PRPE_BACC1
ID PRPE_BACC1 Reviewed; 246 AA.
AC Q73BU4;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
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=BCE_1324;
OS Bacillus cereus (strain ATCC 10987 / NRS 248).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=222523;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 10987 / NRS 248;
RX PubMed=14960714; DOI=10.1093/nar/gkh258;
RA Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL Nucleic Acids Res. 32:977-988(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; AE017194; AAS40253.1; -; Genomic_DNA.
DR RefSeq; WP_000872682.1; NC_003909.8.
DR AlphaFoldDB; Q73BU4; -.
DR SMR; Q73BU4; -.
DR EnsemblBacteria; AAS40253; AAS40253; BCE_1324.
DR GeneID; 59159025; -.
DR KEGG; bca:BCE_1324; -.
DR HOGENOM; CLU_023125_3_0_9; -.
DR OMA; CNKLYRY; -.
DR Proteomes; UP000002527; 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 Pfam; PF00149; Metallophos; 1.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW GTP-binding; Hydrolase; Nickel; Nucleotide-binding.
FT CHAIN 1..246
FT /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT [asymmetrical]"
FT /id="PRO_0000297696"
SQ SEQUENCE 246 AA; 28279 MW; 6D26BA9B4189D21F CRC64;
MKYDIIGDIH GCFQEFQDLT KKLGYNWNSD LPIHPDQRKL AFVGDITDRG PHSLRMIEIV
WELVINKKVA YYAPGNHCNK LYRFFLGRNV TIAHGLETTV AEYEALPSHQ QNMIKEKFIT
LYEQSPLYHV LDEKRLIVCH AGIRQDYIGR QDKKVQTFVL YGDITGEKHA DGSPVRRDWA
KEYKGTAWVV YGHTPVKEPR FVNHTVNIDT GAVFGGKLTG LRYPEMETVS VPSSLPFVPE
KFRPIS