ID   A0A372K484_9BURK        Unreviewed;       493 AA.
AC   A0A372K484;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=D-aminoacylase {ECO:0000313|EMBL:RFU47030.1};
GN   ORFNames=D0B32_12735 {ECO:0000313|EMBL:RFU47030.1};
OS   Paraburkholderia sp. DHOC27.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=2303330 {ECO:0000313|EMBL:RFU47030.1, ECO:0000313|Proteomes:UP000263097};
RN   [1] {ECO:0000313|EMBL:RFU47030.1, ECO:0000313|Proteomes:UP000263097}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DHOC27 {ECO:0000313|EMBL:RFU47030.1,
RC   ECO:0000313|Proteomes:UP000263097};
RA   Gao Z.-H., Qiu L.-H.;
RT   "Paraburkholderia sp. DHOC27, isolated from subtropical forest soil.";
RL   Submitted (AUG-2018) 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:RFU47030.1}.
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DR   EMBL; QVQV01000003; RFU47030.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A372K484; -.
DR   OrthoDB; 9766983at2; -.
DR   Proteomes; UP000263097; Unassembled WGS sequence.
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; PTHR43135; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 1.
DR   PANTHER; PTHR43135:SF3; ALPHA-D-RIBOSE 1-METHYLPHOSPHONATE 5-TRIPHOSPHATE DIPHOSPHATASE; 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:UP000263097}.
FT   DOMAIN          50..464
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   493 AA;  53003 MW;  AB3B0AE965AD479B CRC64;
     MHSHPEAADT LIIDAQLYDG TGAPPVERDV AVRDGRIVAI GNLSNWLAEE VIEANGRALA
     PGFIDVHTHD DTHVIRAPQM LPKISQGVTT VIVGNCGISA SPVALKGDPP DPMNLLGERD
     AFSYPTFAAY VDAVNAARPA VNVGALIGHT ALRNNQMDRL DRAATPQEIE GMRAQLEEAL
     KNGALGLSSG LAYGSAFAAP TEEVMALAEP LAAAGALYTT HMRTEFDAIL DAMDEAYRVG
     RHASVPVVIS HLKCAGPSNW GRSTEVLKSL DGARRLQPVG CDCYPYNRSS STLDVKQVTG
     DIDITVTWST PHPEMAGKLV KEIAAEWGVT QQEAARRLQP AGAVYHNMSE EDVRRILSHP
     ASMVGSDGLP NDPLPHPRLW GAFPRVLGHY VRDAALLPLE EAIRKMTSLS ARRYGLAQRG
     EAHIGYHADL VLFDPERVRD AATFEKPQQP ADGIDAVWVN GVLSYRDGQP TGERAGHFVA
     RGVASRVDAQ GVF
//