ID   APAH_NEIMA              Reviewed;         276 AA.
AC   Q9JVF4; A1IQR3;
DT   27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 112.
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=NMA0860;
OS   Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS   Z2491).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15465 / Z2491;
RX   PubMed=10761919; DOI=10.1038/35006655;
RA   Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA   Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA   Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA   Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA   Barrell B.G.;
RT   "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT   Z2491.";
RL   Nature 404:502-506(2000).
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; AL157959; CAM08097.1; -; Genomic_DNA.
DR   PIR; H81931; H81931.
DR   RefSeq; WP_002231975.1; NC_003116.1.
DR   AlphaFoldDB; Q9JVF4; -.
DR   SMR; Q9JVF4; -.
DR   EnsemblBacteria; CAM08097; CAM08097; NMA0860.
DR   KEGG; nma:NMA0860; -.
DR   HOGENOM; CLU_056184_2_0_4; -.
DR   OMA; INAFTRM; -.
DR   BioCyc; NMEN122587:NMA_RS04320-MON; -.
DR   Proteomes; UP000000626; 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..276
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_0000197999"
SQ   SEQUENCE   276 AA;  31116 MW;  8D71929FA25C5471 CRC64;
     MAHYAIGDIQ GCFDELTALL GKIGFNHGTD TLWLTGDIVN RGPKSLETLQ FCIRHENSVQ
     IVLGNHDLHL LAVGYGEGAP KRSDTIEPIL KHPDGRKMLD WLRAQPLLIR EGNRVMVHAG
     ILPQWRITKA ESLAGEAEAE LRGKKYVKFF SKMYGNKPAA WDEGLEGYAR LRFIVNAFTR
     MRALTFKNEL DFDYKSTVKK MPLYLRPWFK APDRQNLDHT IIFGHWSSLG YTNADNVISL
     DTGALWGGQL TAVNLETEEI TQVQAAGGID WKSFTK