ID   APAH_BAUCH              Reviewed;         288 AA.
AC   Q1LSS3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   28-JAN-2026, entry version 105.
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};
GN   OrderedLocusNames=BCI_0562;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Candidatus Palibaumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA   Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT   sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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=P(1),P(4)-bis(5'-adenosyl) tetraphosphate + H2O = 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; CP000238; ABF13981.1; -; Genomic_DNA.
DR   RefSeq; WP_011520724.1; NC_007984.1.
DR   AlphaFoldDB; Q1LSS3; -.
DR   SMR; Q1LSS3; -.
DR   STRING; 374463.BCI_0562; -.
DR   KEGG; bci:BCI_0562; -.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OrthoDB; 9807890at2; -.
DR   Proteomes; UP000002427; 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.
DR   InterPro; IPR029052; Metallo-depent_PP-like.
DR   NCBIfam; TIGR00668; apaH; 1.
DR   NCBIfam; NF001204; PRK00166.1; 1.
DR   PANTHER; PTHR40942; -; 1.
DR   PANTHER; PTHR40942:SF4; CYTOCHROME C5; 1.
DR   Pfam; PF00149; Metallophos; 1.
DR   PIRSF; PIRSF000903; B5n-ttraPtase_sm; 1.
DR   SUPFAM; SSF56300; Metallo-dependent phosphatases; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..288
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_1000012045"
SQ   SEQUENCE   288 AA;  33032 MW;  F0BF5E76254BA1E2 CRC64;
     MSTYFIGDIH GCYDELQTIL EKVAFDPLID TLWLTGDLVA RGPSSLEVLR MIRRLGNSVR
     IVLGNHDLHL LAVYTGIMRN RIKDHTIPLL TAPDAEDLMN WLRYQPVLQV DNKKKILMAH
     AGITPQWNID TALQCASEIE TVLRSESYPL FLHSIYEDIP NYWSNELSYR ARLQFSTNVF
     TRMRYCFPNG KLDMLCKDIP NKAPEPLRPW FNLPSTIVEK YSIIFGHWSS LLGKGTPTGI
     YGLDTGCCWG GKLTLLCWED KKIIQIPSQK KRNKKCSYLC YNGKGKKN
//