ID A0A0G3BCC9_9BURK Unreviewed; 890 AA.
AC A0A0G3BCC9;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=AAW51_0281 {ECO:0000313|EMBL:AKJ26972.1};
OS Caldimonas brevitalea.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Caldimonas.
OX NCBI_TaxID=413882 {ECO:0000313|EMBL:AKJ26972.1, ECO:0000313|Proteomes:UP000035352};
RN [1] {ECO:0000313|EMBL:AKJ26972.1, ECO:0000313|Proteomes:UP000035352}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7029 {ECO:0000313|EMBL:AKJ26972.1,
RC ECO:0000313|Proteomes:UP000035352};
RA Tang B., Yu Y.;
RL Submitted (MAY-2015) 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; CP011371; AKJ26972.1; -; Genomic_DNA.
DR RefSeq; WP_047193197.1; NZ_CP011371.1.
DR AlphaFoldDB; A0A0G3BCC9; -.
DR STRING; 413882.AAW51_0281; -.
DR KEGG; pbh:AAW51_0281; -.
DR PATRIC; fig|413882.6.peg.290; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000035352; 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 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:UP000035352}.
FT DOMAIN 42..175
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 226..419
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 433..588
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 638..675
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 724..854
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 46..56
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 637..641
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 640
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 890 AA; 100078 MW; 49C73F7AE0663538 CRC64;
MNTEHPNAYN PREVEPAAQA DWRARDAYRV VEDRSKKKFY ACSMLPYPSG KLHMGHVRNY
TINDMLARHL RMNGYNVLMP MGWDAFGLPA ENAALKNRVP PAQWTYDNIA YMKKQMQAMG
LAIDWSREVA TCDPSYYKWN QWLFLKMLEK GIAYRKTQVV NWDPVDQTVL ANEQVIDGRG
WRTGAPVEKR EIPGYYLKIT DYADELLDQV QHHLPGWPER VRLMQENWIG KSEGVRFAFR
HDIRDAGGQL IQDGKLYVFT TRADTIMGVT FCAVAPEHPL AQHAAAGNAA LAAFIEDCKK
GGTTEAELAL KEKEGQPTGL FVTHPLTGDQ VEVWVGNYVL MSYGDGAVMG VPAHDERDFA
FAKKYGLPIR QVVAVEGENY STDAWAEWYA DKQRGITINS GRYDGLRYKE AVDAIAAALA
ALGLGEKKTT WRLRDWGISR QRYWGTPIPI IHCHECGPVP VPEQDLPVVL PLDCVPDGSG
NPLNKRADFL NVACPKCGKP AQRETDTMDT FVDSSWYFMR YCDPTNEQQM VAGGAQYWMP
VDQYIGGIEH AILHLLYARF WTKVMRDLGL VTVDEPFTKL LTQGMVLNHI YSRRTDKGGV
EYFWPQEVEN QYDEHGKIVG AKLKQDGSPI DYGGVGTMSK SKNNGVDPQD LIDTYGADTA
RLFVMFASPP EQTLEWNDAG VEGAHRFLRR VWNYAQTHRE QIGEVLPEGL AAELIYAAAP
ADVKKLRREV HKLLQQASYD YERMQYNTVV SACMKLLNTL EGFDAQQHPD RHYASWAVHE
AVGILLRVLY PACPHLTHAL WQQLGYTAQY GDLLDAPWPH VDEAALVQDE IELMLQVNGK
LRGAVTVPAS ADKAAIEAAA LASPDFVKFA EGKPVKKVVI VPGRLVNVVV
//
