ID A0A0X8XAT9_HALHR Unreviewed; 834 AA.
AC A0A0X8XAT9;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 2.
DT 27-MAR-2024, entry version 35.
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:BAU58565.2};
GN ORFNames=HH1059_18770 {ECO:0000313|EMBL:BAU58565.2};
OS Halorhodospira halochloris (Ectothiorhodospira halochloris).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Halorhodospira.
OX NCBI_TaxID=1052 {ECO:0000313|EMBL:BAU58565.2, ECO:0000313|Proteomes:UP000218890};
RN [1] {ECO:0000313|Proteomes:UP000218890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM-1059 {ECO:0000313|Proteomes:UP000218890};
RA Tsukatani Y.;
RT "Halorhodospira halochloris DSM-1059 complete genome sequence.";
RL Submitted (FEB-2016) 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 ECO:0000256|RuleBase:RU363035}.
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DR EMBL; AP017372; BAU58565.2; -; Genomic_DNA.
DR AlphaFoldDB; A0A0X8XAT9; -.
DR KEGG; hhk:HH1059_18770; -.
DR Proteomes; UP000218890; Chromosome.
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; 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:UP000218890}.
FT DOMAIN 50..182
FT /note="Methionyl/Leucyl tRNA synthetase"
FT /evidence="ECO:0000259|Pfam:PF09334"
FT DOMAIN 232..415
FT /note="Leucyl-tRNA synthetase editing"
FT /evidence="ECO:0000259|Pfam:PF13603"
FT DOMAIN 428..626
FT /note="Aminoacyl-tRNA synthetase class Ia"
FT /evidence="ECO:0000259|Pfam:PF00133"
FT DOMAIN 671..795
FT /note="Methionyl/Valyl/Leucyl/Isoleucyl-tRNA synthetase
FT anticodon-binding"
FT /evidence="ECO:0000259|Pfam:PF08264"
FT MOTIF 53..63
FT /note="'HIGH' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT MOTIF 587..591
FT /note="'KMSKS' region"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
FT BINDING 590
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00049"
SQ SEQUENCE 834 AA; 93806 MW; 49110CCEDE274F52 CRC64;
MLSIHINNAS AMEEQYQPQK IETQAQQYWQ EKESFRATEG DSRPKYYCLS MFPYPSGRLH
MGHVRNYTIG DVVSRYKRMQ GYNVLQPMGW DAFGLPAENA AMERGVPPAA WTRENIEAMR
EQLQRLGFGY DWQRELATCD PQYYRWEQWL FTRLYRKGLV YRDTAAVNWD PVDQTVLANE
QVIDGRGWRS GALVERREIP QWFLRITDYV GELLDGLDNL KGWPDQVLNM QRNWIGRSEG
VELSFALDGR DEVLTVFTTR PDTLYGVTYM GLAPEHPLAL ELAASNQQIA DLVDEARSGG
TAEADMATRE KRGVDTGLEA IHPLTGQRIP VWVANFVLME YGSGAVMAVP AHDQRDWEFA
TQYNIPIKPV IHPGDGSDLD ISEGAFSDYG VLVESGPFSG MTSQNAFVAI AERLEAEGLG
QRQTQYRLRD WGISRQRYWG APIPIIHCPS CGAVPVPDEQ LPVTLPEEVE ITGAGSPLKS
MPSFYSTTCP ECGGSAERET DTFDTFMESS WYFARFACAD QDQSMLDERA DQWLPVDQYI
GGIEHAVLHL LYARFFHKVL RDEGLVSSDE PFTRLLTQGM VLKDGAKMSK SKGNTVDPQE
MVERFGADTV RLFTMFAAPP DQSLEWSDSG VEGSYRFLRR LYGLVRDHVS AGAPPDLDAQ
SLHESLTKEQ KDLRRKVHET IVKASDDIGK RFTFNTAIAA TMELTNALGK AVEDQSDAGR
AVMQEGLETA VLILAPITPH LSHYLWWQLG YEQPVVDARW PQADASALER DELELVVQVN
GKLRGHVTLP ADASEDEARQ AALQEPNVQR FVEGKEVKKV IFVPGKLLNV VVAK
//
