ID A0A317MRJ2_9GAMM Unreviewed; 865 AA.
AC A0A317MRJ2;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 18-JUN-2025, entry version 24.
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=C7443_111108 {ECO:0000313|EMBL:PWV59336.1};
OS Plasticicumulans acidivorans.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Candidatus Competibacteraceae; Plasticicumulans.
OX NCBI_TaxID=886464 {ECO:0000313|EMBL:PWV59336.1, ECO:0000313|Proteomes:UP000246569};
RN [1] {ECO:0000313|EMBL:PWV59336.1, ECO:0000313|Proteomes:UP000246569}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23606 {ECO:0000313|EMBL:PWV59336.1,
RC ECO:0000313|Proteomes:UP000246569};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (MAY-2018) 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:PWV59336.1}.
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DR EMBL; QGTJ01000011; PWV59336.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A317MRJ2; -.
DR Proteomes; UP000246569; 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; 2.20.28.290:FF:000001; Leucine--tRNA ligase; 1.
DR FunFam; 3.10.20.590:FF:000001; 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 FunFam; 3.90.740.10:FF:000012; 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; 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; 2.
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:UP000246569}.
FT DOMAIN 43..175
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 225..408
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 423..578
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 625..661
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 709..830
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 626..630
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 629
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 865 AA; 96251 MW; 2FCAE42DA7E827E7 CRC64;
MTDVIDESYQ PQATEAAAQR FWNEHRSFEV AEDPAKEKFY CLSMFPYPSG RLHMGHVRNY
TIGDVIARYQ RMLGKNVLQP MGWDAFGMPA ENAALKHRVA PAKWTYENIE HMRGQLKALG
LGIDWSREVA TCTPEYYRWE QWLFTKLFEK GVIYRRNGVV NWDPVDQTVL ANEQVIDGRG
WRSGALVERR EIPMYYFRIT QYADELLAAL DELPGWPEQV KTMQRNWIGK SRGMEVHFPR
VGAEGVLKVY TTRPDTLMGA TYVAVAAEHP LALEAAVGNA ELGAFIDECR KGGVAEADIA
TQEKKGLPTG LYVRHPFSGR ELPVWVANYV LMGYGEGAVM AVPAHDARDF EFALKHELPI
EPVIRTSAGD STPAPWQEAY AEHGILINSG AFDGLDFDGA FERMAQVLAE QGLGAPRTQF
RLRDWGISRQ RYWGCPIPVV HCADCGDLPV PEDQLPVVLP ESVVPDGSGN PLAKMPEFYE
TTCPRCGKPA RRETDTMDTF VESSWYFARY ASADCTQGMV DERAAYWLPV DQYVGGIEHA
ILHLLYSRFF TKLMRDEGLL AVDEPFTRLL TQGMVIAETY FREDEAGRKN WFNPAEVKVE
RDGKGRITSA VLPADGQPVQ FGGIEKMSKS KNNGIDPQSL IDGQGADTAR LFMMFAAPPD
ASLEWSDAGV EGAARFLKRL WGFAYEHQTL LHAHPVVDVA RLDATLKAAR REIHEALAQA
LFDYGRQQFN TVVSAGMKML NTLAKLPAGA AADALRAEGY SILLRVLAPV VPHITHVLWQ
ALGWGEAIID ASLPQPDAAA LVRDSITLAV QVNGKLRAQI EVPADAAREV IEASALAEDN
VQRFMEGKPV KKLIIVPGKL VNIVC
//
