ID   NDDD_ALCXX              Reviewed;         498 AA.
AC   P94212;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=N-acyl-D-aspartate deacylase;
DE            EC=3.5.1.83;
DE   AltName: Full=N-acyl-D-aspartate amidohydrolase;
OS   Alcaligenes xylosoxydans xylosoxydans (Achromobacter xylosoxidans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Achromobacter.
OX   NCBI_TaxID=85698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=A-6;
RA   Wakayama M., Watanabe E., Takenaka Y., Miyamoto Y., Tau Y., Sakai K.,
RA   Moriguchi M.;
RT   "Cloning, expression, and nucleotide sequence of the N-acy1-D-aspartate
RT   amidohydrolase gene from Alcaligenes xylosoxydans subsp. xylosoxydans A-
RT   6.";
RL   J. Ferment. Bioeng. 80:311-317(1995).
RN   [2]
RP   CHARACTERIZATION.
RC   STRAIN=A-6;
RX   PubMed=7763985; DOI=10.1271/bbb.57.1145;
RA   Moriguchi M., Sakai K., Katsuno Y., Maki T., Wakayama M.;
RT   "Purification and characterization of novel N-acyl-D-aspartate
RT   amidohydrolase from Alcaligenes xylosoxydans subsp. xylosoxydans A-6.";
RL   Biosci. Biotechnol. Biochem. 57:1145-1148(1993).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-D-aspartate + H2O = a carboxylate + D-aspartate;
CC         Xref=Rhea:RHEA:18285, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:29990, ChEBI:CHEBI:57512; EC=3.5.1.83;
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. N-
CC       acyl-D-amino-acid deacylase family. {ECO:0000305}.
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DR   EMBL; D45919; BAA08350.1; -; Genomic_DNA.
DR   AlphaFoldDB; P94212; -.
DR   SMR; P94212; -.
DR   STRING; 1216976.AX27061_2768; -.
DR   KEGG; ag:BAA08350; -.
DR   eggNOG; COG3653; Bacteria.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047422; F:N-acyl-D-aspartate deacylase activity; IEA:UniProtKB-EC.
DR   Gene3D; 2.30.40.10; -; 1.
DR   Gene3D; 3.30.1490.130; -; 1.
DR   InterPro; IPR013108; Amidohydro_3.
DR   InterPro; IPR023100; D-aminoacylase_insert_dom_sf.
DR   InterPro; IPR011059; Metal-dep_hydrolase_composite.
DR   InterPro; IPR032466; Metal_Hydrolase.
DR   Pfam; PF07969; Amidohydro_3; 2.
DR   SUPFAM; SSF51338; SSF51338; 1.
DR   SUPFAM; SSF51556; SSF51556; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Hydrolase; Zinc.
FT   CHAIN           1..498
FT                   /note="N-acyl-D-aspartate deacylase"
FT                   /id="PRO_0000182706"
FT   REGION          478..498
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   498 AA;  53585 MW;  EAFF8662891F9F1B CRC64;
     MTDRSTLDDA PAQADFIIAG ATLIDGGGGP ARQGDLAVRG GRIVALGDFA HAPGVPVIDA
     RGLALAPGFI DSHTHDDGYL LAHPEMLPKV SQGITTVVTG NCGISLAPLS RRQIPQPLDL
     LGPPELFRFA TFRDWLRALA ETPAAVNVIP LVGHTTLRVA VMDDTGRAAT DAERAAMRAL
     LDEALQAGAF GVSTGTFYPP ASAAPTDEII DVCQPLRGRA GAIYATHLRD EADHIVPAME
     EALLIGRELD CRVVFSHHKL AGERNHGRSR ETLDMISRAA ATQRVCLDCH PYPATSTMLR
     LDRARLASRT LITWSKGYPE ATGRDFSEVM AELGLDDEAA IARLAPAGAI YFLMDQADVN
     RIFSHPLTTV GSDGLPFDPH PHPRQWGTFT NVLRTMVREQ RLLSLETAIH KMTGLAAAQY
     GLTERGLLRQ GYHADLVLFD PANVTDTATF SAPIQVSQGI HAVWVNGRQV WDGERTGAER
     PGQVLAPGDA IPWSQQSE