ID A0A9X2C3K7_9BURK Unreviewed; 881 AA.
AC A0A9X2C3K7;
DT 08-NOV-2023, integrated into UniProtKB/TrEMBL.
DT 08-NOV-2023, sequence version 1.
DT 28-JAN-2026, entry version 10.
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 ECO:0000313|EMBL:MCK9687680.1};
GN ORFNames=LPC04_18410 {ECO:0000313|EMBL:MCK9687680.1};
OS Scleromatobacter humisilvae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria;
OC Burkholderiales; Sphaerotilaceae; Scleromatobacter.
OX NCBI_TaxID=2897159 {ECO:0000313|EMBL:MCK9687680.1, ECO:0000313|Proteomes:UP001139353};
RN [1] {ECO:0000313|EMBL:MCK9687680.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=BS-T2-15 {ECO:0000313|EMBL:MCK9687680.1};
RA Mieszkin S., Alain K.;
RT "BS-T2-15 a new species belonging to the Comamonadaceae family isolated
RT from the soil of a French oak forest.";
RL Submitted (NOV-2021) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=tRNA(Leu) + L-leucine + ATP = L-leucyl-tRNA(Leu) + AMP +
CC diphosphate; 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:ARBA00047469, 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}.
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:MCK9687680.1}.
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DR EMBL; JAJLJH010000005; MCK9687680.1; -; Genomic_DNA.
DR RefSeq; WP_275683719.1; NZ_JAJLJH010000005.1.
DR AlphaFoldDB; A0A9X2C3K7; -.
DR Proteomes; UP001139353; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0002161; F:aminoacyl-tRNA deacylase 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 FunFam; 1.10.730.10:FF:000003; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000003; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000056; Leucine--tRNA ligase; 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; 1.10.730.10; Isoleucyl-tRNA Synthetase, Domain 1; 1.
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:UP001139353}.
FT DOMAIN 38..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 227..419
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 636..674
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 718..844
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 636..640
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 639
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 881 AA; 97563 MW; 03C620F067D094C7 CRC64;
MNEKYVPSEV EAAAQAHWRS TDAYRVSEDA SRAKFYACSM LPYPSGKLHM GHVRNYTIND
MLARQLRMKG MNVLMPMGWD AFGLPAENAA IKNKVPPAKW TYDNIAHMKE QMQAMGLAID
WSREVATCDP KYYKWNQWLF LKMLEAGICE RRTQIVNWDP VDMTVLANEQ VIDGHGWRSG
APVEKREIPG YYLNIVKYAE ELLSAVTNPE DPEYLSGWPE RVRLMQENWI GKSEGVRFAF
PHTIHDDTGA LIGDGKLYVF TTRADTIMGV TFCAVAPEHP LATHAAKGNP ALDAFIAAAK
AGGTTEAELA TREKEGLPTG LMVIHPLTGA QIPVWVGNYV LMSYGDGAVM GVPAHDERDF
AFARKYGLEI KQVVSVNGET FSTDAWQEWY GDKQRGVCIE SGALDGFGMK EAVSRVAELL
SAANLGEKKT TWRLRDWGVS RQRYWGTPIP IIHCDDCGVV PVPEKDLPVV LPEDLIPDGS
GNPLNKHAAF LNVGCPKCGK PAKRETDTMD TFVDSSWYFM RYCDPTNDDR MVAGGTDYWM
PMDQYIGGIE HAILHLLYAR FWTKVMRDLK LVKFSEPFKN LLTQGMVLKG AFFHKPEDAG
KNYYWEHDLD IERDAHGNVV SAKLKDGTPV SYEMTTMSKS KNNGVDPQAL IDRYGADTAR
LFVMFASPPE QTLEWNDSGV EGAHRFLKRV WAFGVKHGEA VKAAADGVAG LELSAPAKAL
RREVHVLLKQ VTYDYERMQY NTVVSGAMKL LNALEGFAMD GGAGSAAVLR EGFSVLLRAL
YPACPHITQG LWTDLGYAAT GKQLLDAGWP AVDESALVQD EIELVLQVLG KTRGSVLVPA
SADKAAIEAI AVASPEAVRW MEGKPARKVV VVPGRLVNIV V
//
