ID   ACY2_DANRE              Reviewed;         315 AA.
AC   A8KB34;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Aspartoacylase;
DE            EC=3.5.1.15;
DE   AltName: Full=Aminoacylase-2;
DE            Short=ACY-2;
GN   Name=aspa; ORFNames=zgc:171507;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Olfactory epithelium;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to
CC       produce acetate and L-aspartate. {ECO:0000250}.
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; Evidence={ECO:0000250};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm. Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC153945; AAI53946.1; -; mRNA.
DR   RefSeq; NP_001103573.1; NM_001110103.1.
DR   AlphaFoldDB; A8KB34; -.
DR   SMR; A8KB34; -.
DR   STRING; 7955.ENSDARP00000068606; -.
DR   PaxDb; A8KB34; -.
DR   Ensembl; ENSDART00000074117; ENSDARP00000068606; ENSDARG00000005154.
DR   GeneID; 557232; -.
DR   KEGG; dre:557232; -.
DR   CTD; 443; -.
DR   ZFIN; ZDB-GENE-080204-11; aspa.
DR   eggNOG; ENOG502QRAK; Eukaryota.
DR   GeneTree; ENSGT00390000001189; -.
DR   HOGENOM; CLU_083292_0_0_1; -.
DR   InParanoid; A8KB34; -.
DR   OMA; THGNEIN; -.
DR   OrthoDB; 1074294at2759; -.
DR   PhylomeDB; A8KB34; -.
DR   TreeFam; TF328708; -.
DR   Reactome; R-DRE-8963693; Aspartate and asparagine metabolism.
DR   PRO; PR:A8KB34; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Chromosome 5.
DR   Bgee; ENSDARG00000005154; Expressed in retina and 19 other tissues.
DR   ExpressionAtlas; A8KB34; baseline.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0019807; F:aspartoacylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   HAMAP; MF_00704; Aspartoacylase; 1.
DR   InterPro; IPR016708; Aspartoacylase.
DR   InterPro; IPR007036; Aste_AspA.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF018001; Aspartoacylase; 1.
PE   2: Evidence at transcript level;
KW   Cytoplasm; Hydrolase; Metal-binding; Nucleus; Reference proteome; Zinc.
FT   CHAIN           1..315
FT                   /note="Aspartoacylase"
FT                   /id="PRO_0000363360"
FT   ACT_SITE        180
FT                   /evidence="ECO:0000250"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         26
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         72..73
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         118
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         166..170
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         180
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         290
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   315 AA;  35535 MW;  E98CA129BFD94F3D CRC64;
     MSSRTNISCL QEAKRVAIFG GTHGNEMSGI VLANMWIQNA TEIERKGLVC KPFITNPRAV
     EKCTRYIDTD LNRAFTPENL SASELEALPY EVQRAKEINQ MFGPKGGSDA YDVIFDLHNT
     TSNMGSTLIL ESSTDLFNLQ MVHYIKKAMA PHTCSVLLNE HPQLKYSTTR SVAKHPVGLE
     VGPQPQGVLR SNVFESMRTI LKHALDFIEL FNNGVEFPPC TVNVFRVQER MDYPRDTNGN
     ITAMVHPHLQ DCDWEPLNRG DPMFLTFDGR TILYEGANTV YPTFINEAAY YEKQQAFVTT
     CREILAANAI RKAFK