AC   MF_00044;
DC   Protein; auto
TR   HAMAP; MF_00044; -; 1; level=0
XX
Names: Asp_tRNA_synth_type1
XX
case <FTTag:NonDiscr1_bact> or <FTTag:NonDiscr2_bact>
ID   SYDND
DE   RecName: Full=Aspartate--tRNA(Asp/Asn) ligase;
DE            EC=6.1.1.23;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
DE   AltName: Full=Non-discriminating aspartyl-tRNA synthetase;
DE            Short=ND-AspRS;
else
ID   SYD
DE   RecName: Full=Aspartate--tRNA ligase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
end case
GN   Name=aspS;
XX
case <FTTag:NonDiscr1_bact> or <FTTag:NonDiscr2_bact>
CC   -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity since
CC       it is able to aspartylate not only its cognate tRNA(Asp) but also
CC       tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first
CC       activated by ATP to form Asp-AMP and then transferred to the acceptor
CC       end of tRNA(Asp/Asn).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L-
CC         aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710,
CC         Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516,
CC         ChEBI:CHEBI:456215; EC=6.1.1.23;
else
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   -!- 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;
end case
CC   -!- SUBUNIT: Homodimer.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       Type 1 subfamily.
XX
DR   Pfam; PF02938; GAD; 1; trigger=no
DR   Pfam; PF00152; tRNA-synt_2; 1; trigger=no
DR   Pfam; PF01336; tRNA_anti-codon; 1; trigger=no
DR   PRINTS; PR01042; TRNASYNTHASP; 1; trigger=no
DR   NCBIfam; TIGR00459; aspS_bact; 1; trigger=no
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1; trigger=no
XX
KW   Cytoplasm
KW   Aminoacyl-tRNA synthetase
KW   Protein biosynthesis
KW   Ligase
KW   ATP-binding
KW   Nucleotide-binding
XX
GO   GO:0004815; F:aspartate-tRNA ligase activity
GO   GO:0005524; F:ATP binding
GO   GO:0006422; P:aspartyl-tRNA aminoacylation
GO   GO:0005737; C:cytoplasm
XX
FT   From: SYD_THETH (P36419)
FT   BINDING         223..225
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: R-x-E
FT   BINDING         528..531
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Condition: G-x-x-R
FT   REGION          201..204
FT                   /note="Aspartate"
FT   Condition: Q-x-x-K
FT   BINDING         177
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Optional; Condition: E
FT   BINDING         223
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Optional; Condition: R
FT   BINDING         232
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: Q
FT   BINDING         442
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Optional; Condition: H
FT   BINDING         476
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT   Optional; Condition: E
FT   BINDING         483
FT                   /ligand="L-aspartate"
FT                   /ligand_id="ChEBI:CHEBI:29991"
FT   Optional; Condition: R
FT   From: SYDND_PSEAE (Q51422)
FT   SITE            31
FT                   /note="Important for tRNA non-discrimination"
FT   Tag: NonDiscr1_bact; Optional; Condition: H
FT   SITE            82
FT                   /note="Important for tRNA non-discrimination"
FT   Tag: NonDiscr2_bact; Optional; Condition: G
XX
Size: 430-700;
Related: MF_02075;
Template: P21889; P36419; Q5SKD2; P56459; Q51422; Q9RUN7; O84546;
Scope:
 Bacteria
 Archaea
Fusion:
 Nter: <Unknown>
 Cter: None
Duplicate: in STRMU, SYNAS, DEIRA, THET8
Plasmid: None
Comments: This subfamily contains most bacterial aspartate--tRNA ligases
 and eukaryotic mitochondrial aspartate--tRNA ligases.
 See MF_02075 for type 2 subfamily.
 Unknown N-terminal domain in MAGSA.
XX
# Revision 1.42 2023/06/01
//