ID   APAH_SALCH              Reviewed;         282 AA.
AC   Q57TH2;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   25-MAY-2022, entry version 88.
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=SCH_0083;
OS   Salmonella choleraesuis (strain SC-B67).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=321314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SC-B67;
RX   PubMed=15781495; DOI=10.1093/nar/gki297;
RA   Chiu C.-H., Tang P., Chu C., Hu S., Bao Q., Yu J., Chou Y.-Y., Wang H.-S.,
RA   Lee Y.-S.;
RT   "The genome sequence of Salmonella enterica serovar Choleraesuis, a highly
RT   invasive and resistant zoonotic pathogen.";
RL   Nucleic Acids Res. 33:1690-1698(2005).
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; AE017220; AAX63989.1; -; Genomic_DNA.
DR   RefSeq; WP_001538938.1; NC_006905.1.
DR   AlphaFoldDB; Q57TH2; -.
DR   SMR; Q57TH2; -.
DR   EnsemblBacteria; AAX63989; AAX63989; SCH_0083.
DR   KEGG; sec:SCH_0083; -.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OMA; INAFTRM; -.
DR   Proteomes; UP000000538; 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..282
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_1000012086"
SQ   SEQUENCE   282 AA;  31477 MW;  EFC5958B7313F8A2 CRC64;
     MATYLIGDVH GCYDELIALL QQVEFTPDTD TLWLTGDLVA RGPGSLDMLR YVKSLGNSVR
     LVLGNHDLHL LAVFAGISRN KPKDRLTPLL EAPDADELLN WLRRQPLLQV DEEKKLIMAH
     AGITPQWDLQ TAKECARDVE AVLSSDSYPF FLDAMYGDMP NNWSPELSGL ARLRFITNAF
     TRMRYCFPNG QLDMYSKASP ENAPAPLKPW FAIPGPVSEA YSIAFGHWAS LEGKGTPEGI
     YALDTGCCWG GELTCLRWED KQYFVQPSNR QMDMGEGEAV NA