ID A0A0C5G0P6_9ACTN Unreviewed; 536 AA.
AC A0A0C5G0P6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=N-acyl-D-amino acid deacylase {ECO:0000313|EMBL:AJP03558.1};
GN ORFNames=TU94_20815 {ECO:0000313|EMBL:AJP03558.1};
OS Streptomyces cyaneogriseus subsp. noncyanogenus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=477245 {ECO:0000313|EMBL:AJP03558.1, ECO:0000313|Proteomes:UP000032234};
RN [1] {ECO:0000313|EMBL:AJP03558.1, ECO:0000313|Proteomes:UP000032234}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NMWT 1 {ECO:0000313|EMBL:AJP03558.1,
RC ECO:0000313|Proteomes:UP000032234};
RA Wang H., Li C., Xiang W., Wang X.;
RT "Genome sequence of thermotolerant Streptomyces cyaneogriseus subsp.
RT Noncyanogenus NMWT1, the producer of nematocidal antibiotics nemadectin.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP010849; AJP03558.1; -; Genomic_DNA.
DR RefSeq; WP_044383442.1; NZ_CP010849.1.
DR AlphaFoldDB; A0A0C5G0P6; -.
DR STRING; 477245.TU94_20815; -.
DR KEGG; scw:TU94_20815; -.
DR PATRIC; fig|477245.3.peg.4390; -.
DR HOGENOM; CLU_016107_2_1_11; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000032234; Chromosome.
DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.30.1490.130; D-aminoacylase. Domain 3; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.30.40.10; Urease, subunit C, domain 1; 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 PANTHER; PTHR11647:SF99; D-PHENYLHYDANTOINASE-RELATED; 1.
DR PANTHER; PTHR11647; HYDRANTOINASE/DIHYDROPYRIMIDINASE FAMILY MEMBER; 1.
DR Pfam; PF07969; Amidohydro_3; 1.
DR SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000032234}.
FT DOMAIN 51..517
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 536 AA; 57792 MW; A8643E71CDB9EDD7 CRC64;
MEDLVIRDAD VVDGSGAPSY RADVVVDGGR IVSIVKEAAA AGCQRPSATR ELDAEGLVLS
PGFIDMHAHS DLALLRDPDH SAKAAQGVTL EVIGQDGLSY APVDDRTLEE VRRAIAGWNG
PGDDIDFDWR SVGEYLDRLD RGIAVNAAYL VPQGTVRALA VGWEDRPATE AELDRMRRLV
AQGLEQGAVG LSSGLTYTPG MYAEDAELTE LCRVVARYGG YYCPHHRSYG AGALEAYREM
VELTRAAGCP LHLAHATMNF GVNKGRAPEL LTLLDEALAA GADITLDTYP YTPGCTTLAA
LLPSWASEGG PEAVLGRLAD DGTAERIRHH MEAVGSDGCH GVPVEWETIE ISGVSDPALA
EYVGRTVLES ARLRGETPWA VARRLLLADR LAPTILQHVG HEENVRAIMR HRVHTGGSDG
ILQGSKPHPR AYGTFPHYLG RYVRELGVLS LEECVAHLTS RPAARLRLPD RGLVREGHRA
DLVLFDPATV AAGSTFAEPR ALPTGIPYVL VDGRFVIEDG RRTDVLAGRS VRRTPR
//