ID SYD_PYRAE Reviewed; 428 AA.
AC Q8ZYM8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 27-MAR-2024, entry version 129.
DE RecName: Full=Aspartate--tRNA(Asp) ligase {ECO:0000255|HAMAP-Rule:MF_02075};
DE EC=6.1.1.12 {ECO:0000255|HAMAP-Rule:MF_02075};
DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
DE AltName: Full=Discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02075};
DE Short=D-AspRS {ECO:0000255|HAMAP-Rule:MF_02075};
GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_02075}; OrderedLocusNames=PAE0703;
OS Pyrobaculum aerophilum (strain ATCC 51768 / DSM 7523 / JCM 9630 / CIP
OS 104966 / NBRC 100827 / IM2).
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Pyrobaculum.
OX NCBI_TaxID=178306;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51768 / DSM 7523 / JCM 9630 / CIP 104966 / NBRC 100827 / IM2;
RX PubMed=11792869; DOI=10.1073/pnas.241636498;
RA Fitz-Gibbon S.T., Ladner H., Kim U.-J., Stetter K.O., Simon M.I.,
RA Miller J.H.;
RT "Genome sequence of the hyperthermophilic crenarchaeon Pyrobaculum
RT aerophilum.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:984-989(2002).
CC -!- FUNCTION: Catalyzes the attachment of L-aspartate to tRNA(Asp) in a
CC two-step reaction: L-aspartate is first activated by ATP to form Asp-
CC AMP and then transferred to the acceptor end of tRNA(Asp).
CC {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L-
CC aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660,
CC Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC ChEBI:CHEBI:456215; EC=6.1.1.12; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_02075};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02075};
CC Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium site
CC (Mg1) is bound to the beta- and gamma-phosphates of ATP and four water
CC molecules complete its coordination sphere. {ECO:0000255|HAMAP-
CC Rule:MF_02075};
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02075}.
CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02075}.
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DR EMBL; AE009441; AAL62965.1; -; Genomic_DNA.
DR PDB; 4GLA; X-ray; 2.75 A; C/D=2-104.
DR PDBsum; 4GLA; -.
DR AlphaFoldDB; Q8ZYM8; -.
DR SMR; Q8ZYM8; -.
DR STRING; 178306.PAE0703; -.
DR EnsemblBacteria; AAL62965; AAL62965; PAE0703.
DR KEGG; pai:PAE0703; -.
DR PATRIC; fig|178306.9.peg.510; -.
DR eggNOG; arCOG00406; Archaea.
DR HOGENOM; CLU_004553_2_1_2; -.
DR InParanoid; Q8ZYM8; -.
DR Proteomes; UP000002439; Chromosome.
DR GO; GO:0017101; C:aminoacyl-tRNA synthetase multienzyme complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IBA:GO_Central.
DR CDD; cd00776; AsxRS_core; 1.
DR CDD; cd04316; ND_PkAspRS_like_N; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR HAMAP; MF_02075; Asp_tRNA_synth_type2; 1.
DR InterPro; IPR004364; Aa-tRNA-synt_II.
DR InterPro; IPR006195; aa-tRNA-synth_II.
DR InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR InterPro; IPR004523; Asp-tRNA_synthase_2.
DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA.
DR NCBIfam; TIGR00458; aspS_nondisc; 1.
DR PANTHER; PTHR43450:SF1; ASPARTATE--TRNA LIGASE, CYTOPLASMIC; 1.
DR PANTHER; PTHR43450; ASPARTYL-TRNA SYNTHETASE; 1.
DR Pfam; PF00152; tRNA-synt_2; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF55681; Class II aaRS and biotin synthetases; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW Magnesium; Metal-binding; Nucleotide-binding; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..428
FT /note="Aspartate--tRNA(Asp) ligase"
FT /id="PRO_0000111002"
FT REGION 192..195
FT /note="Aspartate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 170
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 213..215
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 213
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 351
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 351
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 354
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 354
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 358
FT /ligand="L-aspartate"
FT /ligand_id="ChEBI:CHEBI:29991"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT BINDING 399..402
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT SITE 87
FT /note="Important for tRNA discrimination"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02075"
FT STRAND 20..32
FT /evidence="ECO:0007829|PDB:4GLA"
FT STRAND 34..42
FT /evidence="ECO:0007829|PDB:4GLA"
FT STRAND 48..53
FT /evidence="ECO:0007829|PDB:4GLA"
FT TURN 54..56
FT /evidence="ECO:0007829|PDB:4GLA"
FT HELIX 60..65
FT /evidence="ECO:0007829|PDB:4GLA"
FT STRAND 73..82
FT /evidence="ECO:0007829|PDB:4GLA"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:4GLA"
FT STRAND 90..99
FT /evidence="ECO:0007829|PDB:4GLA"
SQ SEQUENCE 428 AA; 49083 MW; 7BF061FF83956BDD CRC64;
MYPKKTHWTA EITPNLHGTE VVVAGWVWEL RDIGRVKFVV VRDREGFVQV TLKAGKTPDH
LFKVFAELSR EDVVVIKGIV EASKIAKSGV EIFPSEIWIL NKAKPLPIDI WSETPDLATR
LKWRSVDLKR PRNLVVFTVA SAMLRSIREV LYGEGFVEVF TPKIIVTSTE GGAELFPVMY
FERVAYLSQS PQLYKEQLTA SLERVFEIGP AYRAEKHNTD YHLNEFISVD AEAAFMDYND
IMDILEKIMR RLASTVSEYA PKLEEVGIKA LMELSNIPRV DYDEAVDRLR QLGYAVNWGD
DFTVEMQKAL MKYYGPVYFI VNFPASLRPF YTKRKDGEKS ESYDLIINGI EVASGATRIH
KRDELEEEMK KRGLDPRLFE SHLSVFDYGM PPHAGFGLGF NRLVTALLGL DNVRHATLYP
RDRYRVEP
//
