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Database: UniProt
Entry: D2R0K3_PIRSD
LinkDB: D2R0K3_PIRSD
Original site: D2R0K3_PIRSD 
ID   D2R0K3_PIRSD            Unreviewed;       522 AA.
AC   D2R0K3;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   SubName: Full=N-acyl-D-amino-acid deacylase {ECO:0000313|EMBL:ADB16601.1};
DE            EC=3.5.1.81 {ECO:0000313|EMBL:ADB16601.1};
GN   OrderedLocusNames=Psta_1927 {ECO:0000313|EMBL:ADB16601.1};
OS   Pirellula staleyi (strain ATCC 27377 / DSM 6068 / ICPB 4128) (Pirella
OS   staleyi).
OC   Bacteria; Planctomycetota; Planctomycetia; Pirellulales; Pirellulaceae;
OC   Pirellula.
OX   NCBI_TaxID=530564 {ECO:0000313|EMBL:ADB16601.1, ECO:0000313|Proteomes:UP000001887};
RN   [1] {ECO:0000313|EMBL:ADB16601.1, ECO:0000313|Proteomes:UP000001887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27377 / DSM 6068 / ICPB 4128
RC   {ECO:0000313|Proteomes:UP000001887};
RX   PubMed=21304671; DOI=10.4056/sigs.51657;
RA   Clum A., Tindall B.J., Sikorski J., Ivanova N., Mavrommatis K., Lucas S.,
RA   Glavina del Rio T., Nolan M., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Ovchinikova G., Pati A., Mikhailova N., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Chang Y.J., Jeffries C.D., Chain P.,
RA   Rohde M., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Complete genome sequence of Pirellula staleyi type strain (ATCC 27377).";
RL   Stand. Genomic Sci. 1:308-316(2009).
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DR   EMBL; CP001848; ADB16601.1; -; Genomic_DNA.
DR   RefSeq; WP_012910864.1; NC_013720.1.
DR   AlphaFoldDB; D2R0K3; -.
DR   STRING; 530564.Psta_1927; -.
DR   KEGG; psl:Psta_1927; -.
DR   eggNOG; COG3653; Bacteria.
DR   HOGENOM; CLU_016107_2_1_0; -.
DR   Proteomes; UP000001887; Chromosome.
DR   GO; GO:0047420; F:N-acyl-D-amino-acid deacylase activity; IEA:UniProtKB-EC.
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; PTHR11113; N-ACETYLGLUCOSAMINE-6-PHOSPHATE DEACETYLASE; 1.
DR   Pfam; PF07969; Amidohydro_3; 2.
DR   SUPFAM; SSF51338; Composite domain of metallo-dependent hydrolases; 1.
DR   SUPFAM; SSF51556; Metallo-dependent hydrolases; 1.
PE   4: Predicted;
KW   Hydrolase {ECO:0000313|EMBL:ADB16601.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001887}.
FT   DOMAIN          44..188
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
FT   DOMAIN          391..499
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   522 AA;  58349 MW;  6076B41397E819A7 CRC64;
     MFDLLFRGGM VLDGSGGPSL RADVGVLGDQ ITAVGDLSHA SATRVVDVSG RVIAPGFIDV
     HNHSEGWLLS HKNFWPKTSQ GFTTEVLMAD GISYAPVDRH NWREWIYYLR SLNGLRYEQY
     QGWQSIADYL SLLDRRTAQN VIAHVPYANC RVLAQGWGRH APDDFQMRQI RNEIRLGMEQ
     GCVGLSTGMD YVGECFASTD ELVEACKVIA PYQGLYVTHV RYKMGLLPAF REAVEIGRRS
     GARVHISHLK ATSTQDVDEV LAFCDWASRE VDFSFDVYPY QRGSTMLNYL LPYEVWDDGP
     LAVLSKLGKS EVLERFRIAL AQSGTPIERY TIAWTNTWDN STHHGKLLSE YVEEMGRSPE
     EALYHLLLEE NLATLLVIDS GDDQLIEPIL QHPKFMLGSD GIYFPDSVVH PRVYGSTGRL
     LGPCVREKRL FTLADAVYKM TLAPARRFGL AGRGQIAEGC FADLVIFDPD SVGDLATYDQ
     PHQVCTGIEQ VVVNGVVIVD NSQPVHFLGE ELPGRVLKYQ PV
//
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