ID E0XRT9_9GAMM Unreviewed; 793 AA.
AC E0XRT9;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 66.
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};
OS uncultured gamma proteobacterium HF0070_03O15.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; environmental samples.
OX NCBI_TaxID=710982 {ECO:0000313|EMBL:ADI17130.1};
RN [1] {ECO:0000313|EMBL:ADI17130.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20695878; DOI=10.1111/j.1462-2920.2010.02314.x;
RA Rich V.I., Pham V.D., Eppley J., Shi Y., DeLong E.F.;
RT "Time-series analyses of Monterey Bay coastal microbial picoplankton using
RT a 'genome proxy' microarray.";
RL Environ. Microbiol. 13:116-134(2011).
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; GU474854; ADI17130.1; -; Genomic_DNA.
DR AlphaFoldDB; E0XRT9; -.
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; 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 39..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 220..395
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 408..596
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 634..754
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 557..561
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 560
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 793 AA; 91731 MW; C2373F64474FEBF2 CRC64;
MKIEYDHSKI EKDIQSKWNE SNAFTAKIDN KKPKYYCLSM LPYPSGNLHM GHVRNYAIGD
AVSRYKRLKG FNVLQPMGWD AFGLPAENAA KGKNIHPKDW TEKNIENMRE QLKSLGFSYD
WSKELNTSDV SYYKFEQELF LKFYERGLAY RKKSLVNWDP VDETVLANEQ VIDGKGWRTG
AEVELKEIDT WFLKITDYAD ELEESLATID WPENVINMQK NWIGKSKGVE IKFTTDTNKE
IKAFTTRPDT IFGVTFFGIS PNHPIVNEIS KNDEGLIEFL SEVKKISSAE ADLAKAEKLG
YKTELNIIHP ITDEKIPVWI INYVLMDYGT GAIMGVPGHD ERDFEFAQKY EIPITRVIDS
KDELPYSGQG KLVNSKDFDG LNSVKAFDKV TKRLEKNNAA KILYQYRLRD WGISRQRYWG
CPIPIIYKDG KTMPSEELPV ELPVSADGKY SPLHQNEEFK KLDNGFERET DTFDTFMESS
WYFARYTSAT NDKEIFDENT KYWLPVDLYI GGVEHAILHL LYSRFFFKAL RDMDIVEGDE
PFKKLLTQGM VLKDGAKMSK SKGNTVDPKE YITKYGADSI RTFMIFASPP EQSLEWSDNG
LEGCHKFLKR LWNLSTNISE LDEKQFKDSK NQLTDECKKL FKKINDDYEK RLNLNTIVSS
CMEILNNING RFDDKNVNCS KEDLLNVYDF LLLALHPIAP HICETLYAEV LKKDIAQAEW
PEDSFFVADL SESNYLVQVN GKLRANIMMP IDLREDEVKE IALTNENVAR HLENKNIIKI
IFIKNKLINF VHS
//
