ID   APAH_BURP2              Reviewed;         282 AA.
AC   I1WGA2; O69115; Q63RI5;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2012, sequence version 1.
DT   03-AUG-2022, entry version 40.
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=BP1026B_I0632;
OS   Burkholderia pseudomallei (strain 1026b).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=884204;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1026b;
RX   PubMed=9988483; DOI=10.1046/j.1365-2958.1998.01139.x;
RA   DeShazer D., Brett P.J., Woods D.E.;
RT   "The type II O-antigenic polysaccharide moiety of Burkholderia pseudomallei
RT   lipopolysaccharide is required for serum resistance and virulence.";
RL   Mol. Microbiol. 30:1081-1100(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1026b;
RX   PubMed=22615773; DOI=10.1371/journal.pone.0036507;
RA   Hayden H.S., Lim R., Brittnacher M.J., Sims E.H., Ramage E.R., Fong C.,
RA   Wu Z., Crist E., Chang J., Zhou Y., Radey M., Rohmer L., Haugen E.,
RA   Gillett W., Wuthiekanun V., Peacock S.J., Kaul R., Miller S.I., Manoil C.,
RA   Jacobs M.A.;
RT   "Evolution of Burkholderia pseudomallei in recurrent melioidosis.";
RL   PLoS ONE 7:E36507-E36507(2012).
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield
CC       ADP. {ECO:0000255|HAMAP-Rule:MF_00199}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 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; AF064070; AAD05453.1; -; Genomic_DNA.
DR   EMBL; CP002833; AFI65296.1; -; Genomic_DNA.
DR   RefSeq; WP_004522249.1; NZ_CP004379.1.
DR   AlphaFoldDB; I1WGA2; -.
DR   SMR; I1WGA2; -.
DR   EnsemblBacteria; AFI65296; AFI65296; BP1026B_I0632.
DR   GeneID; 56528510; -.
DR   KEGG; bpz:BP1026B_I0632; -.
DR   PATRIC; fig|884204.3.peg.689; -.
DR   Proteomes; UP000010087; Chromosome 1.
DR   GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:UniProtKB-UniRule.
DR   CDD; cd07422; MPP_ApaH; 1.
DR   Gene3D; 3.60.21.10; -; 1.
DR   HAMAP; MF_00199; ApaH; 1.
DR   InterPro; IPR004617; ApaH.
DR   InterPro; IPR004843; Calcineurin-like_PHP_ApaH.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1.
DR   SUPFAM; SSF56300; SSF56300; 1.
DR   TIGRFAMs; TIGR00668; apaH; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..282
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_0000429784"
SQ   SEQUENCE   282 AA;  30610 MW;  5D8BF833C5C27F44 CRC64;
     MTNFSSSPPI AFGDLQGCHA AYRQLFDTLA PAADTPLWFA GDLVNRGPAS LATLREIVAL
     GERAIAVLGN HDLHLLAVAA GIRTLKPGDT IGEILDAPDA DDLIEWVRHR PFAHFERGML
     MVHAGLLPQW DAALALELAD ELQRALRAPN WRDTLRSLYG NDPNCWSPDL KHADRLRVAF
     NAFTRIRFCT PEGAMEFRAN GGPAAAPAGY LPWFDAPGRK TADVTVVFGH WAALGLMLRE
     NLVALDSGCV WGNRLSAVRL ADDPAARVVT QVACERCGAA DE