PRPE_GEOTN
ID PRPE_GEOTN Reviewed; 245 AA.
AC A4IL88;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 76.
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=GTNG_0712;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO66092.1; -; Genomic_DNA.
DR RefSeq; WP_011886949.1; NC_009328.1.
DR AlphaFoldDB; A4IL88; -.
DR SMR; A4IL88; -.
DR STRING; 420246.GTNG_0712; -.
DR EnsemblBacteria; ABO66092; ABO66092; GTNG_0712.
DR KEGG; gtn:GTNG_0712; -.
DR eggNOG; COG0639; Bacteria.
DR HOGENOM; CLU_023125_3_0_9; -.
DR OMA; CNKLYRY; -.
DR OrthoDB; 900869at2; -.
DR Proteomes; UP000001578; 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..245
FT /note="Bis(5'-nucleosyl)-tetraphosphatase PrpE
FT [asymmetrical]"
FT /id="PRO_0000297704"
SQ SEQUENCE 245 AA; 27791 MW; B075BA5C62B354B7 CRC64;
MHIDIIGDIH GCYREFTALT EKLGYVWDKG IPIHPDGRKL GFVGDLTDRG PESLKMIDIV
CALVDRKLAH YVPGNHCNKL YRFFLGRNVQ VTHGLETTVA EYRALPPSEQ EMIRRKFIRL
YEGAPLYAVL DEGRLVIAHA GIRHDYIGRM DKKVKTFVLY GDITGETNPD GTPVRRDWAK
RYRGDAWIVY GHTPVEKPRF VGRTVNIDTG CVFGGALTAL RYPEMTTVSV PSSMPHVPEK
FRTFS