APAH_AERS4
ID APAH_AERS4 Reviewed; 273 AA.
AC A4SR08;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 84.
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=ASA_3352;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(2008).
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; CP000644; ABO91330.1; -; Genomic_DNA.
DR RefSeq; WP_005311698.1; NC_009348.1.
DR AlphaFoldDB; A4SR08; -.
DR SMR; A4SR08; -.
DR STRING; 382245.ASA_3352; -.
DR EnsemblBacteria; ABO91330; ABO91330; ASA_3352.
DR KEGG; asa:ASA_3352; -.
DR eggNOG; COG0639; Bacteria.
DR HOGENOM; CLU_056184_2_0_6; -.
DR OMA; INAFTRM; -.
DR OrthoDB; 900869at2; -.
DR Proteomes; UP000000225; 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..273
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_1000012042"
SQ SEQUENCE 273 AA; 31103 MW; A4ACA17FA8FA8CC7 CRC64;
MANCFVGDIQ GCYDDLRRLL DLAKFDPAKD VLWLCGDLVA RGPDSLKTLR YVKSLGQRAV
TVLGNHDLHL LAVADGVAPL KKKDKLQALM EAPDRDELLT WLRHRPLLAE HPDLPIMMVH
AGISPAWDAR TARNCAREVE SLLRGDQYSW LLHNMYGDLP DGWSEDLAGI ERYRYIINTF
TRMRFCYFDG RLEFKCKKGP TESTPGLRPW FEQREHHMDD PILVFGHWAA LMGNTGRNDI
KALDTGCVWG NSLTLWRYED DALIATPCPT HAK