ID   ACY3_XENTR              Reviewed;         310 AA.
AC   Q5BJ91;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-APR-2005, sequence version 1.
DT   03-AUG-2022, entry version 89.
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 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=Embryo;
RG   NIH - Xenopus Gene Collection (XGC) project;
RL   Submitted (MAR-2005) 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; BC091576; AAH91576.1; -; mRNA.
DR   RefSeq; NP_001025627.1; NM_001030456.1.
DR   RefSeq; XP_012812542.1; XM_012957088.2.
DR   AlphaFoldDB; Q5BJ91; -.
DR   SMR; Q5BJ91; -.
DR   STRING; 8364.ENSXETP00000019664; -.
DR   PaxDb; Q5BJ91; -.
DR   Ensembl; ENSXETT00000019664; ENSXETP00000019664; ENSXETG00000008975.
DR   GeneID; 595015; -.
DR   KEGG; xtr:595015; -.
DR   CTD; 91703; -.
DR   Xenbase; XB-GENE-5934782; acy3.
DR   eggNOG; ENOG502RMBB; Eukaryota.
DR   HOGENOM; CLU_083292_0_0_1; -.
DR   InParanoid; Q5BJ91; -.
DR   OMA; YPRDPTT; -.
DR   OrthoDB; 1074294at2759; -.
DR   PhylomeDB; Q5BJ91; -.
DR   TreeFam; TF328708; -.
DR   Reactome; R-XTR-5423646; Aflatoxin activation and detoxification.
DR   Proteomes; UP000008143; Chromosome 2.
DR   Proteomes; UP000790000; Unplaced.
DR   Bgee; ENSXETG00000008975; Expressed in skeletal muscle tissue and 5 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004046; F:aminoacylase activity; IBA:GO_Central.
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   Cell membrane; Cytoplasm; Hydrolase; Membrane; Metal-binding;
KW   Reference proteome; Zinc.
FT   CHAIN           1..310
FT                   /note="N-acyl-aromatic-L-amino acid amidohydrolase
FT                   (carboxylate-forming)"
FT                   /id="PRO_0000363366"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         23
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         62
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         69..70
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000255"
FT   BINDING         176
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
FT   BINDING         286
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   310 AA;  34724 MW;  D68B9EEF2B1A0637 CRC64;
     MSPTVQCGAV SQVVVVGGTH GNEMSGVCLA KHWLQDPSEL HRKSFTAEVL LANPIAVERC
     VRYIDRDLNR SFSHELLSAS GSESDSYEAK RAREIYQKYG PKQSSLNFVI DLHNTTSNMG
     TTFLLFKGDN FALHLANYLQ TKCVDPSFPC HILLIDIPEG GHVHLQSMGK HSVSLELGPQ
     PQGVARADVL TRMRALVNCS LDFLDLFNQG TEFPSFETDV HQVLYRADFP RNEDGEIEAV
     IHSELQDKDY LPLKPGDPIF QRLNGEDILY NGEKQIYPVF INEAAYYEKK VAFIATEKTH
     CLVPALKVQN