ID   ACY2_XENTR              Reviewed;         313 AA.
AC   Q28C61; B0JZ84;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Aspartoacylase;
DE            EC=3.5.1.15;
DE   AltName: Full=Aminoacylase-2;
DE            Short=ACY-2;
GN   Name=aspa; ORFNames=TEgg122g12.1;
OS   Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX   NCBI_TaxID=8364;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Egg;
RG   Sanger Xenopus tropicalis EST/cDNA project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (FEB-2008) 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; CR942438; CAJ82275.1; -; mRNA.
DR   EMBL; BC159075; AAI59076.1; -; mRNA.
DR   RefSeq; NP_001039114.1; NM_001045649.1.
DR   RefSeq; XP_012812619.1; XM_012957165.2.
DR   AlphaFoldDB; Q28C61; -.
DR   SMR; Q28C61; -.
DR   STRING; 8364.ENSXETP00000012487; -.
DR   PaxDb; Q28C61; -.
DR   GeneID; 733935; -.
DR   KEGG; xtr:733935; -.
DR   CTD; 443; -.
DR   Xenbase; XB-GENE-1016250; aspa.
DR   eggNOG; ENOG502QRAK; Eukaryota.
DR   HOGENOM; CLU_083292_0_0_1; -.
DR   InParanoid; Q28C61; -.
DR   OrthoDB; 1074294at2759; -.
DR   TreeFam; TF328708; -.
DR   Reactome; R-XTR-8963693; Aspartate and asparagine metabolism.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
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..313
FT                   /note="Aspartoacylase"
FT                   /id="PRO_0000363361"
FT   ACT_SITE        177
FT                   /evidence="ECO:0000250"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         69..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000250"
FT   BINDING         163..167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         177
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         287
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        252
FT                   /note="K -> N (in Ref. 1; CAJ82275)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        270
FT                   /note="A -> V (in Ref. 2; AAI59076)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        306
FT                   /note="A -> S (in Ref. 1; CAJ82275)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   313 AA;  35472 MW;  97E3FD1FBFFE8E1C CRC64;
     MTARRVLNPV QRVAIFGGTH GNELSGVFLV NHWLKHGEEI ARPGIEVRPF ITNPGAVEKC
     VRYVDTDLNR VFDSENLRNE NNLNLSYEVK RAQYINSIFG PKGSEDAYDV ILDLHNTTSH
     MGATLILEDS KDDFTIQMFN YIKTSMAPLA CSVLLIEHPR LKYATTRSIA KHPIGVEVGP
     QPQGVLRADV LDKMRRIIKH ALDFINYFND GKEFLPCILE VFKVLDNVAY PRNANGDCTA
     IIHNNLQDQD WKELKPGDPM FLTLDGRMIA YEGDCIVYPT FINEAAYYEK NQAFTTTQKM
     TLCAQAIRCT EPK