ID A0A2U8WT40_9HYPH Unreviewed; 863 AA.
AC A0A2U8WT40;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 18-JUN-2025, entry version 27.
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=DK419_20230 {ECO:0000313|EMBL:AWN48392.1};
OS Methylobacterium terrae.
OC Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC Hyphomicrobiales; Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=2202827 {ECO:0000313|EMBL:AWN48392.1, ECO:0000313|Proteomes:UP000245444};
RN [1] {ECO:0000313|EMBL:AWN48392.1, ECO:0000313|Proteomes:UP000245444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17Sr1-28 {ECO:0000313|EMBL:AWN48392.1,
RC ECO:0000313|Proteomes:UP000245444};
RA Srinivasan S.;
RT "Complete Genome Sequence of Methylobacterium sp. 17Sr1-28.";
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}.
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DR EMBL; CP029553; AWN48392.1; -; Genomic_DNA.
DR RefSeq; WP_109960681.1; NZ_CP029553.1.
DR AlphaFoldDB; A0A2U8WT40; -.
DR KEGG; mtea:DK419_20230; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000245444; Chromosome.
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:000002; Leucine--tRNA ligase; 1.
DR FunFam; 3.40.50.620:FF:000003; 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; 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:UP000245444}.
FT DOMAIN 37..171
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 221..410
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 430..587
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 627..666
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 704..825
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 628..632
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 631
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 863 AA; 96456 MW; F75489A425AA5F77 CRC64;
MAERYNAKDS EPHWQQVWAE REIFRTRNDD PRPKYYVLEM FPYPSGRIHM GHVRNYAMGD
VVARYKRAKG FNVLHPMGWD AFGLPAENAA MQNKVNPRDW TYANIATMRA QLQSMGLSLD
WSREIATCDP EYYKHQQRMF LDFLQAGLVS RRTAKVNWDP VDHTVLANEQ VIDGRGWRSG
AFVEQRELTQ WFFKITDFAQ DLDDRLDTLE RWPEKVRLMQ RNWIGRSEGL ELRFALESAP
EGAARDVTVY TTRPDTLFGA KFLAVAADHP LAAAVAADNP ALQDFIAECR RMGTAQAAID
TAEKLGFDTG LEVRHPLDPS WTLPVYVANF VLMEYGTGAV FGCPAHDQRD LDFANKYALG
NTPVVCPPDQ DPAAFTITDT AYDGDGRMIN SRFLDGMSTD EAFKAVADRL KAETLDGGVM
GRRRVQFRLR DWGVSRQRYW GCPIPVIHCD ACGVVPVPVA DLPVRLPEEV SFDVPGNPLE
RDAAWRNVPC PSCGAPARRE TDTMDTFVDS SWYFARFTAP WLEDAPTDKA VADHWLPVDQ
YIGGIEHAIL HLLYSRFFMR AMRQTGWAGV DEPFAGLFTQ GMVVHETYRD EAGAWVQPVD
VKVVTEDGAR KAFHVKTDAP IAIGAIEKMS KSKKNVVDPD DIIASYGADT ARWFMLSDSP
PERDVIWTED GVQGASRFVQ RVWRMVSEVA EGGSEPALAG SEAVLKAAHK ALAAVGEDIE
RLRFNRCVAH VYELANSLQE AVNAERGRAP SPALREATLI LVQLIAPMMP HLAETCWTAL
GQDGLVAEAA WPAVKRELLV EDSVTLPVQI NGRKRADVMV PRDADQAAVQ AAVLALEPVQ
RALEGKPPRK VIVVPLRIVN IVV
//
