ID   APAH_BUCBP              Reviewed;         278 AA.
AC   Q89AV3;
DT   19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   28-JAN-2026, entry version 118.
DE   RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000255|HAMAP-Rule:MF_00199};
DE            EC=3.6.1.41 {ECO:0000255|HAMAP-Rule:MF_00199};
DE   AltName: Full=Ap4A hydrolase {ECO:0000255|HAMAP-Rule:MF_00199};
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00199};
DE   AltName: Full=Diadenosine tetraphosphatase {ECO:0000255|HAMAP-Rule:MF_00199};
GN   Name=apaH {ECO:0000255|HAMAP-Rule:MF_00199};
GN   OrderedLocusNames=bbp_132;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Enterobacterales; Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield
CC       ADP. {ECO:0000255|HAMAP-Rule:MF_00199}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=P(1),P(4)-bis(5'-adenosyl) tetraphosphate + H2O = 2 ADP + 2
CC         H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:58141, ChEBI:CHEBI:456216; EC=3.6.1.41;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00199};
CC   -!- SIMILARITY: Belongs to the Ap4A hydrolase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00199}.
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DR   EMBL; AE016826; AAO26866.1; -; Genomic_DNA.
DR   RefSeq; WP_011091267.1; NC_004545.1.
DR   AlphaFoldDB; Q89AV3; -.
DR   SMR; Q89AV3; -.
DR   STRING; 224915.bbp_132; -.
DR   KEGG; bab:bbp_132; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OrthoDB; 9807890at2; -.
DR   Proteomes; UP000000601; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:TreeGrafter.
DR   GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0016791; F:phosphatase activity; IEA:TreeGrafter.
DR   GO; GO:0110154; P:RNA decapping; IEA:TreeGrafter.
DR   CDD; cd07422; MPP_ApaH; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_00199; ApaH; 1.
DR   InterPro; IPR050126; Ap4A_hydrolase.
DR   InterPro; IPR004617; ApaH.
DR   InterPro; IPR004843; Calcineurin-like_PHP.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   NCBIfam; TIGR00668; apaH; 1.
DR   NCBIfam; NF001204; PRK00166.1; 1.
DR   PANTHER; PTHR42850:SF11; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [SYMMETRICAL]; 1.
DR   PANTHER; PTHR42850; METALLOPHOSPHOESTERASE; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..278
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_0000197983"
SQ   SEQUENCE   278 AA;  32363 MW;  D24AF9A3B5E0EC29 CRC64;
     MSTYFIGDIH GCFNELMHLL EKVSFDANSD VLWLTGDLIN RGPKSLEVLR FVSSLGDNVK
     MVLGNHDVNL IALYASIKNS KKSSLMNNLL KSHDIDYLIY WLRKQPLFRV DHKKKIIMSH
     AGMYPYWDIQ TASCYAKKIE SMLCNHNYDT FLDFLYNNSD IKSKLYECTV FKNRELECLK
     LALNVFTRMR YCLPNGELDM TCKQSPSKNI SSLLPWFFIK NSCLEDYCVF FGHWASLEKN
     ITPKNIISLD TGCCWGGILS MFRLEDKKWF VQESEIKK
//