ID   ACY3_XENLA              Reviewed;         305 AA.
AC   A0JMS7;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   03-AUG-2022, entry version 52.
DE   RecName: Full=N-acyl-aromatic-L-amino acid amidohydrolase (carboxylate-forming);
DE            EC=3.5.1.114;
DE   AltName: Full=Aminoacylase-3;
DE            Short=ACY-3;
DE   AltName: Full=Aspartoacylase-2;
GN   Name=acy3;
OS   Xenopus laevis (African clawed frog).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC   Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX   NCBI_TaxID=8355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Plays an important role in deacetylating mercapturic acids in
CC       kidney proximal tubules. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-aromatic L-alpha-amino acid + H2O = a carboxylate +
CC         an aromatic L-alpha-amino acid; Xref=Rhea:RHEA:54184,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:29067, ChEBI:CHEBI:84824,
CC         ChEBI:CHEBI:138093; EC=3.5.1.114;
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acetyl-L-cysteine-S-conjugate + H2O = acetate + an S-
CC         substituted L-cysteine; Xref=Rhea:RHEA:36855, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:30089, ChEBI:CHEBI:58717, ChEBI:CHEBI:58718;
CC         EC=3.5.1.114;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000305};
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane; Peripheral membrane
CC       protein. Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC       {ECO:0000305}.
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DR   EMBL; BC125990; AAI25991.1; -; mRNA.
DR   RefSeq; NP_001090428.1; NM_001096959.1.
DR   AlphaFoldDB; A0JMS7; -.
DR   SMR; A0JMS7; -.
DR   DNASU; 779340; -.
DR   GeneID; 779340; -.
DR   KEGG; xla:779340; -.
DR   CTD; 779340; -.
DR   Xenbase; XB-GENE-6252462; acy3.L.
DR   OMA; YPRDPTT; -.
DR   OrthoDB; 1074294at2759; -.
DR   Proteomes; UP000186698; Chromosome 2L.
DR   Bgee; 779340; Expressed in kidney and 16 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
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   Cell membrane; Cytoplasm; Hydrolase; Membrane; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..305
FT                   /note="N-acyl-aromatic-L-amino acid amidohydrolase
FT                   (carboxylate-forming)"
FT                   /id="PRO_0000363365"
FT   BINDING         15
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         18
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         57
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         64..65
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         108
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         171
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         281
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   305 AA;  34310 MW;  85913B880AB1519D CRC64;
     MSPPVSQVVV VGGTHGNEMS GVCLAKHWLQ DPSELRRKSF TADILLANPI AVERCVRYID
     RDLNRSFSHE LLSASASESD SYEVKRAREI YQKYGPKQSS LNFVIDLHNT TSNMGTTILL
     FKGDNFALHL ANYLKTKCVD PSFPCHILLI DIPEQGHVHL QSMGKHSISL ELGPQPQGVV
     RTDVLARMKV LVNSSLDFLD LFNQGTEFPS FEAEVHQVLH KADFPRGADG EIQAFIHSEL
     QDKDYLPLKP GDPIFQRLNG DDILYNGEKL IYPVFINESA YYEKKVAFIA TEKKHCFVPA
     LKLQN