ID A0A193GGM1_9BORD Unreviewed; 887 AA.
AC A0A193GGM1;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-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=BAU07_17875 {ECO:0000313|EMBL:ANN78738.1};
OS Bordetella flabilis.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=463014 {ECO:0000313|EMBL:ANN78738.1, ECO:0000313|Proteomes:UP000091926};
RN [1] {ECO:0000313|EMBL:ANN78738.1, ECO:0000313|Proteomes:UP000091926}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AU10664 {ECO:0000313|EMBL:ANN78738.1,
RC ECO:0000313|Proteomes:UP000091926};
RA LiPuma J.J., Spilker T.;
RT "Complete genome sequences of Bordetella bronchialis and Bordetella
RT flabilis.";
RL Submitted (JUN-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; CP016172; ANN78738.1; -; Genomic_DNA.
DR RefSeq; WP_066660303.1; NZ_CP016172.1.
DR AlphaFoldDB; A0A193GGM1; -.
DR STRING; 463014.BAU07_17875; -.
DR KEGG; bfz:BAU07_17875; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000091926; 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 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; 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}.
FT DOMAIN 44..177
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 228..421
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 435..590
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 723..849
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 48..58
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 639..643
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 642
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 887 AA; 99262 MW; 64EABF7E92D1ABD4 CRC64;
MQERYNPNAV ESTAQQAWRQ NDVYRVSEHA VNASGAEKPK FYACSMLPYP SGKLHMGHVR
NYTINDMMAR QLRMRGYNVL MPMGWDAFGM PAENAAIKSK VPPAKWTYDN IAYMKKQMQA
MGLAIDWSRE MSACDPAYYK WNQWLFLKML EKGIAYRKTQ VVNWDPVDQT VLANEQVIDG
RGWRSGALVE KREIPGYYLR ITDYAEELLE QVRTGLPGWP ERVRLMQENW IGKSEGVRFA
FPHAIRDESG QLVQDGRLYV FTTRADTIMG VTFCAVAPEH PLAALAARDN PALAEFIERC
KLGGTTEAEL ATREKEGMPT GLAVTHPLTG LPVDVWVGNY VLMSYGDGAV MGVPAHDERD
FAFARKYGLE IRQVVDVAGK DYSTDAWQEW YADKQSGRLV HSGKYDGLSS KQAIDAIAAD
LSGQGLGEKQ TTWRLRDWGI SRQRYWGTPI PIIHCDDCGP VPVPEKDLPV VLPEDLIPDG
SGNPLARNEA FLSCACPRCG KPARRETDTM DTFVDSAWYF MRYTSPGNDN AMVDDRNDYW
MPMDQYIGGI EHAVLHLLYA RFWTKVMRDL GMVKFDEPFT RLLCQGMVLN HIYSRKTEHG
GIEYFWPEEV ENVYDAKGAI TGARRKSDGS EVSYGGVGTM SKSKNNGVDP QSLIDTLGAD
TARLFVMFAS PPEQTLEWSD SGVEGANRFL RRLWSHACGQ RDAVQRGLAA AASAWQDAPA
AAKDLRREIH TLLKQADYDY QRIQYNTVVS ACMKMLNAIE SATLPDGDPL ADAARAESLG
VLLRVLYPVV PHITWQLWQE LGYAAVYGDL LDAPWPQVDE GALVADEIEL MLQVNGKLRG
ALRVAAAASR EQIEAQAATH EAVERFLEGR PPKRVIVVPG KLVNVVG
//
