ID   ACY1_PIG                Reviewed;         407 AA.
AC   P37111;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   24-JAN-2024, entry version 132.
DE   RecName: Full=Aminoacylase-1;
DE            Short=ACY-1;
DE            EC=3.5.1.14 {ECO:0000250|UniProtKB:Q99JW2};
DE   AltName: Full=N-acyl-L-amino-acid amidohydrolase;
GN   Name=ACY1;
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, AND ACETYLATION AT
RP   ALA-2.
RC   TISSUE=Kidney;
RX   PubMed=1284246; DOI=10.1093/oxfordjournals.jbchem.a123968;
RA   Mitta M., Ohnogi H., Yamamoto A., Kato I., Sakiyama F., Tsunasawa S.;
RT   "The primary structure of porcine aminoacylase 1 deduced from cDNA
RT   sequence.";
RL   J. Biochem. 112:737-742(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Kidney;
RX   PubMed=1292507; DOI=10.1515/bchm3.1992.373.2.1227;
RA   Jakob M., Miller Y.E., Roehm K.H.;
RT   "Cloning and sequence analyses of cDNAs encoding aminoacylase I from
RT   porcine kidney.";
RL   Biol. Chem. Hoppe-Seyler 373:1227-1231(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Sawazaki T., Hamasima N.;
RT   "Porcine cosmid clone containing the ACY-1 and rpL29/HIP genes.";
RL   Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the hydrolysis of N-acetylated amino acids to
CC       acetate and free amino acids. {ECO:0000250|UniProtKB:Q99JW2}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-amino acid + H2O = a carboxylate + an L-alpha-
CC         amino acid; Xref=Rhea:RHEA:15565, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:29067, ChEBI:CHEBI:59869, ChEBI:CHEBI:59874; EC=3.5.1.14;
CC         Evidence={ECO:0000250|UniProtKB:Q99JW2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:15566;
CC         Evidence={ECO:0000250|UniProtKB:Q99JW2};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(alpha)-acetyl-L-methionine = acetate + L-methionine;
CC         Xref=Rhea:RHEA:67440, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:57844, ChEBI:CHEBI:71670;
CC         Evidence={ECO:0000250|UniProtKB:Q03154};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67441;
CC         Evidence={ECO:0000250|UniProtKB:Q03154};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N-acetyl-L-glutamine = acetate + L-glutamine;
CC         Xref=Rhea:RHEA:67368, ChEBI:CHEBI:15377, ChEBI:CHEBI:30089,
CC         ChEBI:CHEBI:58359, ChEBI:CHEBI:143879;
CC         Evidence={ECO:0000250|UniProtKB:Q99JW2};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67369;
CC         Evidence={ECO:0000250|UniProtKB:Q99JW2};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000250|UniProtKB:Q03154};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250|UniProtKB:Q03154};
CC   -!- SUBUNIT: Homodimer (By similarity). Interacts with SPHK1 (By
CC       similarity). {ECO:0000250|UniProtKB:Q99JW2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; D13514; BAA02731.1; -; mRNA.
DR   EMBL; X68564; CAA48565.1; -; mRNA.
DR   EMBL; AB017196; BAA76403.1; -; Genomic_DNA.
DR   PIR; JN0584; JN0584.
DR   RefSeq; NP_999061.1; NM_213896.1.
DR   AlphaFoldDB; P37111; -.
DR   SMR; P37111; -.
DR   STRING; 9823.ENSSSCP00000074309; -.
DR   MEROPS; M20.973; -.
DR   iPTMnet; P37111; -.
DR   PaxDb; 9823-ENSSSCP00000025679; -.
DR   PeptideAtlas; P37111; -.
DR   Ensembl; ENSSSCT00000088369.2; ENSSSCP00000074309.2; ENSSSCG00000023325.4.
DR   Ensembl; ENSSSCT00015087499.1; ENSSSCP00015035649.1; ENSSSCG00015064834.1.
DR   Ensembl; ENSSSCT00015087631.1; ENSSSCP00015035709.1; ENSSSCG00015064834.1.
DR   Ensembl; ENSSSCT00015088517.1; ENSSSCP00015036094.1; ENSSSCG00015064834.1.
DR   Ensembl; ENSSSCT00015088643.1; ENSSSCP00015036143.1; ENSSSCG00015064834.1.
DR   Ensembl; ENSSSCT00015089017.1; ENSSSCP00015036313.1; ENSSSCG00015064834.1.
DR   Ensembl; ENSSSCT00015089254.1; ENSSSCP00015036402.1; ENSSSCG00015064834.1.
DR   Ensembl; ENSSSCT00040043190.1; ENSSSCP00040018123.1; ENSSSCG00040032105.1.
DR   Ensembl; ENSSSCT00040043263.1; ENSSSCP00040018158.1; ENSSSCG00040032105.1.
DR   Ensembl; ENSSSCT00040043452.1; ENSSSCP00040018234.1; ENSSSCG00040032105.1.
DR   Ensembl; ENSSSCT00040043801.1; ENSSSCP00040018385.1; ENSSSCG00040032105.1.
