000031843}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=4G11 {ECO:0000313|EMBL:AJG20937.1};
RX PubMed=25977418;
RA Ray J., Waters R.J., Skerker J.M., Kuehl J.V., Price M.N., Huang J.,
RA Chakraborty R., Arkin A.P., Deutschbauer A.;
RT "Complete Genome Sequence of Cupriavidus basilensis 4G11, Isolated from the
RT Oak Ridge Field Research Center Site.";
RL Genome Announc. 3:0-0(2015).
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; CP010536; AJG20937.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C4Y682; -.
DR STRING; 68895.RR42_m3571; -.
DR KEGG; cbw:RR42_m3571; -.
DR Proteomes; UP000031843; Chromosome main.
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 CDD; cd00812; LeuRS_core; 1.
DR Gene3D; 2.20.28.290; -; 1.
DR Gene3D; 3.10.20.590; -; 1.
DR Gene3D; 3.40.50.620; HUPs; 2.
DR Gene3D; 3.90.740.10; Valyl/Leucyl/Isoleucyl-tRNA synthetase, editing domain; 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 NCBIfam; TIGR00396; leuS_bact; 1.
DR PANTHER; PTHR43740:SF2; LEUCINE--TRNA LIGASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; 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:UP000031843}.
FT DOMAIN 36..238
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 247..443
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 458..613
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 660..700
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 739..859
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 69..79
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 661..665
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 664
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 899 AA; 99647 MW; 41CC8827F7EFD680 CRC64;
MPAAYLFHAF RTPTHRAVVL NMQDKYLPSA VEQAAQQHWQ AIDAYRVSEE AKLADGSEKP
KFYACSMLPY PSGKLHMGHV RNYTINDMMA RHLRMNGHNV LMPMGWDAFG MPAENAALNN
GVAPAAWTYN NIAEMKRQMQ SMGLAIDWSR EVATCSPDYY RWNQWLFLKM LEKGIAYRKT
GTVNWDPVDQ TVLANEQVID GRGWRSGALV EKREIPMYYL RITDYAEELL GDLDDLGWPE
RVKIMQQNWI GKSVGVRFGF THAIAGDDGK LIGDGKLYVF TTRADTIMGV TFCAVAAEHP
LATHAAATNP ELAAFINECK HGSVMEADMA TMEKKGMPTG LKVVHPLTGE QVEVWVGNYV
LMSYGDGAVM GVPAHDERDF AFANKYGLPI KQVVDMVDAK KGQPFSTEAW QEWYGDKEHG
TCIHSGKYDG LDYKAAVEAI AADLGAKGLG EKKITWRLRD WGISRQRYWG TPIPLIHCDG
CGVVPVPEQD LPVVLPEDLV PDGTGNPLAK DPRFLACTCP SCGKPARRET DTMDTFIDSC
WYYMRYTCPD AATMVDARND YWMPMDQYIG GIEHAILHLL YARFWTKVMR DMGLVTFNEP
FSNLLTQGMV LNDTYYREDA AGKKTWYNPA EVDVSTDERG RPLGAVLKAD GQPVVIGGVE
KMSKSKNNGI DPQALIDQYG ADTARLFVMF AAPPEQQLEW SGSGVEGASR FLRRVWNYGY
ANAEAIAAAG NAVPSGDADA ALRREIHGVL KQANYDYQRI QYNTVVSATM KMLNALEDAK
QATPAARREG LGILLRVLYP VVPHITHGLW QELGYATQYG DLLDAAWPQV DESALVQSEL
DLVLQINGKV RGSLKVPAVA DRAAIEAMAA ASEIVARFAE GAAPKKIVVV PGRLVNVVL
//
