ID E5GAJ3_BURPE Unreviewed; 282 AA.
AC E5GAJ3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 24-JAN-2024, entry version 59.
DE RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase, symmetrical {ECO:0000256|HAMAP-Rule:MF_00199};
DE EC=3.6.1.41 {ECO:0000256|HAMAP-Rule:MF_00199};
DE AltName: Full=Ap4A hydrolase {ECO:0000256|HAMAP-Rule:MF_00199};
DE AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00199};
DE AltName: Full=Diadenosine tetraphosphatase {ECO:0000256|HAMAP-Rule:MF_00199};
GN Name=apaH {ECO:0000256|HAMAP-Rule:MF_00199,
GN ECO:0000313|EMBL:ADQ27819.1};
GN ORFNames=BURP1950_LPSb01 {ECO:0000313|EMBL:ADQ27819.1}, BURP446_LPSb22
GN {ECO:0000313|EMBL:ADQ27861.1};
OS Burkholderia pseudomallei (Pseudomonas pseudomallei).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=28450 {ECO:0000313|EMBL:ADQ27819.1};
RN [1] {ECO:0000313|EMBL:ADQ27861.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSHR446 {ECO:0000313|EMBL:ADQ27861.1};
RA Stone J.K., Gruendike J.M., Georgia S., Warrington S., Currie B.,
RA Wagner D., Keim P., Tuanyok A.;
RL Submitted (AUG-2010) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ADQ27819.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=MSHR1950 {ECO:0000313|EMBL:ADQ27819.1};
RX PubMed=22235357; DOI=10.1371/journal.pntd.0001453;
RA Tuanyok A., Stone J.K., Mayo M., Kaestli M., Gruendike J., Georgia S.,
RA Warrington S., Mullins T., Allender C.J., Wagner D.M., Chantratita N.,
RA Peacock S.J., Currie B.J., Keim P.;
RT "The genetic and molecular basis of O-antigenic diversity in Burkholderia
RT pseudomallei lipopolysaccharide.";
RL PLoS Negl. Trop. Dis. 6:E1453-E1453(2012).
CC -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to yield
CC ADP. {ECO:0000256|ARBA:ARBA00003413, ECO:0000256|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:0000256|ARBA:ARBA00001682, ECO:0000256|HAMAP-
CC Rule:MF_00199};
CC -!- SIMILARITY: Belongs to the Ap4A hydrolase family.
CC {ECO:0000256|ARBA:ARBA00005419, ECO:0000256|HAMAP-Rule:MF_00199}.
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DR EMBL; HM852062; ADQ27819.1; -; Genomic_DNA.
DR EMBL; HQ023427; ADQ27861.1; -; Genomic_DNA.
DR RefSeq; WP_038770988.1; NZ_LXAW01000041.1.
DR AlphaFoldDB; E5GAJ3; -.
DR PATRIC; fig|28450.150.peg.239; -.
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 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 {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00199}.
FT DOMAIN 11..148
FT /note="Calcineurin-like phosphoesterase"
FT /evidence="ECO:0000259|Pfam:PF00149"
SQ SEQUENCE 282 AA; 30626 MW; 318BF834A9C27F48 CRC64;
MTNFSSSPPI AFGDLQGCHA AYRQLFDTLA LAADTPLWFA GDLVNRGPAS LATLREIVAL
GERAIAVLGN HDLHLLAVAA GIRTLKPGDT IGEILDAPDA DDLIEWVRHR PFAHFERGML
MVHAGLLPQW DAALALELAD ELQRALRAPN WRDTLRSLYG NDPNCWSPDL KHADRLRVAF
NAFTRIRFCT PEGAMEFRAN GGPAAAPAGY LPWFDAPGRK TADVTVVFGH WAALGLMLRE
NLVALDSGCV WGNRLSAVRL ADDPAARVVT QVACERCGAA DE
//
