NDED_ALCXX
ID NDED_ALCXX Reviewed; 488 AA.
AC P94211;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1997, sequence version 1.
DT 25-MAY-2022, entry version 101.
DE RecName: Full=N-acyl-D-glutamate deacylase {ECO:0000305};
DE EC=3.5.1.82 {ECO:0000269|PubMed:8537313};
DE AltName: Full=D-AGase {ECO:0000303|PubMed:8537313};
DE AltName: Full=N-acyl-D-glutamate amidohydrolase {ECO:0000303|PubMed:8537313};
GN Name=dag {ECO:0000303|PubMed:8537313};
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], PROTEIN SEQUENCE OF 1-20, CATALYTIC
RP ACTIVITY, ACTIVITY REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=A-6;
RX PubMed=8537313; DOI=10.1093/oxfordjournals.jbchem.a124879;
RA Wakayama M., Ashika T., Miyamoto Y., Yoshikawa T., Sonoda Y., Sakai K.,
RA Moriguchi M.;
RT "Primary structure of N-acyl-D-glutamate amidohydrolase from Alcaligenes
RT xylosoxydans subsp. xylosoxydans A-6.";
RL J. Biochem. 118:204-209(1995).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an N-acyl-D-glutamate + H2O = a carboxylate + D-glutamate;
CC Xref=Rhea:RHEA:12833, ChEBI:CHEBI:15377, ChEBI:CHEBI:17503,
CC ChEBI:CHEBI:29067, ChEBI:CHEBI:29986; EC=3.5.1.82;
CC Evidence={ECO:0000269|PubMed:8537313};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by cobalt, copper and EDTA.
CC {ECO:0000269|PubMed:8537313}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:8537313};
CC Temperature dependence:
CC Optimum temperature is 55 degrees Celsius.
CC {ECO:0000269|PubMed:8537313};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
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; D50061; BAA08778.1; -; Genomic_DNA.
DR PIR; JC4165; JC4165.
DR RefSeq; WP_006384305.1; NZ_LN890476.1.
DR AlphaFoldDB; P94211; -.
DR SMR; P94211; -.
DR STRING; 1216976.AX27061_3945; -.
DR PATRIC; fig|85698.22.peg.5897; -.
DR eggNOG; COG3653; Bacteria.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0047421; F:N-acyl-D-glutamate 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 CHAIN 1..488
FT /note="N-acyl-D-glutamate deacylase"
FT /id="PRO_0000182705"
SQ SEQUENCE 488 AA; 51493 MW; F5A1B8315BEA167F CRC64;
MQEKLDLVIE GGWVIDGLGG PRRRADVGIR GERIAAIGDL SAAPADRRLD AGGRIVAPGF
IDTHGHDDLM FVEKPGLEWK TSQGITSVVV GNCGISGAPA PLPGNTAAAL ALLGDSPLFA
DMAMYFGALE AQRPMINVAA LVGHANLRLA AMRDPAAQPS AKEQRAMERM LADALEAGAV
GFSTGLAYQP GGVAEQAELD GLARVAAARG ALHTSHIRNE GDAVEAAVDE VLAVGRRTGC
ATVLSHHKCM MPANWGKSAA TLANIDRARA AGVDVALDIY PYPGSSTILI PERADQIDDI
RITWSTPHPE CGGQSLAEIA ARWGCDAVTA ARRLCPAGAI YFAMDENEVR RIFQHECCMV
GSDGLPNDAH PHPRLWGSFT RVLGRYVREA ELLTLEAAVA KMTALPARVF GLADRGRLAV
GAWADVVVFD ADTVCDRATW DAPTLASAGI EHVLVNGCAV FPQAPPSHRP GRILRRDASI
AGAPEFSR
