ID   APAH_ECOLI              Reviewed;         280 AA.
AC   P05637; P78039;
DT   01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 2.
DT   16-DEC-2008, entry version 81.
DE   RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [symmetrical];
DE            EC=3.6.1.41;
DE   AltName: Full=Diadenosine tetraphosphatase;
DE   AltName: Full=Ap4A hydrolase;
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase;
GN   Name=apaH; OrderedLocusNames=b0049, JW0048;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87172305; PubMed=3031429; DOI=10.1007/BF00338091;
RA   Blanchin-Roland S., Blanquet S., Schmitter J.-M., Fayat G.;
RT   "The gene for Escherichia coli diadenosine tetraphosphatase is located
RT   immediately clockwise to folA and forms an operon with ksgA.";
RL   Mol. Gen. Genet. 205:515-522(1986).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12;
RX   MEDLINE=92334977; PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N.,
RA   Isono K., Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the
RT   0-2.4 min region.";
RL   Nucleic Acids Res. 20:3305-3308(1992).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   MEDLINE=97426617; PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1474(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION
RP   TO 83 AND 275.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   CHARACTERIZATION.
RC   STRAIN=K12;
RX   MEDLINE=84087863; PubMed=6317672;
RA   Guranowski A., Jakubowski H., Holler E.;
RT   "Catabolism of diadenosine 5',5''-P1,P4-tetraphosphate in procaryotes.
RT   Purification and properties of diadenosine 5',5''-P1,P4-tetraphosphate
RT   (symmetrical) pyrophosphohydrolase from Escherichia coli K12.";
RL   J. Biol. Chem. 258:14784-14789(1983).
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to
CC       yield ADP.
CC   -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-adenosyl) tetraphosphate +
CC       H(2)O = 2 ADP.
CC   -!- ENZYME REGULATION: Co(2+) is a strong stimulator (100-fold
CC       increase in rate of hydrolysis). Mn(2+), Cd(2+), Ni(2+), Mg(2+)
CC       and Ca(2+) are weak stimulators; the two latter act
CC       synergistically with Co(2+).
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the Ap4A hydrolase family.
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DR   EMBL; X04711; CAA28416.1; -; Genomic_DNA.
DR   EMBL; U00096; AAC73160.1; -; Genomic_DNA.
DR   EMBL; AP009048; BAB96617.2; -; Genomic_DNA.
DR   PIR; A64726; A64726.
DR   RefSeq; AP_000713.1; -.
DR   RefSeq; NP_414591.1; -.
DR   SMR; P05637; 2-268.
DR   ECO2DBASE; C031.3; 6TH EDITION.
DR   GeneID; 944770; -.
DR   GenomeReviews; AP009048_GR; JW0048.
DR   GenomeReviews; U00096_GR; b0049.
DR   KEGG; ecj:JW0048; -.
DR   KEGG; eco:b0049; -.
DR   EchoBASE; EB0046; -.
DR   EcoGene; EG10048; apaH.
DR   HOGENOM; P05637; -.
DR   BioCyc; EcoCyc:EG10048-MON; -.
DR   BioCyc; MetaCyc:EG10048-MON; -.
DR   GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetr...; IEA:HAMAP.
DR   HAMAP; MF_00199; -; 1.
DR   InterPro; IPR004617; ApaH.
DR   InterPro; IPR004843; M-pesterase.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1.
DR   TIGRFAMs; TIGR00668; apaH; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Hydrolase.
FT   CHAIN         1    280       Bis(5'-nucleosyl)-tetraphosphatase
FT                                [symmetrical].
FT                                /FTId=PRO_0000197988.
FT   CONFLICT     83     83       K -> L (in Ref. 1).
SQ   SEQUENCE   280 AA;  31297 MW;  BD6560C73446C1BB CRC64;
     MATYLIGDVH GCYDELIALL HKVEFTPGKD TLWLTGDLVA RGPGSLDVLR YVKSLGDSVR
     LVLGNHDLHL LAVFAGISRN KPKDRLTPLL EAPDADELLN WLRRQPLLQI DEEKKLVMAH
     AGITPQWDLQ TAKECARDVE AVLSSDSYPF FLDAMYGDMP NNWSPELRGL GRLRFITNAF
     TRMRFCFPNG QLDMYSKESP EEAPAPLKPW FAIPGPVAEE YSIAFGHWAS LEGKGTPEGI
     YALDTGCCWG GTLTCLRWED KQYFVQPSNR HKDLGEAAAS
//