ID A0A1V6MJG2_9ACTN Unreviewed; 538 AA.
AC A0A1V6MJG2;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:OQD52508.1};
GN ORFNames=BM536_030500 {ECO:0000313|EMBL:OQD52508.1};
OS Streptomyces phaeoluteigriseus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=114686 {ECO:0000313|EMBL:OQD52508.1, ECO:0000313|Proteomes:UP000184286};
RN [1] {ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|Proteomes:UP000184286};
RA Schniete J.K., Salih T., Algora Gallardo L., Martinez Fernandez S.,
RA Herron P.R.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OQD52508.1, ECO:0000313|Proteomes:UP000184286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 41896 {ECO:0000313|EMBL:OQD52508.1,
RC ECO:0000313|Proteomes:UP000184286};
RA Salih T.S., Algora Gallardo L., Melo Santos T., Filgueira Martinez S.,
RA Herron P.R.;
RT "Draft genome sequence of Streptomyces phaeoluteigriseus type strain
RT DSM41896.";
RL Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OQD52508.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MPOH02000019; OQD52508.1; -; Genomic_DNA.
DR RefSeq; WP_073490863.1; NZ_MPOH02000019.1.
DR AlphaFoldDB; A0A1V6MJG2; -.
DR STRING; 114686.BM536_030500; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000184286; Unassembled WGS sequence.
DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro.
DR CDD; cd01297; D-aminoacylase; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 2.
DR InterPro; IPR013108; Amidohydro_3.
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;
FT DOMAIN 51..517
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 538 AA; 57747 MW; 4C2F61E66A3CE3F0 CRC64;
MEDLVIRDAD VVDGTGADSY RADVVVDGGR IVSIVKEAAA AGCQRPKAVR ELDAEGLVLS
PGFIDMHAHS DLALLRDPDH SAKAAQGVTL EVLGQDGLSY APVDDRTLDG VRRSIAGWNG
SGEDIDFDWR SVGEYLDRLD RGIAVNAAYL IPQGTVRALV VGWDDREATP AELDRMRQLV
AEGLEQGAVG MSSGLTYTPG MYAKNAELTE LCRVVASYGG YYCPHHRSYG AGALEAYAEM
VELSRQAGCP LHLAHATMNF GVNEGRAPEL LALLDEALAA GADLTLDTYP YTAGCTTLVA
LLPSWASEGG PEETLRRLTD DGTAERIRHE LEALGSDGCH GVPVDWDTIE ISGVGGAGLG
EYVGRTVRES AALRGEAPWA TARRLLVEDR LAPAILQHVG HEENVRAIMR HRVHTGGSDG
ILQGTKPHPR AYGTFPRYLG QYVRELGVLS LEECVARLTG RPAARLRLPD RGLIREGHRA
DLVLFDPRTV AAGSTYDAPR TPPTGIPYVL VDGRFVIEDG RRTDVLAGRA VRRGPVAG
//