ID   APAH_PSEU5              Reviewed;         275 AA.
AC   A4VHH8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-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=PST_0724;
OS   Pseudomonas stutzeri (strain A1501).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=379731;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A1501;
RX   PubMed=18495935; DOI=10.1073/pnas.0801093105;
RA   Yan Y., Yang J., Dou Y., Chen M., Ping S., Peng J., Lu W., Zhang W.,
RA   Yao Z., Li H., Liu W., He S., Geng L., Zhang X., Yang F., Yu H., Zhan Y.,
RA   Li D., Lin Z., Wang Y., Elmerich C., Lin M., Jin Q.;
RT   "Nitrogen fixation island and rhizosphere competence traits in the genome
RT   of root-associated Pseudomonas stutzeri A1501.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:7564-7569(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; CP000304; ABP78429.1; -; Genomic_DNA.
DR   RefSeq; WP_011911936.1; NC_009434.1.
DR   AlphaFoldDB; A4VHH8; -.
DR   SMR; A4VHH8; -.
DR   STRING; 379731.PST_0724; -.
DR   EnsemblBacteria; ABP78429; ABP78429; PST_0724.
DR   GeneID; 66819864; -.
DR   KEGG; psa:PST_0724; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OMA; INAFTRM; -.
DR   Proteomes; UP000000233; 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; Reference proteome.
FT   CHAIN           1..275
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_1000012083"
SQ   SEQUENCE   275 AA;  30842 MW;  745B832B97C6C9C0 CRC64;
     MTTYAVGDLQ GCLEPLTCLL ERVDFSPSRD CLWLAGDLVN RGPQSLEALR FVRDLESSAI
     TVLGNHDLHL LAVAHNIERM RKSDTLQAIL DAPDRADLID WLRQQKLIHY DAERHTAMVH
     AGIPPQWSLE KALRRAAEVE QALQDDALLL PFLDGMYGNQ PAKWNKELHG VPRLRLITNY
     FTRMRFCKAD GTLDLDAKEG ADSAPAGYAP WFSHASRKTR NVKLIFGHWA ALEGQCDEPN
     VFALDTGCVW GNAMTLMNLD SGEMHRCECE HGKPA