APAH_YERPB
ID APAH_YERPB Reviewed; 289 AA.
AC B2K485;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-JUN-2008, sequence version 1.
DT 03-AUG-2022, entry version 77.
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=YPTS_0654;
OS Yersinia pseudotuberculosis serotype IB (strain PB1/+).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=502801;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PB1/+;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Challacombe J.F., Green L., Lindler L.E., Nikolich M.P., Richardson P.;
RT "Complete sequence of Yersinia pseudotuberculosis PB1/+.";
RL Submitted (APR-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001048; ACC87638.1; -; Genomic_DNA.
DR RefSeq; WP_011191708.1; NZ_CP009780.1.
DR AlphaFoldDB; B2K485; -.
DR SMR; B2K485; -.
DR GeneID; 66842948; -.
DR KEGG; ypb:YPTS_0654; -.
DR PATRIC; fig|502801.10.peg.4339; -.
DR OMA; INAFTRM; -.
DR BioCyc; YPSE502801:YPTS_RS03415-MON; -.
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..289
FT /note="Bis(5'-nucleosyl)-tetraphosphatase, symmetrical"
FT /id="PRO_1000099342"
SQ SEQUENCE 289 AA; 32413 MW; 74C61EBA4A6A4B5A CRC64;
MSTYLIGDIH GCLDELLALL AQVNFDPQQD TLWLTGDLVA RGPASLDVLR YVRSLGPAVR
MVLGNHDLHL LAVYAGISRN KPKDRITPLL DAPDADELIN WLRRQPVLQV DDQLKLIMAH
AGITPQWDIE TAKMCAREVE AVLSSDSYPL FLDAMYGDMP NNWSPELTGL ARLRFSTNAL
TRMRFCFPNG QLDMICKDTP ENAPAPLKPW FDLPRLVDPE YSIIFGHWAS LEGKGVPEGI
YGLDTGCCWG GDLTLLRWED KRYFTQRAFK AEAEINNNNG FAAGEEVQH