APAH_COXBN
ID APAH_COXBN Reviewed; 291 AA.
AC A9KH04;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 25-MAY-2022, entry version 82.
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=CBUD_2085;
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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; CP000733; ABS77008.1; -; Genomic_DNA.
DR RefSeq; WP_011997409.1; NC_009727.1.
DR AlphaFoldDB; A9KH04; -.
DR SMR; A9KH04; -.
DR EnsemblBacteria; ABS77008; ABS77008; CBUD_2085.
DR KEGG; cbd:CBUD_2085; -.
DR HOGENOM; CLU_056184_2_0_6; -.
DR OMA; INAFTRM; -.
DR OrthoDB; 900869at2; -.
DR Proteomes; UP000008555; 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..291
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_1000077712"
SQ SEQUENCE 291 AA; 33302 MW; 4C9FB329F52D9764 CRC64;
MDARAINSRE KADLKYPRNT YIIGDVQGCY RELQELLELI QFDSTKDRLG FVGDLVNRGP
NSLEVLRFLK SLSSPLIVLG NHDLYLLILG YGLMPEDSYE HTLHAVLQAP DKLELLEWLR
HCPLIRYEKS LSAVLVHAGL PPQWNIKESI LHAEEISTAL KGPHYLAFLK NLFGNEPSQW
KDDLEGQDRL RYICNAFTRM RFCDAKGHLD LESEGKTNQA PSRFRPWFEW RNPQEDNVDI
VFGHWAALNG QSSAPHTHAL DTGCAWGYKL TAINLKTKER FSVPCQSALR M