ID A0A091FYZ8_9AVES Unreviewed; 314 AA.
AC A0A091FYZ8;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=Aspartoacylase {ECO:0000256|ARBA:ARBA00040105};
DE EC=3.5.1.15 {ECO:0000256|ARBA:ARBA00039016};
DE AltName: Full=Aminoacylase-2 {ECO:0000256|ARBA:ARBA00042829};
GN ORFNames=N303_12442 {ECO:0000313|EMBL:KFO74381.1};
OS Cuculus canorus (common cuckoo).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Cuculiformes; Cuculidae; Cuculus.
OX NCBI_TaxID=55661 {ECO:0000313|EMBL:KFO74381.1, ECO:0000313|Proteomes:UP000053760};
RN [1] {ECO:0000313|EMBL:KFO74381.1, ECO:0000313|Proteomes:UP000053760}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N303 {ECO:0000313|EMBL:KFO74381.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the AspA/AstE family. Aspartoacylase subfamily.
CC {ECO:0000256|ARBA:ARBA00006173}.
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DR EMBL; KL447514; KFO74381.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091FYZ8; -.
DR STRING; 55661.A0A091FYZ8; -.
DR Proteomes; UP000053760; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
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:SF9; ASPARTOACYLASE; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR018001-3}; Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000053760};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR018001-3}.
FT ACT_SITE 179
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT BINDING 22
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 25
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 64
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 71..72
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 117
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 165..169
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 179
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 284
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
SQ SEQUENCE 314 AA; 35441 MW; 9D7DECD9907FFACC CRC64;
MTSSSVVDKP PVRRVAIFGG THGNELSGVF LVKHWQENGA EIQRTGMEVK PFLTNPRAVK
KCTRYIDCDL NRVFDPDNLG RTVVEDIPYE VRRAQEINHI FGPKGSDDAY DLIFDLHNTT
SNMGGTLILE NSRDDFTIQM FHYIKNALAP ECCPVLLIEH PSLKYATTRS VAKHPVGVEV
GPQPQGVVRA DILDKMRKIV KYGLDFVQLF NEGKEFPPCT IEVFKIMEKV DYPRNKNDEV
IAIIHPKLQP LNKGDPLFLT LDGEVIAYKG DCTVYPTFIN EAAYYEKKQA FVITVKMKLT
ANHIRSSVLE QNAS
//