ID A0A0N9VAR5_9GAMM Unreviewed; 873 AA.
AC A0A0N9VAR5;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, 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=AOY20_01545 {ECO:0000313|EMBL:ALH94329.1};
OS Acinetobacter equi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=1324350 {ECO:0000313|EMBL:ALH94329.1, ECO:0000313|Proteomes:UP000064939};
RN [1] {ECO:0000313|EMBL:ALH94329.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114 {ECO:0000313|EMBL:ALH94329.1};
RX PubMed=26620413;
RA Poppel M.T., Skiebe E., Laue M., Bergmann H., Ebersberger I., Garn T.,
RA Fruth A., Baumgardt S., Busse H.J., Wilharm G.;
RT "Acinetobacter equi sp. nov. isolated from horse faeces.";
RL Int. J. Syst. Evol. Microbiol. 0:0-0(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; CP012808; ALH94329.1; -; Genomic_DNA.
DR RefSeq; WP_054580242.1; NZ_CP012808.1.
DR AlphaFoldDB; A0A0N9VAR5; -.
DR STRING; 1324350.AOY20_01545; -.
DR KEGG; aei:AOY20_01545; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000064939; 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 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; 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}; Reference proteome {ECO:0000313|Proteomes:UP000064939}.
FT DOMAIN 40..176
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 226..416
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 634..674
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 717..836
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 635..639
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 638
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 873 AA; 97829 MW; 4E2649E1360CB937 CRC64;
MTTHIDPEYQ ASAIEPTVQQ DWEARKAFKV ADTVEGPRRY ILSMFPYPSG KLHMGHVRNY
TIGDVISRFH RLKGETVLQP MGWDAFGLPA ENAAIAHQVA PAKWTFENID YMRNQLKKLG
LSIDWDREFA TCTPEYYRWE QWLFVQLYKK GLIYRKLSTV NWDPVDQTVL ANEQVENGRG
WRSGALVEKR DIPMYYFRIT DYAQELLDDL DTLKDGWPQQ VLTMQRNWIG RSQGMEITFP
SANPTVYADG LTVFTTRADT LMGVTYVAVA AEHPMALKAA ENNPELAAFI EECRMGSVAE
ADLATAEKKG MATGLSVKHP VTGEEVPVWI ANYVLMSYGS GAVMAVPSHD ERDFEFANKY
GLTIKQVIDA KGADDAEFSA TEWQEWYGSK EGKLVNSGEF DGLDFQGAFD AFLAKLEPQS
LANVKVQFRL RDWGVSRQRY WGCPIPMINC NTCGQVPVPE EQLPVVLPTD VVPDGSGNPL
NKMPEFYETT CPCCGGDARR ETDTLDTFVE SSWYYARYAS PDFTDGMVKP EAGQTWLPVN
QYIGGVEHAI LHLLYARFFH KLMRDEGVVQ GNEPFTNLLT QGMVLADTYY RESESGKKTW
FNPADIELER DEKGRITSAK YNGDGQDVIV GGQEKMSKSK NNGIDPQAII DQYGADTARV
FMMFAAPPDQ SLEWSDAGVE GSNRFLKRVW RLTTSFLEKG NNATNIDKAA LSTAAQDLRR
KTHETIQKVG DDIERRHAFN TAIAAMMELL NANNKFEAKD DNDVAVSRES ITTLLTLLAP
FAPHLSQTLL AQFGIELTAT QFPQVDESAL TRNTQTIVVQ VNGKLRGKLE VSVDASKDDI
LAQAKALPEV QQFLTGPTKK EIVVPNKLVN LVV
//
