(data stored in ACNUC7421 zone)

SWISSPROT: APAH_ECODH

ID   APAH_ECODH              Reviewed;         280 AA.
AC   B1XC50;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 1.
DT   05-JUL-2017, entry version 59.
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=ECDH10B_0050;
OS   Escherichia coli (strain K12 / DH10B).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=316385;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / DH10B;
RX   PubMed=18245285; DOI=10.1128/JB.01695-07;
RA   Durfee T., Nelson R., Baldwin S., Plunkett G. III, Burland V., Mau B.,
RA   Petrosino J.F., Qin X., Muzny D.M., Ayele M., Gibbs R.A., Csorgo B.,
RA   Posfai G., Weinstock G.M., Blattner F.R.;
RT   "The complete genome sequence of Escherichia coli DH10B: insights into
RT   the biology of a laboratory workhorse.";
RL   J. Bacteriol. 190:2597-2606(2008).
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to
CC       yield ADP. {ECO:0000255|HAMAP-Rule:MF_00199}.
CC   -!- CATALYTIC ACTIVITY: P(1),P(4)-bis(5'-adenosyl) tetraphosphate +
CC       H(2)O = 2 ADP. {ECO:0000255|HAMAP-Rule:MF_00199}.
CC   -!- SIMILARITY: Belongs to the Ap4A hydrolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00199}.
DR   EMBL; CP000948; ACB01254.1; -; Genomic_DNA.
DR   RefSeq; WP_000257192.1; NC_010473.1.
DR   ProteinModelPortal; B1XC50; -.
DR   SMR; B1XC50; -.
DR   EnsemblBacteria; ACB01254; ACB01254; ECDH10B_0050.
DR   KEGG; ecd:ECDH10B_0050; -.
DR   eggNOG; ENOG4105DDT; Bacteria.
DR   eggNOG; COG0639; LUCA.
DR   HOGENOM; HOG000251871; -.
DR   KO; K01525; -.
DR   OMA; MPWFDVP; -.
DR   GO; GO:0008803; F:bis(5'-nucleosyl)-tetraphosphatase (symmetrical) activity; IEA:UniProtKB-EC.
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   PANTHER; PTHR24032:SF49; PTHR24032:SF49; 1.
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;
DR   PRODOM; B1XC50.
DR   SWISS-2DPAGE; B1XC50.
KW   Hydrolase.
FT   CHAIN         1    280       Bis(5'-nucleosyl)-tetraphosphatase,
FT                                symmetrical.
FT                                /FTId=PRO_1000099323.
SQ   SEQUENCE   280 AA;  31297 MW;  BD6560C73446C1BB CRC64;
     MATYLIGDVH GCYDELIALL HKVEFTPGKD TLWLTGDLVA RGPGSLDVLR YVKSLGDSVR
     LVLGNHDLHL LAVFAGISRN KPKDRLTPLL EAPDADELLN WLRRQPLLQI DEEKKLVMAH
     AGITPQWDLQ TAKECARDVE AVLSSDSYPF FLDAMYGDMP NNWSPELRGL GRLRFITNAF
     TRMRFCFPNG QLDMYSKESP EEAPAPLKPW FAIPGPVAEE YSIAFGHWAS LEGKGTPEGI
     YALDTGCCWG GTLTCLRWED KQYFVQPSNR HKDLGEAAAS
//

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