ID A0A0Q5PCM8_9BURK Unreviewed; 494 AA.
AC A0A0Q5PCM8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=D-aminoacylase {ECO:0000313|EMBL:KQR84716.1};
GN ORFNames=ASG35_28385 {ECO:0000313|EMBL:KQR84716.1};
OS Burkholderia sp. Leaf177.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1736287 {ECO:0000313|EMBL:KQR84716.1, ECO:0000313|Proteomes:UP000051826};
RN [1] {ECO:0000313|EMBL:KQR84716.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR84716.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR84716.1, ECO:0000313|Proteomes:UP000051826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf177 {ECO:0000313|EMBL:KQR84716.1,
RC ECO:0000313|Proteomes:UP000051826};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) 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:KQR84716.1}.
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; LMPF01000006; KQR84716.1; -; Genomic_DNA.
DR RefSeq; WP_056355765.1; NZ_LMPF01000006.1.
DR AlphaFoldDB; A0A0Q5PCM8; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000051826; 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; 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:UP000051826}.
FT DOMAIN 52..465
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 494 AA; 52641 MW; F52E4E9F0D7F10DC CRC64;
MALDSQTHAD TLIKGARVID GTGAPAVQCD VAVKDGQIVA IGALGQWTAE NVVEAEGRVL
APGFIDVHTH DDTHVIRSPE MLPKISQGVT TVIVGNCGIS ASPVTLKGAP PDPMNLLGAQ
GDFKYPTFAA YIDAVNHARP AVNVGALIGH TALRNNHMDR LDRGASADEI EGMRAQLEQA
LAHGALGLSS GLAYGSAFSA PPEEVMALAE PLANAGALYT THMRTEFDAI LDAMDEAYRV
GKHARVPVVI SHLKCAGPSN WGRSTEVLKS LDRVRDGQPV GCDCYPYNRS SSTLDVKQVT
GDIDITITWS TPHPEMAGKL ISEVAAEWQV TQQEAGKRLQ PAGAVYHNMS EDDVRRILSH
PATMVGSDGL PNDPLPHPRL WGAFPRVLGH YARDTTLVPL EEAVRKMTGL SARRFGLPGR
GLVKVAYHAD LVLFDADKVR DTATFAEPRQ TADGIDAVWV NGALSYLDGA VTGLRAGRFV
ARGEASKLDT AGHF
//