DR   Ensembl; ENSSSCT00040043896.1; ENSSSCP00040018429.1; ENSSSCG00040032105.1.
DR   Ensembl; ENSSSCT00065033227.1; ENSSSCP00065013723.1; ENSSSCG00065024868.1.
DR   Ensembl; ENSSSCT00065033231.1; ENSSSCP00065013727.1; ENSSSCG00065024868.1.
DR   Ensembl; ENSSSCT00065033263.1; ENSSSCP00065013741.1; ENSSSCG00065024868.1.
DR   Ensembl; ENSSSCT00065033274.1; ENSSSCP00065013749.1; ENSSSCG00065024868.1.
DR   Ensembl; ENSSSCT00065033301.1; ENSSSCP00065013760.1; ENSSSCG00065024868.1.
DR   Ensembl; ENSSSCT00065033313.1; ENSSSCP00065013766.1; ENSSSCG00065024868.1.
DR   GeneID; 396930; -.
DR   KEGG; ssc:396930; -.
DR   CTD; 95; -.
DR   eggNOG; KOG2275; Eukaryota.
DR   GeneTree; ENSGT00940000155631; -.
DR   HOGENOM; CLU_021802_5_0_1; -.
DR   InParanoid; P37111; -.
DR   OMA; GTDAKQF; -.
DR   OrthoDB; 158507at2759; -.
DR   TreeFam; TF313693; -.
DR   BRENDA; 3.5.1.14; 6170.
DR   Reactome; R-SSC-5423646; Aflatoxin activation and detoxification.
DR   Reactome; R-SSC-9753281; Paracetamol ADME.
DR   SABIO-RK; P37111; -.
DR   Proteomes; UP000008227; Chromosome 13.
DR   Proteomes; UP000314985; Unplaced.
DR   Proteomes; UP000694570; Unplaced.
DR   Proteomes; UP000694571; Unplaced.
DR   Proteomes; UP000694720; Unplaced.
DR   Proteomes; UP000694722; Unplaced.
DR   Proteomes; UP000694723; Unplaced.
DR   Proteomes; UP000694724; Unplaced.
DR   Proteomes; UP000694725; Unplaced.
DR   Proteomes; UP000694726; Unplaced.
DR   Proteomes; UP000694727; Unplaced.
DR   Proteomes; UP000694728; Unplaced.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0070062; C:extracellular exosome; IEA:Ensembl.
DR   GO; GO:0004046; F:aminoacylase activity; IBA:GO_Central.
DR   GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   CDD; cd05646; M20_AcylaseI_like; 1.
DR   Gene3D; 1.10.150.900; -; 1.
DR   Gene3D; 3.30.70.360; -; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR001261; ArgE/DapE_CS.
DR   InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR   InterPro; IPR010159; N-acyl_aa_amidohydrolase.
DR   InterPro; IPR002933; Peptidase_M20.
DR   InterPro; IPR011650; Peptidase_M20_dimer.
DR   NCBIfam; TIGR01880; Ac-peptdase-euk; 1.
DR   PANTHER; PTHR45892; AMINOACYLASE-1; 1.
DR   PANTHER; PTHR45892:SF1; AMINOACYLASE-1; 1.
DR   Pfam; PF07687; M20_dimer; 1.
DR   Pfam; PF01546; Peptidase_M20; 1.
DR   PIRSF; PIRSF036696; ACY-1; 1.
DR   SUPFAM; SSF55031; Bacterial exopeptidase dimerisation domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
DR   PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR   PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
DR   Genevisible; P37111; SS.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Metal-binding; Reference proteome; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:1284246"
FT   CHAIN           2..407
FT                   /note="Aminoacylase-1"
FT                   /id="PRO_0000185237"
FT   ACT_SITE        82
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        147
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         80
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q03154"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q03154"
FT   BINDING         113
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q03154"
FT   BINDING         148
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q03154"
FT   BINDING         175
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q03154"
FT   BINDING         372
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:Q03154"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:1284246"
FT   CONFLICT        395
FT                   /note="Missing (in Ref. 2; CAA48565)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        398
FT                   /note="A -> T (in Ref. 2; CAA48565)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   407 AA;  45347 MW;  FCB88982ADBFF3D4 CRC64;
     MASKGREGEH PSVTLFRQYL RIRTVQPEPD YGAAVAFLEE RARQLGLGCQ KVEVVPGHVV
     TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEGFK DADGYIYGRG AQDMKCVSIQ
     YLEAVRRLKV EGHHFPRTIH MTFVPDEEVG GHQGMELFVK RPEFQALRAG FALDEGLASP
     TDAFTVFYSE RSPWWLRVTS TGKPGHGSRF IEDTAAEKLH KVINSILAFR EKEKQRLQSN
     QLKPGAVTSV NLTMLEGGVA YNVVPATMSA CFDFRVAPDV DLKAFEEQLQ SWCQAAGEGV
     TFEFVQKWME TQVTSTDDSD PWWAAFSGVF KDMKLALELE ICPASTDARY IRAAGVPALG
     FSPMNHTPVL LHDHDERLHE AVFLRGVDIY TQLLSALASV PALPSES
//