ID   APAH_BUCAP              Reviewed;         273 AA.
AC   Q8K9Z9;
DT   15-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 106.
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=BUsg_135;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield
CC       ADP. {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the Ap4A hydrolase family. {ECO:0000305}.
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DR   EMBL; AE013218; AAM67703.1; -; Genomic_DNA.
DR   RefSeq; WP_011053670.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9Z9; -.
DR   SMR; Q8K9Z9; -.
DR   STRING; 198804.BUsg_135; -.
DR   EnsemblBacteria; AAM67703; AAM67703; BUsg_135.
DR   KEGG; bas:BUsg_135; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OMA; INAFTRM; -.
DR   OrthoDB; 900869at2; -.
DR   Proteomes; UP000000416; 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..273
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_0000197982"
SQ   SEQUENCE   273 AA;  32424 MW;  0A3932B6C04AF711 CRC64;
     MSIYFISDIH GCYKEFKLLL KKSFFNDKKD FLWIAGDLVS RGPDSLKVIR YLYSLRKRIK
     IILGNHDLNL IAVYSGVKEN KKENYFDEFL SAKDNLQLIN WLRCQSILKI DEERKIIMSH
     AGISPKWDID TAKKYALEIE KCLSGKNYSS FLRSVFNNKI NYWNLNLNKL DRLRYSINVF
     TRMRYCYPDS RLNLICKKSP NLVKYPLIPW FKIPNKIPKE YSVFFGHWSS LIGTKVPQPF
     FPLDSGCCWG GKLTMFRWED KKYFFQSFQK NNS