ID A0A2K6JV02_RHIBE Unreviewed; 313 AA.
AC A0A2K6JV02;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ENSRBIP00000002849.1};
OS Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Rhinopithecus.
OX NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000002849.1, ECO:0000313|Proteomes:UP000233180};
RN [1] {ECO:0000313|Ensembl:ENSRBIP00000002849.1, ECO:0000313|Proteomes:UP000233180}
RP NUCLEOTIDE SEQUENCE.
RA Wu, C.-I. and Zhang, Y.;
RT "Genome of Rhinopithecus bieti.";
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSRBIP00000002849.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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_017719103.1; XM_017863614.1.
DR RefSeq; XP_017719104.1; XM_017863615.1.
DR STRING; 61621.ENSRBIP00000002849; -.
DR Ensembl; ENSRBIT00000014786.1; ENSRBIP00000002817.1; ENSRBIG00000013487.1.
DR Ensembl; ENSRBIT00000014933.1; ENSRBIP00000002849.1; ENSRBIG00000013487.1.
DR GeneID; 108523103; -.
DR KEGG; rbb:108523103; -.
DR CTD; 443; -.
DR GeneTree; ENSGT00390000001189; -.
DR OrthoDB; 35794at2759; -.
DR Proteomes; UP000233180; Unplaced.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0019807; F:aspartoacylase activity; IEA:Ensembl.
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:UP000233180};
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; 35468 MW; 1222A7A95101A3EF CRC64;
MTSCHLAEAP IKKVAIFGGT HGNELTGVFL VKHWLENGAE IQRTGLEVKP FITNPSAVKK
CTRYIDCDLN RIFDLENLGK KMSEDLPYEV RRAQEIYHLF GPKGGEDSYD IIFDLHNTTS
NMGCTLILED SRNNFLIQMF HYIKTSLAPL PCYVYLIEHP SLKYATTRSI AKYPVGIEVG
PQPQGVLRAD ILDQMRKMIK HALDFIHHFN EGKEFPPCAI EVYKIIEKVD YPRDANGEIA
AVIHPNLQDQ DWKPLHPGDP MFLTLDGKTM PLGGDRTVYP VFVNEAAYYE KKEAFAKTTK
LTLNAKGIRC SVH
//