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   03-AUG-2022, entry version 169.
DE   RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [symmetrical];
DE            EC=3.6.1.41;
DE   AltName: Full=Ap4A hydrolase;
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase;
DE   AltName: Full=Diadenosine tetraphosphatase;
GN   Name=apaH; OrderedLocusNames=b0049, JW0048;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   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   PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA   Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA   Mizobuchi K., Nakata A.;
RT   "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT   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   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., Mau B.,
RA   Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO 83
RP   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 MG1655
RT   and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND SUBUNIT.
RC   STRAIN=K12;
RX   PubMed=6317672; DOI=10.1016/s0021-9258(17)43729-x;
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).
RN   [6]
RP   IDENTIFICATION BY 2D-GEL.
RX   PubMed=9298644; DOI=10.1002/elps.1150180805;
RA   VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT   "Escherichia coli proteome analysis using the gene-protein database.";
RL   Electrophoresis 18:1243-1251(1997).
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield
CC       ADP. {ECO:0000269|PubMed:6317672}.
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:0000269|PubMed:6317672};
CC   -!- ACTIVITY REGULATION: Co(2+) is a strong stimulator (100-fold increase
CC       in rate of hydrolysis). Mn(2+), Cd(2+), Ni(2+), Mg(2+) and Ca(2+) are
CC       weak stimulators; the two latter act synergistically with Co(2+).
CC       {ECO:0000269|PubMed:6317672}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:6317672}.
CC   -!- SIMILARITY: Belongs to the Ap4A hydrolase family. {ECO:0000305}.
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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; NP_414591.1; NC_000913.3.
DR   RefSeq; WP_000257192.1; NZ_STEB01000010.1.
DR   AlphaFoldDB; P05637; -.
DR   SMR; P05637; -.
DR   BioGRID; 4262205; 12.
DR   BioGRID; 849172; 3.
DR   DIP; DIP-9113N; -.
DR   IntAct; P05637; 5.
DR   STRING; 511145.b0049; -.
DR   jPOST; P05637; -.
DR   PaxDb; P05637; -.
DR   PRIDE; P05637; -.
DR   EnsemblBacteria; AAC73160; AAC73160; b0049.
DR   EnsemblBacteria; BAB96617; BAB96617; BAB96617.
DR   GeneID; 944770; -.
DR   KEGG; ecj:JW0048; -.
DR   KEGG; eco:b0049; -.
DR   PATRIC; fig|1411691.4.peg.2234; -.
DR   EchoBASE; EB0046; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   InParanoid; P05637; -.
DR   OMA; INAFTRM; -.
DR   PhylomeDB; P05637; -.
DR   BioCyc; EcoCyc:EG10048-MON; -.
DR   BioCyc; MetaCyc:EG10048-MON; -.
DR   PRO; PR:P05637; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IDA:EcoCyc.
DR   GO; GO:0008796; F:bis(5'-nucleosyl)-tetraphosphatase activity; IMP:EcoliWiki.
DR   GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR   GO; GO:0015949; P:nucleobase-containing small molecule interconversion; IMP:EcoliWiki.
DR   GO; GO:0010165; P:response to X-ray; IMP:EcoCyc.
DR   GO; GO:0110154; P:RNA decapping; IDA:EcoCyc.
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   1: Evidence at protein level;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..280
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase [symmetrical]"
FT                   /id="PRO_0000197988"
FT   CONFLICT        83
FT                   /note="K -> L (in Ref. 1; CAA28416)"
FT                   /evidence="ECO:0000305"
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