ID   APAH_YERE8              Reviewed;         292 AA.
AC   A1JJF2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
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}; OrderedLocusNames=YE0628;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL10740.1; -; Genomic_DNA.
DR   RefSeq; WP_011815544.1; NC_008800.1.
DR   RefSeq; YP_001004980.1; NC_008800.1.
DR   AlphaFoldDB; A1JJF2; -.
DR   SMR; A1JJF2; -.
DR   STRING; 393305.YE0628; -.
DR   EnsemblBacteria; CAL10740; CAL10740; YE0628.
DR   KEGG; yen:YE0628; -.
DR   PATRIC; fig|393305.7.peg.721; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OMA; INAFTRM; -.
DR   Proteomes; UP000000642; Chromosome.
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..292
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_1000012108"
SQ   SEQUENCE   292 AA;  32690 MW;  C019C9411F527E0D CRC64;
     MSTYLIGDVH GCLDELLALL AQVDFDPQHD TLWLTGDLVA RGPASLDVLR YVRSLGPAVR
     MVLGNHDLHL LAVYAGISRN KPKDRITPLL EAPDADELIN WLRRQPVLQV DDELKLIMAH
     AGITPQWDIE TAQMCAREVE SVLSSDSYPL FLDAMYGDMP NNWSPELTGL ARLRFSTNAL
     TRMRFCFPNG QLDMICKDTP ENAPAPLKPW FELPRLVSPE YSIIFGHWAS LEGKGVPEGI
     YGLDTGCCWG GNLTLLRWED KRYFTQPAFK VEAEITNADE IAAAAKDPFS YL