PRPE_BACC7
ID PRPE_BACC7 Reviewed; 246 AA.
AC B7I0B6;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 62.
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=BCAH187_A1362;
OS Bacillus cereus (strain AH187).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=405534;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AH187;
RA Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Kolsto A.B.,
RA Okstad O.A., Ravel J., Sutton G.;
RT "Genome sequence of Bacillus cereus AH187.";
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=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; CP001177; ACJ77521.1; -; Genomic_DNA.
DR RefSeq; WP_000872720.1; NC_011658.1.
DR AlphaFoldDB; B7I0B6; -.
DR SMR; B7I0B6; -.
DR EnsemblBacteria; ACJ77521; ACJ77521; BCAH187_A1362.
DR KEGG; bcr:BCAH187_A1362; -.
DR HOGENOM; CLU_023125_3_0_9; -.
DR OMA; CNKLYRY; -.
DR OrthoDB; 900869at2; -.
DR Proteomes; UP000002214; Chromosome.
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 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 Hydrolase; Nickel.
FT CHAIN 1..246
FT /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT [asymmetrical]"
FT /id="PRO_1000145930"
SQ SEQUENCE 246 AA; 28225 MW; 3868DF986C032BFA CRC64;
MKYDIIGDIH GCLQEFQNLT EKLGYNWSSG LPVHPDQRKL AFVGDITDRG PHSLRMIEIV
WELVIHKKVA YYAPGNHCNK LYRFFLGRNV TIAHGLETTV AEYEALPSHK QNMIKEKFIT
LYEQSPLYHV LDEKRLLVCH AGIRQDYIGR QDKKVQTFVL YGDITGEKHA DGSPVRRDWA
KEYKGTTWIV YGHTPVKEPR FVNHTVNIDT GAVFGGKLTG LRYPEMEIVS VPSSLPFVPE
KFRPIS