ID   PRPE_BACC2              Reviewed;         246 AA.
AC   B7ILE8;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   02-SEP-2026, entry version 77.
DE   RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase PrpE [asymmetrical] {ECO:0000255|HAMAP-Rule:MF_01443};
DE            EC=3.6.1.17 {ECO:0000255|HAMAP-Rule:MF_01443};
DE   AltName: Full=Ap4A hydrolase {ECO:0000255|HAMAP-Rule:MF_01443};
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase {ECO:0000255|HAMAP-Rule:MF_01443};
DE            Short=Diadenosine tetraphosphatase {ECO:0000255|HAMAP-Rule:MF_01443};
GN   Name=prpE {ECO:0000255|HAMAP-Rule:MF_01443};
GN   OrderedLocusNames=BCG9842_B4084;
OS   Bacillus cereus (strain G9842).
OC   Bacteria; Bacillati; Bacillota; Bacilli; Caryophanales; Bacillaceae;
OC   Bacillus; Bacillus cereus group.
OX   NCBI_TaxID=405531;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=G9842;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus G9842.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_01443}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=P(1),P(4)-bis(5'-guanosyl) tetraphosphate + H2O = GMP + GTP +
CC         2 H(+); Xref=Rhea:RHEA:22484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57553, ChEBI:CHEBI:58115; EC=3.6.1.17;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01443};
CC   -!- COFACTOR:
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01443};
CC   -!- SIMILARITY: Belongs to the PrpE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01443}.
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; CP001186; ACK98023.1; -; Genomic_DNA.
DR   RefSeq; WP_000872690.1; NC_011772.1.
DR   AlphaFoldDB; B7ILE8; -.
DR   SMR; B7ILE8; -.
DR   KEGG; bcg:BCG9842_B4084; -.
DR   HOGENOM; CLU_023125_3_0_9; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016791; F:phosphatase activity; IEA:TreeGrafter.
DR   CDD; cd07423; MPP_Prp_like; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_01443; PrpE; 1.
DR   InterPro; IPR050126; Ap4A_hydrolase.
DR   InterPro; IPR023937; Bis(5'-nucleosyl)-tetraP_PrpE.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041780; MPP_PrpE-like.
DR   NCBIfam; NF010148; PRK13625.1; 1.
DR   PANTHER; PTHR42850:SF7; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE PRPE [ASYMMETRICAL]; 1.
DR   PANTHER; PTHR42850; METALLOPHOSPHOESTERASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Nickel.
FT   CHAIN           1..246
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT                   [asymmetrical]"
FT                   /id="PRO_1000145928"
SQ   SEQUENCE   246 AA;  28263 MW;  29419ED342A04096 CRC64;
     MKYDIIGDIH GCFQEFQNLT EKLGYNWSSG LPIHPEQRKL AFVGDITDRG PHSLRMIEIV
     WELVIHKKEA YYAPGNHCNK LYRFFLGRNV TIAHGLETTV AEYEALPSHK QNIIKEKFIT
     LYEQSPLYHI LDEKKVIVCH AGIRQDYIGR RDKKVQTFVL YGDITGEKHA DGSPVRRDWA
     QEYKGQAWIV YGHTPVKEPR FVNQTVNIDT GAVFGGKLTG LRYPEMETIS VPSSLPFVAE
     KFRPIS
//