ID   APAH_ACTP7              Reviewed;         270 AA.
AC   B3GXJ7;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 77.
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=APP7_0804;
OS   Actinobacillus pleuropneumoniae serotype 7 (strain AP76).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=537457;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AP76;
RA   Linke B., Buettner F., Martinez-Arias R., Goesmann A., Baltes N.,
RA   Tegetmeyer H., Singh M., Gerlach G.F.;
RT   "Genome and proteome analysis of A. pleuropneumoniae serotype 7.";
RL   Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001091; ACE61456.1; -; Genomic_DNA.
DR   RefSeq; WP_011848461.1; NC_010939.1.
DR   AlphaFoldDB; B3GXJ7; -.
DR   SMR; B3GXJ7; -.
DR   EnsemblBacteria; ACE61456; ACE61456; APP7_0804.
DR   GeneID; 66259635; -.
DR   KEGG; apa:APP7_0804; -.
DR   PATRIC; fig|416269.6.peg.795; -.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OMA; INAFTRM; -.
DR   BioCyc; APLE537457:APP7_RS04075-MON; -.
DR   Proteomes; UP000001226; 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..270
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_1000099313"
SQ   SEQUENCE   270 AA;  31224 MW;  9D0715E800D9020D CRC64;
     MATYIVGDLH GCFDELQLLL KQVNYNPAQD ELWLTGDLVA RGAKSLECLR FVKDPKNNAK
     TILGNHDLHL LATLLGVKKV KPNDQVDAIF AAEDRADLQN WLRNQPLLIQ HPKYGFLLTH
     AGISPEWNLT ETIACAREAE AVLQSGHYAD YIAQMYENTP DHWSAEWQGI ERWRYIINVF
     TRMRFCYADK RLDFACKLPV EDAPNELKPW FKLDNPLFHQ QDIIFGHWAS LMGKADKPNI
     YALDTGCAWG NHLTMIRWED KQIFTQERLK