ACY1_PONAB
ID ACY1_PONAB Reviewed; 408 AA.
AC Q5RFB0;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 82.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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 {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAH89547.1; Type=Erroneous initiation; Evidence={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; CR857251; CAH89547.1; ALT_INIT; mRNA.
DR RefSeq; NP_001124673.1; NM_001131201.2.
DR AlphaFoldDB; Q5RFB0; -.
DR SMR; Q5RFB0; -.
DR STRING; 9601.ENSPPYP00000015464; -.
DR MEROPS; M20.973; -.
DR GeneID; 100171519; -.
DR KEGG; pon:100171519; -.
DR CTD; 95; -.
DR eggNOG; KOG2275; Eukaryota.
DR InParanoid; Q5RFB0; -.
DR OrthoDB; 1432382at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004046; F:aminoacylase activity; IEA:UniProtKB-EC.
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 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Metal-binding; Reference proteome; Zinc.
FT CHAIN 1..408
FT /note="Aminoacylase-1"
FT /id="PRO_0000274008"
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 373
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q03154"
SQ SEQUENCE 408 AA; 45969 MW; DA5F3D6468261C84 CRC64;
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE RARQLGLGCQ KVEVAPGYVV
TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCISIQ
YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RPEFHALRAG FALDEGIANP
TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVSSILAFR EKEWQRLQSN
PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG
VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMKLTLEP EIMPAATDNR YIRAVGIPAL
GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSES
