ID F1MUZ8_BOVIN Unreviewed; 313 AA.
AC F1MUZ8;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 79.
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 Name=ASPA {ECO:0000313|Ensembl:ENSBTAP00000004734.4,
GN ECO:0000313|VGNC:VGNC:26217};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913 {ECO:0000313|Ensembl:ENSBTAP00000004734.4, ECO:0000313|Proteomes:UP000009136};
RN [1] {ECO:0000313|Ensembl:ENSBTAP00000004734.4, ECO:0000313|Proteomes:UP000009136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000004734.4,
RC ECO:0000313|Proteomes:UP000009136};
RA Rosen B.D., Bickhart D.M., Koren S., Schnabel R.D., Hall R., Zimin A.,
RA Dreischer C., Schultheiss S., Schroeder S.G., Elsik C.G., Couldrey C.,
RA Liu G.E., Van Tassell C.P., Phillippy A.M., Smith T.P.L., Medrano J.F.;
RT "ARS-UCD1.2.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSBTAP00000004734.4}
RP IDENTIFICATION.
RC STRAIN=Hereford {ECO:0000313|Ensembl:ENSBTAP00000004734.4};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Catalyzes the deacetylation of N-acetylaspartic acid (NAA) to
CC produce acetate and L-aspartate. NAA occurs in high concentration in
CC brain and its hydrolysis NAA plays a significant part in the
CC maintenance of intact white matter. In other tissues it acts as a
CC scavenger of NAA from body fluids. {ECO:0000256|ARBA:ARBA00043907}.
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 RefSeq; XP_005220265.1; XM_005220208.3.
DR RefSeq; XP_010814208.1; XM_010815906.1.
DR Ensembl; ENSBTAT00000004734.5; ENSBTAP00000004734.4; ENSBTAG00000003629.5.
DR Ensembl; ENSBTAT00000069554.1; ENSBTAP00000067259.1; ENSBTAG00000003629.5.
DR GeneID; 509432; -.
DR CTD; 443; -.
DR VEuPathDB; HostDB:ENSBTAG00000003629; -.
DR VGNC; VGNC:26217; ASPA.
DR GeneTree; ENSGT00390000001189; -.
DR HOGENOM; CLU_083292_0_0_1; -.
DR OMA; THGNEIN; -.
DR OrthoDB; 35794at2759; -.
DR TreeFam; TF328708; -.
DR Reactome; R-BTA-8963693; Aspartate and asparagine metabolism.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000003629; Expressed in metanephros cortex and 97 other cell types or tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019807; F:aspartoacylase activity; IEA:Ensembl.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IBA:GO_Central.
DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro.
DR GO; GO:0042802; F:identical protein binding; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006083; P:acetate metabolic process; IEA:Ensembl.
DR GO; GO:0006531; P:aspartate metabolic process; IEA:Ensembl.
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:UP000009136};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR018001-3}.
FT ACT_SITE 178
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-1"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 63
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 70..71
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 116
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-3"
FT BINDING 164..168
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 178
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
FT BINDING 288
FT /ligand="N-acetyl-L-aspartate"
FT /ligand_id="ChEBI:CHEBI:16953"
FT /evidence="ECO:0000256|PIRSR:PIRSR018001-2"
SQ SEQUENCE 313 AA; 35701 MW; 9265B79C89B608A6 CRC64;
MTSCHVAEDP IKKVAIFGGT HGNELTGVFL VKHWLENSTE IQRTGLEVKP FITNPRAVKK
CTRYIDCDLN RVFDPENLGK KKSEDLPYEV RRAQEINHLF GPKDSEDSYD IIFDLHNTTS
NMGCTLILED SRNDFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG
PQPQGVLRAD ILDQMRKMIQ HALDFIHNFN EGKEFPPCAI EVYKIMEKVD YPRNESGEIS
AIIHPKLQDQ DWKPLHPEDP VFLTLDGKTI SLGGDQTVYP VFVNEAAYYE KKEAFAKTTK
LTLNANSIRS SLH
//
