ID C5AAZ9_BURGB Unreviewed; 864 AA.
AC C5AAZ9;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 99.
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 OrderedLocusNames=bglu_1g05460 {ECO:0000313|EMBL:ACR27742.1};
OS Burkholderia glumae (strain BGR1).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=626418 {ECO:0000313|EMBL:ACR27742.1, ECO:0000313|Proteomes:UP000002187};
RN [1] {ECO:0000313|EMBL:ACR27742.1, ECO:0000313|Proteomes:UP000002187}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGR1 {ECO:0000313|EMBL:ACR27742.1,
RC ECO:0000313|Proteomes:UP000002187};
RX PubMed=19329631; DOI=10.1128/JB.00349-09;
RA Lim J., Lee T.H., Nahm B.H., Choi Y.D., Kim M., Hwang I.;
RT "Complete genome sequence of Burkholderia glumae BGR1.";
RL J. Bacteriol. 191:3758-3759(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: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; CP001503; ACR27742.1; -; Genomic_DNA.
DR RefSeq; WP_012734632.1; NC_012724.2.
DR AlphaFoldDB; C5AAZ9; -.
DR STRING; 626418.bglu_1g05460; -.
DR KEGG; bgl:bglu_1g05460; -.
DR PATRIC; fig|626418.3.peg.3300; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_4; -.
DR Proteomes; UP000002187; Chromosome 1.
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:UP000002187}.
FT DOMAIN 38..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 220..407
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 421..576
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 623..663
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 705..827
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 624..628
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 627
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 864 AA; 95699 MW; A1E8F42B0BA35BF7 CRC64;
MQERYVPADV EAAAQRDWRD ADAYLTKEDS QKPKFYCVSM LPYPSGKLHM GHVRNYTIND
VMYRYLRMNG YNTLMPMGWD AFGMPAENAA MANGVPPAKW TYDNIAYMKR QMQAMGLAID
WSREIATCNP DYYKWNQWLF LKMLEKGIAY KKTGTVNWDP VDQTVLANEQ VIDGRGWRSG
AVVEKREIPM YYLRITQYAD ELLDDLEGLG WPERVKVMQQ NWIGKSFGVN FGFPYELDGE
QKLLRVFTTR ADTIMGVTFC AVAAEHPLAT RLAEGRPELL AFIDECKQGG VAEADMATME
KKGMATGFSV KHPLTGEPVP VWIGNYVLMS YGEGAVMGVP AHDERDFAFA AKYGLPIKQV
IAAEGETYST DAWQEWYGDK TKGVCVNSGK YDGLGHEAAV DAVAADLAAG GFGDKQVTWR
LRDWGVSRQR YWGTPIPIIH CPSCGDVPVP EADLPVVLPE DLVPDGSGNP LAKSEAFVNC
TCPKCGAAAK RETDTMDTFV DSSWYFSRYT APDAATMVAA RTDHWMPMDQ YIGGIEHAIL
HLLYSRFWTK VMRDLGLVKF GEPAKNLLTQ GMVLNETFYR EDATGKKTWF NPADVTVTHD
DKGRPVGAVH NADGQPVVLG GIEKMSKSKN NGVDPQVLID QHGADTARLF TMFAAPPEQQ
LEWSGAGVEG ASRFLRRVWA FGAAHREALA VRAGFDAAQL DEGARALRRE IHGVLRQADF
DYQRLQYNTV VSAAMKMLNA IEAAKAAPAG VLRETYGILL RVLYPVVPHI TFALWQALGY
ADEFGTLLDA PWPKVDEAAL EQAEIELVLQ INGKVRGAIK VAKDAGRDVI EAAALADESF
AKFGEGKPAK KVIVVPGRLV NVVV
//
