ID   NDAD_ALCXX              Reviewed;         484 AA.
AC   P72349; O08051;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   25-MAY-2022, entry version 96.
DE   RecName: Full=D-aminoacylase;
DE            EC=3.5.1.81;
DE   AltName: Full=N-acyl-D-amino-acid deacylase;
GN   Name=dan;
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], AND PARTIAL PROTEIN SEQUENCE.
RC   STRAIN=A-6;
RX   PubMed=8541651; DOI=10.1271/bbb.59.2115;
RA   Wakayama M., Katsuno Y., Hayashi S., Miyamoto Y., Sakai K., Moriguchi M.;
RT   "Cloning and sequencing of a gene encoding D-aminoacylase from Alcaligenes
RT   xylosoxydans subsp. xylosoxydans A-6 and expression of the gene in
RT   Escherichia coli.";
RL   Biosci. Biotechnol. Biochem. 59:2115-2119(1995).
CC   -!- FUNCTION: Has a wide specificity; hydrolyzes N-acyl derivative of
CC       neutral D-amino acids.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-D-amino acid + H2O = a carboxylate + a D-alpha-amino
CC         acid; Xref=Rhea:RHEA:18309, ChEBI:CHEBI:15377, ChEBI:CHEBI:29067,
CC         ChEBI:CHEBI:59871, ChEBI:CHEBI:59876; EC=3.5.1.81;
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; S80683; AAB35881.1; -; Genomic_DNA.
DR   EMBL; D45918; BAA08349.1; -; Genomic_DNA.
DR   PIR; JC4394; JC4394.
DR   RefSeq; WP_026385007.1; NZ_CYTP01000001.1.
DR   AlphaFoldDB; P72349; -.
DR   SMR; P72349; -.
DR   STRING; 1216976.AX27061_2896; -.
DR   eggNOG; COG3653; Bacteria.
DR   BRENDA; 3.5.1.81; 238.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0047420; F:N-acyl-D-amino-acid 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; Direct protein sequencing; Hydrolase; Zinc.
FT   INIT_MET        1
FT                   /note="Removed"
FT   CHAIN           2..484
FT                   /note="D-aminoacylase"
FT                   /id="PRO_0000182704"
SQ   SEQUENCE   484 AA;  52053 MW;  A112F80297085C6A CRC64;
     MSQSDSQPFD LLLAGGTLID GSNTPGRRAD LGVRGDRIAA IGDLSDAAAH TRVDVSGLVV
     APGFIDSHTH DDNYLLRRRD MTPKISQGVT TVVTGNCGIS LAPLAHANPP APLDLLDEGG
     SYRFERFADY LDALRATPAA VNAACMVGHS TLRAAVMPDL QRAATDEEIA AMRDLAEEAM
     ASGAIGISTG AFYPPAARAT TEEIIEVCRP LSAHGGIYAT HMRDEGEHIV AALEETFRIG
     RELDVPVVIS HHKVMGQPNF GRSRETLPLI EAAMARQDVS LDAYPYVAGS TMLKQDRVLL
     AGRTIITWCK PFPELSGRDL DEVAAERGKS KYDVVPELQP AGAIYFMMDE PDVQRILAFG
     PTMIGSDGLP HDERPHPRLW GTFPRVLGHY ARDLGLFPLE TAVWKMTGLT AARFGLAGRG
     QLQAGYFADL VVFDPATVAD TATFEHPTER AAGIHSVYVN GAPVWQEQAF TGQHAGRVLA
     RTAA