ID   APAH_THISH              Reviewed;         270 AA.
AC   B8GMY8;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   25-MAY-2022, entry version 69.
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=Tgr7_2728;
OS   Thioalkalivibrio sulfidiphilus (strain HL-EbGR7).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Thioalkalivibrio.
OX   NCBI_TaxID=396588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HL-EbGR7;
RX   PubMed=21475584; DOI=10.4056/sigs.1483693;
RA   Muyzer G., Sorokin D.Y., Mavromatis K., Lapidus A., Clum A., Ivanova N.,
RA   Pati A., d'Haeseleer P., Woyke T., Kyrpides N.C.;
RT   "Complete genome sequence of 'Thioalkalivibrio sulfidophilus' HL-EbGr7.";
RL   Stand. Genomic Sci. 4:23-35(2011).
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; CP001339; ACL73803.1; -; Genomic_DNA.
DR   RefSeq; WP_012639278.1; NC_011901.1.
DR   AlphaFoldDB; B8GMY8; -.
DR   SMR; B8GMY8; -.
DR   STRING; 396588.Tgr7_2728; -.
DR   EnsemblBacteria; ACL73803; ACL73803; Tgr7_2728.
DR   KEGG; tgr:Tgr7_2728; -.
DR   eggNOG; COG0639; Bacteria.
DR   HOGENOM; CLU_056184_2_0_6; -.
DR   OMA; INAFTRM; -.
DR   OrthoDB; 900869at2; -.
DR   Proteomes; UP000002383; 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..270
FT                   /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT                   /id="PRO_1000124456"
SQ   SEQUENCE   270 AA;  30483 MW;  FBE480F4387C83EE CRC64;
     MSIYAVGDLQ GCLTPLKRLL EQVRFDPAAD QLWLVGDLVN RGPESLEALR FVRDLGDAAI
     TVLGNHDLHL LAIHQGVHKV RRKDTVQPIL DAPDRAELMD WLRHRPLLHH DPRIQWTLLH
     AGLPPQWDLA MARACASEVE TVLRGPDHPT LLERMYGDEP DQWSESLQGW ARLRFITNCF
     TRLRYCTADG SVDMAYKGAP GGQLPHLMPW FAVPGRRSVG TRIVFGHWST LGLYQGDDVL
     CLDTGCVWGQ RMTLARLDSS ALETMHTRCE