ID A0A1H5RIZ9_9PSEU Unreviewed; 531 AA.
AC A0A1H5RIZ9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 16.
DE SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:SEF38309.1};
GN ORFNames=SAMN05421837_12033 {ECO:0000313|EMBL:SEF38309.1};
OS Amycolatopsis pretoriensis.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=218821 {ECO:0000313|EMBL:SEF38309.1, ECO:0000313|Proteomes:UP000198878};
RN [1] {ECO:0000313|EMBL:SEF38309.1, ECO:0000313|Proteomes:UP000198878}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44654 {ECO:0000313|EMBL:SEF38309.1,
RC ECO:0000313|Proteomes:UP000198878};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FNUJ01000020; SEF38309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H5RIZ9; -.
DR STRING; 218821.SAMN05421837_12033; -.
DR OrthoDB; 9766983at2; -.
DR Proteomes; UP000198878; 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; 2.
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;
FT DOMAIN 43..507
FT /note="Amidohydrolase 3"
FT /evidence="ECO:0000259|Pfam:PF07969"
SQ SEQUENCE 531 AA; 56990 MW; 7F2E2D3265FF1112 CRC64;
MDVVVKNALV ADGTGEPLAR HDVGITDGRI AEVAEAGSLT GGRTIDADGL VLAPGFIDMH
SHSDLQLLAN PDHPAKITQG VTTEVLGQDG LSYAPVDDTV LEALRQQLAG WNDDPAGFDW
NWRSVGEYLD RLDQGVAVNA AYLVPQGTVR MLTVGWDDRP ATDAELTRMK ELVATGLDEG
AMGMSSGLTY TPGMYAETSE LVELCRVVGE GGGFYSPHHR SYGKGALEAF AEMIDVSRRS
GCPLHLAHAT MNFSVNKGKA PDLLKLLDDA LDDGCDISLD TYPYLPGATY LSALLPSWAT
EGGLDATLAR LSDVDERERI RAEIEESGSD GAHGVPIDWD AIEINGVRHE HNNHLVGHSV
AASARTRGTE PAKLYFDTLL DEKLGTSCLM HVGHEENVQA IMRHRTHTGG SDGLLVGARP
HPRAWGTFPR YLARYVRELG VLDLAECVAH LTGRAARRLR LADRGLVRAG YAADLVLFDP
DAVADTATFD DPRQPAAGIT HVFVNGVAAL DDGRPTGALA GHSLRNPRRA R
//