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HAMAP rule MF_00044

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General rule information [?]

Accession MF_00044
Dates 1-JUN-2001 (Created)
1-JUN-2023 (Last updated, Version 42)
Name Asp_tRNA_synth_type1
Scope(s) Bacteria
Archaea
Template(s) P21889 (SYD_ECOLI); P36419 (SYD_THETH); Q5SKD2 (SYD_THET8); P56459 (SYDND_HELPY); Q51422 (SYDND_PSEAE); Q9RUN7 (SYD_DEIRA); O84546 (SYDND_CHLTR); [ Recover all ]
Triggered by HAMAP; MF_00044 (Get profile general information and statistics)

Propagated annotation [?]

Identifier, protein and gene names [?]

case <FTTag:NonDiscr1_bact> or <FTTag:NonDiscr2_bact>
Identifier SYDND
Protein name RecName: Full=Aspartate--tRNA(Asp/Asn) ligase;
                 EC=6.1.1.23;
AltName: Full=Aspartyl-tRNA synthetase;
                 Short=AspRS;
AltName: Full=Non-discriminating aspartyl-tRNA synthetase;
                 Short=ND-AspRS;
else
Identifier SYD
Protein name RecName: Full=Aspartate--tRNA ligase;
                 EC=6.1.1.12;
AltName: Full=Aspartyl-tRNA synthetase;
                 Short=AspRS;
end case
Gene name Name=aspS;

Comments [?]

case <FTTag:NonDiscr1_bact> or <FTTag:NonDiscr2_bact>
FUNCTIONAspartyl-tRNA synthetase with relaxed tRNA specificity since it is able to aspartylate not only its cognate tRNA(Asp) but also tRNA(Asn). Reaction proceeds in two steps: L-aspartate is first activated by ATP to form Asp-AMP and then transferred to the acceptor end of tRNA(Asp/Asn).
CATALYTIC ACTIVITY Reaction=ATP + L-aspartate + tRNA(Asx) = AMP + diphosphate + L- aspartyl-tRNA(Asx); Xref=Rhea:RHEA:18349, Rhea:RHEA-COMP:9710, Rhea:RHEA-COMP:9711, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.23;
else
FUNCTIONCatalyzes the attachment of L-aspartate to tRNA(Asp) in a two-step reaction: L-aspartate is first activated by ATP to form Asp- AMP and then transferred to the acceptor end of tRNA(Asp).
CATALYTIC ACTIVITY Reaction=ATP + L-aspartate + tRNA(Asp) = AMP + diphosphate + L- aspartyl-tRNA(Asp); Xref=Rhea:RHEA:19649, Rhea:RHEA-COMP:9660, Rhea:RHEA-COMP:9678, ChEBI:CHEBI:29991, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019, ChEBI:CHEBI:78442, ChEBI:CHEBI:78516, ChEBI:CHEBI:456215; EC=6.1.1.12;
end case
SUBUNITHomodimer.
SUBCELLULAR LOCATIONCytoplasm.
SIMILARITYBelongs to the class-II aminoacyl-tRNA synthetase family. Type 1 subfamily.

Keywords [?]

Cytoplasm
Aminoacyl-tRNA synthetase
Protein biosynthesis
Ligase
ATP-binding
Nucleotide-binding

Gene Ontology [?]

GO:0004815; Molecular function:aspartate-tRNA ligase activity
GO:0005524; Molecular function:ATP binding
GO:0006422; Biological process:aspartyl-tRNA aminoacylation
GO:0005737; Cellular component:cytoplasm

Cross-references [?]

Pfam PF02938; GAD; 1;
Pfam PF00152; tRNA-synt_2; 1;
Pfam PF01336; tRNA_anti-codon; 1;
PRINTS PR01042; TRNASYNTHASP; 1;
NCBIfam TIGR00459; aspS_bact; 1;
PROSITE PS50862; AA_TRNA_LIGASE_II; 1;

Features [?]

From: SYD_THETH (P36419)
Key From To Description Tag Condition FTGroup
BINDING 223 225 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 R-x-E
BINDING 528 531 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 G-x-x-R
REGION 201 204 /note="Aspartate" Q-x-x-K
BINDING 177 177 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"		 E
BINDING 223 223 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"		 R
BINDING 232 232 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 Q
BINDING 442 442 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"		 H
BINDING 476 476 /ligand="ATP"
/ligand_id="ChEBI:CHEBI:30616"		 E
BINDING 483 483 /ligand="L-aspartate"
/ligand_id="ChEBI:CHEBI:29991"		 R
From: SYDND_PSEAE (Q51422)
Key From To Description Tag Condition FTGroup
SITE 31 31 /note="Important for tRNA non-discrimination" NonDiscr1_bact H
SITE 82 82 /note="Important for tRNA non-discrimination" NonDiscr2_bact G

Additional information [?]

Size range 430-700 amino acids
Related rules MF_02075
Fusion Nter: <Unknown> Cter: 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.



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