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Database: UniProt
Entry: A0A096MTW7_PAPAN
LinkDB: A0A096MTW7_PAPAN
Original site: A0A096MTW7_PAPAN 
ID   A0A096MTW7_PAPAN        Unreviewed;       319 AA.
AC   A0A096MTW7;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   25-MAY-2022, sequence version 2.
DT   27-MAR-2024, entry version 54.
DE   RecName: Full=N-acyl-aromatic-L-amino acid amidohydrolase {ECO:0000256|ARBA:ARBA00034807};
DE            EC=3.5.1.114 {ECO:0000256|ARBA:ARBA00034807};
GN   Name=ACY3 {ECO:0000313|Ensembl:ENSPANP00000003260.2};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000003260.2, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000003260.2, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000003260.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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; Evidence={ECO:0000256|ARBA:ARBA00036061};
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         Evidence={ECO:0000256|ARBA:ARBA00036225};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|PIRSR:PIRSR018001-3};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR018001-3};
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000256|ARBA:ARBA00037831}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00037831}. Cell membrane
CC       {ECO:0000256|ARBA:ARBA00004202}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004202}. Cytoplasm
CC       {ECO:0000256|ARBA:ARBA00004496}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004170}; Peripheral membrane protein
CC       {ECO:0000256|ARBA:ARBA00004170}.
CC   -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC       {ECO:0000256|ARBA:ARBA00006173}.
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DR   AlphaFoldDB; A0A096MTW7; -.
DR   STRING; 9555.ENSPANP00000003260; -.
DR   Ensembl; ENSPANT00000022438.3; ENSPANP00000003260.2; ENSPANG00000024740.3.
DR   eggNOG; ENOG502QRAK; Eukaryota.
DR   GeneTree; ENSGT00390000001189; -.
DR   HOGENOM; CLU_083292_0_0_1; -.
DR   OMA; AMHLCHH; -.
DR   Proteomes; UP000028761; Chromosome 12.
DR   Bgee; ENSPANG00000024740; Expressed in metanephros cortex and 12 other cell types or tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004046; F:aminoacylase activity; IEA:Ensembl.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd06909; M14_ASPA; 1.
DR   Gene3D; 2.20.25.160; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   HAMAP; MF_00704; Aspartoacylase; 1.
DR   InterPro; IPR016708; Aspartoacylase.
DR   InterPro; IPR007036; Aste_AspA.
DR   PANTHER; PTHR15162; ASPARTOACYLASE; 1.
DR   PANTHER; PTHR15162:SF5; N-ACYL-AROMATIC-L-AMINO ACID AMIDOHYDROLASE (CARBOXYLATE-FORMING); 1.
DR   Pfam; PF04952; AstE_AspA; 1.
DR   PIRSF; PIRSF018001; Aspartoacylase; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR018001-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR018001-3}.
FT   ACT_SITE        178
FT                   /note="Proton donor/acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT   BINDING         21
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT   BINDING         24
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT   BINDING         116
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
SQ   SEQUENCE   319 AA;  35224 MW;  9BD3C7ECF1C6A916 CRC64;
     MCSLPVPREP LRRVAVTGGT HGNEMSGVYL AQHWLQAPAE LQRLSFSAVP VLANPAATAA
     CCRYVDHDLN RAFTSSFLNS RPTPDDPYEV TRARELNQLL GPKASGRAFD FVLDLHNTTA
     NMGTCLIAKS SHEVFAMHLC RHLQLQYPEL SCQVFLCQRS GEESYNLDSV AKNGLALELG
     PQPQGVLRAD IFSRMRTLVA TVLDFIELFN QGTAFPAFEM EAYRPVGVVD FPCTDAGNLA
     GTVHPQLQDR DFQPLQPGAP IFQMFSGEDL LYDEESTVYP VFINEAAYYE KGIAFVQTEK
     FTFTVPAMPV LNPVPSPTS
//
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