ID A0A063BJ31_9BURK Unreviewed; 908 AA.
AC A0A063BJ31;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
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=LIG30_0734 {ECO:0000313|EMBL:KDB10391.1};
OS Burkholderia sp. lig30.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB10391.1, ECO:0000313|Proteomes:UP000027020};
RN [1] {ECO:0000313|EMBL:KDB10391.1, ECO:0000313|Proteomes:UP000027020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA Brown S.D., Hazen T.C.;
RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT Isolated from Wet Tropical Forest Soil.";
RL Submitted (MAR-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDB10391.1}.
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DR EMBL; JGVW01000022; KDB10391.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A063BJ31; -.
DR STRING; 1192124.LIG30_0734; -.
DR PATRIC; fig|1192124.4.peg.368; -.
DR eggNOG; COG0495; Bacteria.
DR Proteomes; UP000027020; Unassembled WGS sequence.
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; 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; 1.
DR PANTHER; PTHR43740; LEUCYL-TRNA SYNTHETASE; 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; 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:UP000027020}.
FT DOMAIN 82..215
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 264..451
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 465..620
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 667..707
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 748..871
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 86..96
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 668..672
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 671
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 908 AA; 101422 MW; A1D9CC9577215B23 CRC64;
MRLVTGRFPA AWHPRPPDKR DFRSTPVCVR AVAARRLKPS PNHTMHERYV PADVEAAAQR
DWRAADAYKT KEDTQKPKFY CVSMLPYPSG KLHMGHVRNY TINDVMYRYL RMNGYNTLMP
MGWDAFGMPA ENAAMANGVP PAKWTYDNID YMKGQMQSMG LAIDWSREIA TCKPDYYKWN
QWLFLKMLEK GIAYKKTGTV NWDPIDQTVL ANEQVIDGRG WRSGALVEKR EIPMYYLRIT
QYADELLNDL DGLGWPERVK IMQQNWIGKS FGVNFGFPYE LDGEQTLLRV FTTRADTIMG
VTFCAIAAEH PLATRLAKDK PELLAFIDEC KRGGVAEADM ATMEKKGVPT GFTVTHPLTN
EPVEVWIGNY VLMSYGEGAV MGVPAHDERD FAFAKKYDLP IKQVIAAEGE TYSTDAWQEW
YGDKDAAACV NSGKYDGLRY GEAVDAIAAD LKAGGFGDKQ VTWRLRDWGV SRQRYWGTPI
PIIHCPSCGD VPVPEQDLPV VLPEDLVPDG SGNPLAKSDA FMNCTCPKCG AAAKRETDTM
DTFVDSSWYF SRYTAPDADT MVDARTDYWM PMDQYIGGIE HAILHLLYSR FWTKVMRDLG
LVKFGEPAKN LLTQGMVLNE TFYREEASGK KTWYNPADVT VAFDEKGRPV GATLNADGQP
VVLGGIEKMS KSKNNGVDPQ VLIDQYGADT ARLFTMFAAP PEQQLEWSGA GVEGASRFLR
RVWSFGAANR EALAERAAFD AARLGDADKA LRREIYSVLK QADFDYQRLQ YNTVVSATMK
MLNAIDGAKG ATPAVLREAY GVLLRVLYPV VPHITFELWK ALGYVDAFGP LLDAPWPKVD
EAALEQAEIE LVLQINGKVR GALKVAKDAS RDAIEAAAVA DEMFAKFGEG RPAKKIVVVP
GRLVNIVV
//
