AC MF_00704; DC Protein; auto TR HAMAP; MF_00704; -; 1; level=0 XX Names: Aspartoacylase XX ID ASPA DE RecName: Full=Probable aspartoacylase; DE EC=3.5.1.15; XX CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + N-acyl-L-aspartate = a carboxylate + L-aspartate; CC Xref=Rhea:RHEA:10872, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, CC ChEBI:CHEBI:29991, ChEBI:CHEBI:58497; EC=3.5.1.15; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Note=Binds 1 zinc ion per subunit.; CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily. XX DR Pfam; PF04952; AstE_AspA; 1; trigger=no DR PIRSF; PIRSF018001; Aspartoacylase; 1; trigger=no XX KW Hydrolase case KW Metal-binding KW Zinc end case XX case GO GO:0008270; F:zinc ion binding end case GO GO:0019807; F:aspartoacylase activity XX FT From: ASPA_NOSS1 (Q8YQC1) FT BINDING 63..64 FT /ligand="substrate" FT Condition: N-R FT BINDING 14 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H FT BINDING 17 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: E FT BINDING 106 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: H FT BINDING 56 FT /ligand="substrate" FT Condition: R FT BINDING 164 FT /ligand="substrate" FT Condition: E FT BINDING 275 FT /ligand="substrate" FT Condition: Y XX Size: 288-307; Related: None; Template: P45381; Scope: Bacteria; Cyanobacteriota Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.21 2023/02/17 //