ID APAH_BURPS STANDARD; PRT; 282 AA. AC O69115; Q63RI5; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1998, sequence version 1. DT 07-MAR-2006, entry version 39. DE Bis(5'-nucleosyl)-tetraphosphatase, symmetrical (EC 3.6.1.41) DE (Diadenosine tetraphosphatase) (Ap4A hydrolase) (Diadenosine 5',5'''- DE P1,P4-tetraphosphate pyrophosphohydrolase). GN Name=apaH; OrderedLocusNames=BPSL2687; OS Burkholderia pseudomallei (Pseudomonas pseudomallei). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia; pseudomallei group. OX NCBI_TaxID=28450; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=1026b; RX MEDLINE=99141012; PubMed=9988483; RA DeShazer D., Brett P.J., Woods D.E.; RT "The type II O-antigenic polysaccharide moiety of Burkholderia RT pseudomallei lipopolysaccharide is required for serum resistance and RT virulence."; RL Mol. Microbiol. 30:1081-1100(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K96243; RX PubMed=15377794; DOI=10.1073/pnas.0403302101; RA Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M., RA Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., RA Bentley S.D., Sebaihia M., Thomson N.R., Bason N., Beacham I.R., RA Brooks K., Brown K.A., Brown N.F., Challis G.L., Cherevach I., RA Chillingworth T., Cronin A., Crossett B., Davis P., DeShazer D., RA Feltwell T., Fraser A., Hance Z., Hauser H., Holroyd S., Jagels K., RA Keith K.E., Maddison M., Moule S., Price C., Quail M.A., RA Rabbinowitsch E., Rutherford K., Sanders M., Simmonds M., RA Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M., RA Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.; RT "Genomic plasticity of the causative agent of melioidosis, RT Burkholderia pseudomallei."; RL Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004). CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to CC yield ADP (By similarity). CC -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-adenosyl) tetraphosphate + CC H(2)O = 2 ADP. CC -!- SIMILARITY: Belongs to the Ap4A hydrolase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF064070; AAD05453.1; -; Genomic_DNA. DR EMBL; BX571965; CAH36695.1; -; Genomic_DNA. DR GenomeReviews; BX571965_GR; BPSL2687. DR HAMAP; MF_00199; -; 1. DR InterPro; IPR004617; ApaH. DR InterPro; IPR004843; M-pesterase. DR InterPro; IPR006186; T_phtase_apaH. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1. DR ProDom; PD000252; T_phtase_apaH; 1. DR TIGRFAMs; TIGR00668; apaH; 1. KW Complete proteome; Hydrolase. FT CHAIN 1 282 Bis(5'-nucleosyl)-tetraphosphatase, FT symmetrical. FT /FTId=PRO_0000197985. 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 //