ID A0A425W8L6_9FIRM Unreviewed; 803 AA.
AC A0A425W8L6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=DUD26_01075 {ECO:0000313|EMBL:RRF94060.1};
OS Eubacteriaceae bacterium.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae.
OX NCBI_TaxID=2049045 {ECO:0000313|EMBL:RRF94060.1, ECO:0000313|Proteomes:UP000285774};
RN [1] {ECO:0000313|EMBL:RRF94060.1, ECO:0000313|Proteomes:UP000285774}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EUB1 {ECO:0000313|EMBL:RRF94060.1};
RA Scarborough M.J., Lawson C.E., Hamilton J., Donohue T.J., Noguera D.R.;
RT "Metatranscriptomic and thermodynamic insights into medium-chain fatty acid
RT production using an anaerobic microbiome.";
RL Submitted (JUL-2018) 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00049}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RRF94060.1}.
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DR EMBL; QOUT01000001; RRF94060.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A425W8L6; -.
DR Proteomes; UP000285774; Unassembled WGS sequence.
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; 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; 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 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.
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}; Cytoplasm {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:UP000285774}.
FT DOMAIN 12..218
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 220..403
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 417..614
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 653..765
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 581..585
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 584
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 803 AA; 92617 MW; C331DB4BC9206B0D CRC64;
MEKYNHEKVE KKWQKIWENT EAFKAEDNFD KPKFYGLVEF PYPSGVGLHV GHVRAYTSLE
VIARKRRMQG YNVLFPIGFD AYGLPTENYA IKTGQHPRKV TDRNIKVFTQ QLKSIGYSFD
WDRVIDTTDP DYFKWTQWIF LQMYKHGLAY KDHTYVNFCT HCKVVLSNED FRDGKCDRCG
SDVIQMEKDV WFLKIRDYAE KLLKGLDDVD YLPRIKIEQK NWIGKSIGAE IDFAIKNHDE
KLKVFTTRAD TLFGVTFMVI APEHPIIEEL SSEIKNMDEI LDYKKEAQHK TEFERVQLVK
DKTGVKIDGI TAVNPVSGKE IPIFVADYVM MGYGTGAIMA VPAHDTRDWD FAKKFDLPII
EVISGGNVQE EAFTDVSSGT LVNSEFLNGL EVKEAIPTMI QYLEEHHIGK ETINYKMKNW
AFNRQRYWGE PIPIVYCDHC GTVPVPEEDL PVELPKVTHY EPTDTGESPL ADIPEWVNTT
CPICGGPAKR ETDTMPQWAG SSWYFLRYTD PHNTEALADM DKMKYWLPVD WYNGGMEHVT
RHLLYSRFWH QFLYDIGAVP TKEPYKKRTA QGLILGSDGE KMSKSKGNVV NPNDIINEYG
ADALRTYIMF IGDYEKPAPW SENGLKGCNR FLERVWRLQD AVVDKNEYSD VLESDMHKTI
KKVSEDYEAM KFNTAIAALM TLLNRFTEVG KVTKAEFGDF LKLLYPVAPH ITEELWKIIG
QPGMLHQASW PTFDEEKTID NVIEIAVQIN GKVRGKIQIA IDADQETAHN MALQNENINK
FVENKQIVKE IYRPGKIYNI VVK
//
