ID APAH_COXBU Reviewed; 291 AA.
AC Q83AB7;
DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 108.
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=CBU_1987;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=227377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RSA 493 / Nine Mile phase I;
RX PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA Fraser C.M., Heidelberg J.F.;
RT "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO91476.1; -; Genomic_DNA.
DR RefSeq; NP_820962.1; NC_002971.3.
DR RefSeq; WP_010958582.1; NC_002971.4.
DR AlphaFoldDB; Q83AB7; -.
DR SMR; Q83AB7; -.
DR STRING; 227377.CBU_1987; -.
DR EnsemblBacteria; AAO91476; AAO91476; CBU_1987.
DR GeneID; 1209900; -.
DR KEGG; cbu:CBU_1987; -.
DR PATRIC; fig|227377.7.peg.1974; -.
DR eggNOG; COG0639; Bacteria.
DR HOGENOM; CLU_056184_2_0_6; -.
DR OrthoDB; 9807890at2; -.
DR Proteomes; UP000002671; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IBA:GO_Central.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0110154; P:RNA decapping; IBA:GO_Central.
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 NCBIfam; TIGR00668; apaH; 1.
DR PANTHER; PTHR42850:SF11; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [SYMMETRICAL]; 1.
DR PANTHER; PTHR42850; METALLOPHOSPHOESTERASE; 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..291
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_0000197987"
SQ SEQUENCE 291 AA; 33300 MW; 27FB606C6A0D9765 CRC64;
MDARAINSRE KADLKYPRNT YIIGDVQGCY RELQELLELI QFDSTKDRLG FVGDLVNRGP
NSLEVLRFLK SLSSPLIVLG NHDLYLLILG YGLMPEDSYE HTLHAVLQAP DKLELLEWLR
HSPLIRYEKS LSAVLVHAGL PPQWNIKESI LHAEEISTAL KGPHYLAFLK NLFGNEPSQW
KEDLEGQDRL RYICNAFTRM RFCDAKGHLD LESEGKTNQA PSRFRPWFEW RNPQEDNVDI
VFGHWAALNG QSSAPHTHAL DTGCAWGYKL TAINLKTKER FSVPCQSALR M
//
