APAH_BURMA
ID APAH_BURMA Reviewed; 282 AA.
AC Q9AEV8; Q62I92;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 2.
DT 03-AUG-2022, 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=BMA1991;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=11790757; DOI=10.1128/jb.184.3.849-852.2002;
RA Burtnick M.N., Brett P.J., Woods D.E.;
RT "Molecular and physical characterization of Burkholderia mallei O
RT antigens.";
RL J. Bacteriol. 184:849-852(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M., Daugherty S.C.,
RA Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J., Durkin A.S.,
RA Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F., Madupu R., Mohammoud Y.,
RA Nelson W.C., Radune D., Romero C.M., Sarria S., Selengut J., Shamblin C.,
RA Sullivan S.A., White O., Yu Y., Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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; AY028370; AAK27390.1; -; Genomic_DNA.
DR EMBL; CP000010; AAU49991.1; -; Genomic_DNA.
DR RefSeq; WP_004186146.1; NC_006348.1.
DR RefSeq; YP_103578.1; NC_006348.1.
DR AlphaFoldDB; Q9AEV8; -.
DR SMR; Q9AEV8; -.
DR STRING; 243160.BMA1991; -.
DR EnsemblBacteria; AAU49991; AAU49991; BMA1991.
DR GeneID; 56594993; -.
DR KEGG; bma:BMA1991; -.
DR PATRIC; fig|243160.12.peg.2058; -.
DR eggNOG; COG0639; Bacteria.
DR HOGENOM; CLU_056184_1_0_4; -.
DR OMA; INAFTRM; -.
DR Proteomes; UP000006693; Chromosome 1.
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..282
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_0000197984"
FT CONFLICT 90
FT /note="T -> S (in Ref. 1; AAK27390)"
FT /evidence="ECO:0000305"
FT CONFLICT 96
FT /note="D -> Y (in Ref. 1; AAK27390)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="A -> P (in Ref. 1; AAK27390)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 282 AA; 30572 MW; 665D4AA4D13EDF9D CRC64;
MTNFSSSPPI AFGDLQGCHA AYRQLFDTLA PAADTPLWFA GDLVNRGPAS LATLREIAAL
GERAIAVLGN HDLHLLAVAA GIRTLKPGDT IGEILDAPDA DDLIEWVRHR PFAHFERGML
MVHAGLLPQW DAALALELAD ELQRALRASN WRDTLRSLYG NDPNCWSPDL KHADRLRVAF
NAFTRIRFCT PEGAMEFRAN GGPAAAPAGY LPWFDAPGRK TADVTVVFGH WAALGLMLRE
NLVALDSGCV WGNRLSAVRL ADDPAARVVT QVACERCGAA DE