ID   PRPE_GEOKA              Reviewed;         245 AA.
AC   Q5L1R3;
DT   21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   27-MAR-2024, entry version 83.
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}; OrderedLocusNames=GK0832;
OS   Geobacillus kaustophilus (strain HTA426).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=235909;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of thermophilic
RT   Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(2004).
CC   -!- FUNCTION: Asymmetrically hydrolyzes Ap4p to yield AMP and ATP.
CC       {ECO:0000255|HAMAP-Rule:MF_01443}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = 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;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01443};
CC   -!- SIMILARITY: Belongs to the PrpE family. {ECO:0000255|HAMAP-
CC       Rule:MF_01443}.
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DR   EMBL; BA000043; BAD75117.1; -; Genomic_DNA.
DR   RefSeq; WP_011230333.1; NC_006510.1.
DR   AlphaFoldDB; Q5L1R3; -.
DR   SMR; Q5L1R3; -.
DR   STRING; 235909.GK0832; -.
DR   KEGG; gka:GK0832; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_023125_3_0_9; -.
DR   Proteomes; UP000001172; Chromosome.
DR   GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-UniRule.
DR   CDD; cd07423; MPP_Prp_like; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_01443; PrpE; 1.
DR   InterPro; IPR023937; Bis(5'-nucleosyl)-tetraP_PrpE.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   InterPro; IPR041780; MPP_PrpE-like.
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   GTP-binding; Hydrolase; Nickel; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..245
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT                   [asymmetrical]"
FT                   /id="PRO_0000297703"
SQ   SEQUENCE   245 AA;  27839 MW;  5512991682FA220F CRC64;
     MQVDIIGDIH GCFREFAALT ETLGYHWDEG VPIHPDGRKL GFVGDLTDRG PESLNMIEIV
     CALVERNLAY YVPGNHCNKL YRFFLGRNVQ IAHGLETTVA EYRTLPPSEQ EMIRRKFIRL
     YEQAPLYAVL DEGRLVIAHA GIRHDYIGRT DKKVKTFVLY GDITGEMNQD GTPVRRDWAK
     RYHGSAWVVY GHTPVEKPRF VGRTVNIDTG CVFGGALTAL RYPEMETVSV PSSMPFVPEK
     FRTFS
//