ID SYL_ACIC1 Reviewed; 832 AA.
AC A0LSY4;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049};
DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049};
DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049};
DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049};
GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=Acel_0771;
OS Acidothermus cellulolyticus (strain ATCC 43068 / DSM 8971 / 11B).
OC Bacteria; Actinomycetota; Actinomycetes; Acidothermales; Acidothermaceae;
OC Acidothermus.
OX NCBI_TaxID=351607;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43068 / DSM 8971 / 11B;
RX PubMed=19270083; DOI=10.1101/gr.084848.108;
RA Barabote R.D., Xie G., Leu D.H., Normand P., Necsulea A., Daubin V.,
RA Medigue C., Adney W.S., Xu X.C., Lapidus A., Parales R.E., Detter C.,
RA Pujic P., Bruce D., Lavire C., Challacombe J.F., Brettin T.S., Berry A.M.;
RT "Complete genome of the cellulolytic thermophile Acidothermus
RT cellulolyticus 11B provides insights into its ecophysiological and
RT evolutionary adaptations.";
RL Genome Res. 19:1033-1043(2009).
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:0000255|HAMAP-Rule:MF_00049};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000255|HAMAP-Rule:MF_00049}.
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DR EMBL; CP000481; ABK52544.1; -; Genomic_DNA.
DR AlphaFoldDB; A0LSY4; -.
DR SMR; A0LSY4; -.
DR STRING; 351607.Acel_0771; -.
DR KEGG; ace:Acel_0771; -.
DR eggNOG; COG0495; Bacteria.
DR HOGENOM; CLU_004427_0_0_11; -.
DR InParanoid; A0LSY4; -.
DR OrthoDB; 9810365at2; -.
DR Proteomes; UP000008221; 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 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; 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 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; ATP-binding; Cytoplasm; Ligase;
KW Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT CHAIN 1..832
FT /note="Leucine--tRNA ligase"
FT /id="PRO_0000334724"
FT MOTIF 58..68
FT /note="'HIGH' region"
FT MOTIF 598..602
FT /note="'KMSKS' region"
FT BINDING 601
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00049"
SQ SEQUENCE 832 AA; 92222 MW; 68DA050860DB42E0 CRC64;
MAGLGSPLGR LTAVTSEIYD FAAIQARWLP VWTELDPFRA SDDPSDPRER RYMLDMFPYP
SGDLHMGHAE AFAIGDVVAR YWFQRGYNVL HPIGWDAFGL PAENAAIQRN LHPADWTYRN
IETQAASFRN YAISFDWSRR LHTCDPEYYK WTQWLFLRLF ERGLAYRKAS PVNWCPNDQT
VLANEQVVGG TCERCGAQVT KKTLTQWYFR ITEYAQRLLD DMALLEGRWP ERVLTMQRNW
IGRSEGAYVD FTIEGRAEPV TVFTTRPDTL YGATFFVIAA DSPLAAEICA PEQRAAFEAY
VDQVRRLSDI DRLSTERQKT GVFLGRYAVN PVNGERIPVW AADYVLADYG TGAIMAVPAH
DQRDLDFALT YGLPVRVVVD TGEGDPAVTG VATEGDGVHI NSGLIDGTDK AEGIARITRY
LEDIGKGRAG VTYRLRDWLV SRQRFWGAPI PIVHCPGCGE VAVPDQDLPV LLPDLRGADL
APKGISPLAG AADWVQTTCP RCGGSAQRDT DTMDTFVDSS WYYLRYCSPH DPSQPFDVAK
VRQWLPVHQY VGGVEHAILH LLYSRFITKV LHDMGLVDFV EPFSALLNQG QVINQGKAMS
KSLGNGVDLG EQLATYGVDA VRLTMVFAGP PEEDIDWADM NPGALGKFLA RVWRIAGEVT
SPVGAPPKDG DPALRRVTHR TIREVTELVE SFRFNVAVAR VMELANALRK AIDTGPGPAD
PAVREGAEAL AVMLSLFAPY TAEECWARLG HQPTVAKAGW PTPDPELLAQ EEVTCVVQVN
GKVRERLRVS PSISEEELRA AALAAPAVEK AIDGRPVQRI IVRAPKLVNV VV
//
