ACY1_DICDI
ID ACY1_DICDI Reviewed; 408 AA.
AC Q55DP8;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Aminoacylase-1;
DE Short=ACY-1;
DE EC=3.5.1.14;
DE AltName: Full=N-acyl-L-amino-acid amidohydrolase;
GN Name=acy1; ORFNames=DDB_G0270562;
OS Dictyostelium discoideum (Slime mold).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Involved in the hydrolysis of N-acylated or N-acetylated
CC amino acids (except L-aspartate). {ECO:0000250}.
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 -!- 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; EC=3.5.1.14;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}.
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DR EMBL; AAFI02000005; EAL72631.1; -; Genomic_DNA.
DR RefSeq; XP_646083.1; XM_640991.1.
DR AlphaFoldDB; Q55DP8; -.
DR SMR; Q55DP8; -.
DR STRING; 44689.DDB0266648; -.
DR PaxDb; Q55DP8; -.
DR EnsemblProtists; EAL72631; EAL72631; DDB_G0270562.
DR GeneID; 8617033; -.
DR KEGG; ddi:DDB_G0270562; -.
DR dictyBase; DDB_G0270562; acy1.
DR eggNOG; KOG2275; Eukaryota.
DR HOGENOM; CLU_021802_5_0_1; -.
DR InParanoid; Q55DP8; -.
DR OMA; GTDAKQF; -.
DR PhylomeDB; Q55DP8; -.
DR Reactome; R-DDI-5423646; Aflatoxin activation and detoxification.
DR Reactome; R-DDI-9753281; Paracetamol ADME.
DR PRO; PR:Q55DP8; -.
DR Proteomes; UP000002195; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004046; F:aminoacylase activity; IBA:GO_Central.
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_0000331214"
FT ACT_SITE 78
FT /evidence="ECO:0000250"
FT ACT_SITE 143
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 76
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 109
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 144
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 172
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
SQ SEQUENCE 408 AA; 46568 MW; 8AD17E450D2FF224 CRC64;
MNSIQENEHV TVFREFLKIR TDHPTPDYES STKFLVEKAK EYNIPYEVYR ETGTPIVLMK
IEGLEPNLKT VLLNSHVDVV PAVHDSWKVD PFSAWKDESG NIFGRGTQDM KCVCMQFLEV
ARRIVQSGQK LKRTLHLSFV PDEEIGGSGK GMEKFVYTEK FRQLNIGLCL DEGLASPTND
FTVFYGERAP WWVHITAVGN AGHGSRFIEG TAIEKLMRTI NKMLAFRQEQ FESLHHGQHE
CGKKLGDVTS LNLTVLKAGI PIDHSNNFSY NVIPTQAEAG FDIRIPPTVN LDQFLDQIKE
WTAEEGLSFK FASYIPKNEM TKLDSDNKWW ENFKESCKKM DINLVTEIFP AATDSRFIRN
LGIPAFGFSP INNTPILLHD HNEFLNEKVY LRGIDIFMGI IPNLVNME
