GenomeNet

Database: UniProt
Entry: B3RBY2_CUPTR
LinkDB: B3RBY2_CUPTR
Original site: B3RBY2_CUPTR 
ID   B3RBY2_CUPTR            Unreviewed;       504 AA.
AC   B3RBY2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 80.
DE   SubName: Full=N-acyl-D-aspartate deacylase (N-acyl-D-aspartate amidohydrolase) {ECO:0000313|EMBL:CAQ72407.1};
DE            EC=3.5.1.83 {ECO:0000313|EMBL:CAQ72407.1};
GN   OrderedLocusNames=RALTA_B1823 {ECO:0000313|EMBL:CAQ72407.1};
OS   Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS   107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=977880 {ECO:0000313|EMBL:CAQ72407.1, ECO:0000313|Proteomes:UP000001692};
RN   [1] {ECO:0000313|EMBL:CAQ72407.1, ECO:0000313|Proteomes:UP000001692}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 /
RC   R1 {ECO:0000313|Proteomes:UP000001692};
RX   PubMed=18490699; DOI=10.1101/gr.076448.108;
RA   Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA   Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA   Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA   Masson-Boivin C.;
RT   "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT   comparative genomics of rhizobia.";
RL   Genome Res. 18:1472-1483(2008).
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; CU633750; CAQ72407.1; -; Genomic_DNA.
DR   RefSeq; WP_012356622.1; NC_010530.1.
DR   AlphaFoldDB; B3RBY2; -.
DR   GeneID; 29765552; -.
DR   KEGG; cti:RALTA_B1823; -.
DR   eggNOG; COG3653; Bacteria.
DR   HOGENOM; CLU_016107_2_0_4; -.
DR   BioCyc; CTAI977880:RALTA_RS24370-MONOMER; -.
DR   Proteomes; UP000001692; Chromosome 2.
DR   GO; GO:0047422; F:N-acyl-D-aspartate deacylase activity; IEA:UniProtKB-EC.
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   Hydrolase {ECO:0000313|EMBL:CAQ72407.1}.
FT   DOMAIN          54..466
FT                   /note="Amidohydrolase 3"
FT                   /evidence="ECO:0000259|Pfam:PF07969"
SQ   SEQUENCE   504 AA;  54094 MW;  03FAACEE51F97807 CRC64;
     MASQSPAPQR ADLLFRHATV VDGTGATRRT ADVAVTGDRI IAVGDCAGIA ADHTVDCSGR
     VLAPGFIDAH THDDGYLLVH RDMTPKVSQG ITTVVTGNCG ISVAPLVSGA PPQPLDLLGP
     PALFRFDTFA QWLDALRAAP ANVNVVPLLG HSTLRVRAMP ELDRPANDAE IAAMRDEVRL
     AMEAGAFGVS TGTFYPPAAA ATEAEIIAVC GPVRSHGGIY STHLRDETDA IVPSIEEALR
     IGRALDCPVV FSHHKVAGKR NHGRSVETLG LLAEAARLQP LCLDCHPYPA TSTMLRLDRV
     RQSTRTLITW STGYPAAGGR DFHELMQELG LDEEALLARL RPAAAIYFIM DERDVARIAQ
     FPLTIFGSDG LPFDPRPHPR QWGTFPRILA RMVREDQLMT LEAAIHKMSG LAAQQYGLED
     RGRIAPGAFA DLVLFDAGRV QDRATFEDPL QLSTGIDGVW VNGARVWQQS AQDGAGDTAG
     SALPAFSGRV LRRLASDNPS AARR
//
DBGET integrated database retrieval system