ID APAH_BURPS STANDARD; PRT; 282 AA. AC O69115; Q63RI5; DT 30-MAY-2000 (Rel. 39, Created) DT 30-MAY-2000 (Rel. 39, Last sequence update) DT 01-FEB-2005 (Rel. 46, Last annotation update) 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. OX NCBI_TaxID=28450; RN [1] RP NUCLEOTIDE SEQUENCE. 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 This Swiss-Prot entry is copyright. It is produced through a collaboration CC between the Swiss Institute of Bioinformatics and the EMBL outstation - CC the European Bioinformatics Institute. There are no restrictions on its CC use as long as its content is in no way modified and this statement is not CC removed. CC -------------------------------------------------------------------------- DR EMBL; AF064070; AAD05453.1; -. DR EMBL; BX571965; CAH36695.1; -. 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. 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 //