ID A0A0S6UKC0_9BRAD Unreviewed; 878 AA.
AC A0A0S6UKC0;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=BDOA9_0112180 {ECO:0000313|EMBL:GAJ32033.1};
OS Bradyrhizobium sp. DOA9.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=1126627 {ECO:0000313|EMBL:GAJ32033.1};
RN [1] {ECO:0000313|EMBL:GAJ32033.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DOA9 {ECO:0000313|EMBL:GAJ32033.1};
RX PubMed=25710540; DOI=10.1371/journal.pone.0117392;
RA Okazaki S., Noisangiam R., Okubo T., Kaneko T., Oshima K., Hattori M.,
RA Teamtisong K., Songwattana P., Tittabutr P., Boonkerd N., Saeki K.,
RA Sato S., Uchiumi T., Minamisawa K., Teaumroong N.;
RT "Genome Analysis of a Novel Bradyrhizobium sp. DOA9 Carrying a Symbiotic
RT Plasmid.";
RL PLoS ONE 10:e0117392-e0117392(2015).
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; DF820425; GAJ32033.1; -; Genomic_DNA.
DR RefSeq; WP_025033068.1; NZ_DF820425.1.
DR AlphaFoldDB; A0A0S6UKC0; -.
DR STRING; 1126627.BDOA9_0112180; -.
DR eggNOG; COG0495; Bacteria.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000066441; 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; 2.20.28.290; -; 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; 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}.
FT DOMAIN 38..172
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 222..413
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 431..619
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 629..669
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 715..840
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 43..53
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 630..634
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 633
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 878 AA; 98359 MW; 0012B34ABE4598E3 CRC64;
MTSERYNARD AEPRWQRLWD EQAIFVSKND DPRPKYYVLE MFPYPSGRIH IGHVRNYTLG
DVLARFMRAK GFNVLHPMGW DAFGLPAENA AIERKVAPKA WTYDNIAAMK KQLRSIGLSL
DWSREIATCD PSYYKHQQKM FLDFLRAGLA EREKRRVNWD PVDMTVLANE QVIDGRGWRS
GAVVEQREMN QWVFKITKYS QELLSALDGL DRWPDKVRLM QRNWIGRSEG LLIRFALDAA
TTPAGESELK IFTTRPDTLF GAKFMAISAD HPLAQAAAAK NPKLAEFIAE IKKIGTAQEI
IDTAEKQGFD TGIRAVHPFD PSWKLPVYVA NFVLMEYGTG AIFGCPAHDQ RDLDFVNKYN
LGNTPVVCPE GQDPKSFVIT DTAYDGDGRM INSRFLDGMT IEQAKEEVAK RLEMELRGNA
PVGERQVNFR LRDWGISRQR YWGCPIPIIH CPKCDVVPVP DADLPVKLPD DATFDRPGNA
LDHHPTWKHV TCPQCGGKAQ RETDTMDTFV DSSWYFARFT DPWNEASPTT PDVANRMLPV
DQYIGGVEHA ILHLLYSRFF TRAMKATGHL ALDEPFAGMF TQGMVVHETY QKADGTYVQP
AEVKVEVGGN GRRATLLTTG EDIAIGPIEK MSKSKKNTVD PDDIIETYGA DVARWFMLSD
SPPDRDVIWS DERVQGASRF VQRLWRLVND AVEVGKAAPA ARPASFGPDA TALRKAAHGA
LDKVTSGIER LHFNVCLAHI REFTNAFSEV LQRPGQPAPD LAPDLAWAIQ EASQILVQLF
SPMMPHLAEE CWQVLGQSGL VSEADWPQIE RDLLVEDSVT LVVQVNGKKR GEVTVATAAQ
NPEIEAAVLA LDAVKLALDG KPVRKVIIVP KRIVNVVG
//
