ACY1_PIG
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 03-AUG-2022, entry version 126.
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}.
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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.ENSSSCP00000025679; -.
DR MEROPS; M20.973; -.
DR iPTMnet; P37111; -.
DR PaxDb; P37111; -.
DR PeptideAtlas; P37111; -.
DR PRIDE; P37111; -.
DR Ensembl; ENSSSCT00015087499; ENSSSCP00015035649; ENSSSCG00015064834.
DR Ensembl; ENSSSCT00015087631; ENSSSCP00015035709; ENSSSCG00015064834.
DR Ensembl; ENSSSCT00015088517; ENSSSCP00015036094; ENSSSCG00015064834.
DR Ensembl; ENSSSCT00015088643; ENSSSCP00015036143; ENSSSCG00015064834.
DR Ensembl; ENSSSCT00015089017; ENSSSCP00015036313; ENSSSCG00015064834.
DR Ensembl; ENSSSCT00015089254; ENSSSCP00015036402; ENSSSCG00015064834.
DR Ensembl; ENSSSCT00040043190; ENSSSCP00040018123; ENSSSCG00040032105.
DR Ensembl; ENSSSCT00040043263; ENSSSCP00040018158; ENSSSCG00040032105.
DR Ensembl; ENSSSCT00040043452; ENSSSCP00040018234; ENSSSCG00040032105.
DR Ensembl; ENSSSCT00040043801; ENSSSCP00040018385; ENSSSCG00040032105.
DR Ensembl; ENSSSCT00040043896; ENSSSCP00040018429; ENSSSCG00040032105.
DR Ensembl; ENSSSCT00065033227; ENSSSCP00065013723; ENSSSCG00065024868.
DR Ensembl; ENSSSCT00065033231; ENSSSCP00065013727; ENSSSCG00065024868.
DR Ensembl; ENSSSCT00065033263; ENSSSCP00065013741; ENSSSCG00065024868.
DR Ensembl; ENSSSCT00065033274; ENSSSCP00065013749; ENSSSCG00065024868.
DR Ensembl; ENSSSCT00065033301; ENSSSCP00065013760; ENSSSCG00065024868.
DR Ensembl; ENSSSCT00065033313; ENSSSCP00065013766; ENSSSCG00065024868.
DR GeneID; 396930; -.
DR KEGG; ssc:396930; -.
DR CTD; 95; -.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_5_0_1; -.
DR InParanoid; P37111; -.
DR OMA; GTDAKQF; -.
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; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; P37111; SS.
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:cellular amino acid metabolic process; IEA:InterPro.
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 Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01880; Ac-peptdase-euk; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
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
