PRPE_ANOFW
ID PRPE_ANOFW Reviewed; 245 AA.
AC B7GLK2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 25-MAY-2022, entry version 66.
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=Aflv_2112;
OS Anoxybacillus flavithermus (strain DSM 21510 / WK1).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Anoxybacillus.
OX NCBI_TaxID=491915;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21510 / WK1;
RX PubMed=19014707; DOI=10.1186/gb-2008-9-11-r161;
RA Saw J.H., Mountain B.W., Feng L., Omelchenko M.V., Hou S., Saito J.A.,
RA Stott M.B., Li D., Zhao G., Wu J., Galperin M.Y., Koonin E.V.,
RA Makarova K.S., Wolf Y.I., Rigden D.J., Dunfield P.F., Wang L., Alam M.;
RT "Encapsulated in silica: genome, proteome and physiology of the
RT thermophilic bacterium Anoxybacillus flavithermus WK1.";
RL Genome Biol. 9:R161.1-R161.16(2008).
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; CP000922; ACJ34471.1; -; Genomic_DNA.
DR RefSeq; WP_012575652.1; NC_011567.1.
DR AlphaFoldDB; B7GLK2; -.
DR SMR; B7GLK2; -.
DR STRING; 491915.Aflv_2112; -.
DR EnsemblBacteria; ACJ34471; ACJ34471; Aflv_2112.
DR KEGG; afl:Aflv_2112; -.
DR PATRIC; fig|491915.6.peg.2169; -.
DR eggNOG; COG0639; Bacteria.
DR HOGENOM; CLU_023125_3_0_9; -.
DR OMA; CNKLYRY; -.
DR OrthoDB; 900869at2; -.
DR Proteomes; UP000000742; 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 InterPro; IPR006186; Ser/Thr-sp_prot-phosphatase.
DR Pfam; PF00149; Metallophos; 1.
DR PRINTS; PR00114; STPHPHTASE.
DR SUPFAM; SSF56300; SSF56300; 1.
PE 3: Inferred from homology;
KW Hydrolase; Nickel; Reference proteome.
FT CHAIN 1..245
FT /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT [asymmetrical]"
FT /id="PRO_1000145926"
SQ SEQUENCE 245 AA; 27854 MW; 3FFE2F79986D4F48 CRC64;
MIYDIIGDIH GCFHEFMLLT KKLGYVWEND VPIHPNGRKL AFVGDLADRG PQSLQVIDTV
ISLVQQNKAV YVPGNHCDKL YRFFLGRNVQ VTHGLETTVA EWEQADEKTK TRIRTQFMKL
YENAPLYAIL DDGKLVIAHA GIRGDYIGKS NQKVKKFVLY GDITGEKHPD GSPVRRDWAK
HYRGDALIVY GHTPVKEPRW LNNTVNIDTG CVFGGQLTAL RYPEMETVSV PSTMPYVAEK
FRPFD