APAH_BURM9
ID APAH_BURM9 Reviewed; 282 AA.
AC A2S9T5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
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};
GN OrderedLocusNames=BMA10229_A2752;
OS Burkholderia mallei (strain NCTC 10229).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=412022;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 10229;
RX PubMed=20333227; DOI=10.1093/gbe/evq003;
RA Losada L., Ronning C.M., DeShazer D., Woods D., Fedorova N., Kim H.S.,
RA Shabalina S.A., Pearson T.R., Brinkac L., Tan P., Nandi T., Crabtree J.,
RA Badger J., Beckstrom-Sternberg S., Saqib M., Schutzer S.E., Keim P.,
RA Nierman W.C.;
RT "Continuing evolution of Burkholderia mallei through genome reduction and
RT large-scale rearrangements.";
RL Genome Biol. Evol. 2:102-116(2010).
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; CP000546; ABN03254.1; -; Genomic_DNA.
DR RefSeq; WP_004186146.1; NC_008836.1.
DR AlphaFoldDB; A2S9T5; -.
DR SMR; A2S9T5; -.
DR EnsemblBacteria; ABN03254; ABN03254; BMA10229_A2752.
DR GeneID; 56594993; -.
DR KEGG; bml:BMA10229_A2752; -.
DR HOGENOM; CLU_056184_1_0_4; -.
DR OMA; INAFTRM; -.
DR Proteomes; UP000002283; Chromosome I.
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_1000012047"
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