ID   APAH_XYLF2              Reviewed;         295 AA.
AC   B2I5R6;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-JUN-2008, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=XfasM23_1290;
OS   Xylella fastidiosa (strain M23).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=405441;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M23;
RX   PubMed=20601474; DOI=10.1128/jb.00651-10;
RA   Chen J., Xie G., Han S., Chertkov O., Sims D., Civerolo E.L.;
RT   "Whole genome sequences of two Xylella fastidiosa strains (M12 and M23)
RT   causing almond leaf scorch disease in California.";
RL   J. Bacteriol. 192:4534-4534(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; CP001011; ACB92711.1; -; Genomic_DNA.
DR   RefSeq; WP_011098001.1; NC_010577.1.
DR   AlphaFoldDB; B2I5R6; -.
DR   SMR; B2I5R6; -.
DR   EnsemblBacteria; ACB92711; ACB92711; XfasM23_1290.
DR   GeneID; 58016749; -.
DR   KEGG; xfn:XfasM23_1290; -.
DR   HOGENOM; CLU_056184_0_0_6; -.
DR   OMA; INAFTRM; -.
DR   Proteomes; UP000001698; 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..295
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_1000099341"
FT   REGION          271..295
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        278..295
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   295 AA;  33637 MW;  95D4FE648A6FA711 CRC64;
     MSIWAIGDLQ GCYDATQRLL ENIRFDPSQD TLWFCGDLVN RGGQSLETLR LVHSLRSHSV
     VVLGNHDLSL LAVTVRSEEE QRKVNPDLLR IITAEDRDEI LTWLRMQKLI HVDRTIGWMM
     VHAGLAPKWT TQMAEKLAHE VEQQLHGTDY RKLLHSMYGD KPEWSPALSG CNRSRAIINV
     LTRMRYCTPR GRISTEDKGT PGTQTQGMYP WFEVPGRVER DLKIVCGHWS TLGLTITQGI
     HAIDTGAVWG GKLTALQIDT DELRLAQVHG LSIEHPRHTH TPRRKAKKRH KRSPK