(data stored in ACNUC7421 zone)

SWISSPROT: APAH_EDWI9

ID   APAH_EDWI9              Reviewed;         279 AA.
AC   C5B7N9;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 63.
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=NT01EI_0694;
OS   Edwardsiella ictaluri (strain 93-146).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Edwardsiella.
OX   NCBI_TaxID=634503;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=93-146;
RA   Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C.,
RA   Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.;
RT   "Complete genome sequence of Edwardsiella ictaluri 93-146.";
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Hydrolyzes diadenosine 5',5'''-P1,P4-tetraphosphate to
CC       yield ADP. {ECO:0000255|HAMAP-Rule:MF_00199}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + P(1),P(4)-bis(5'-adenosyl) tetraphosphate = 2 ADP +
CC         2 H(+); Xref=Rhea:RHEA:24252, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:58141, ChEBI:CHEBI:456216;
CC         EC=3.6.1.41; Evidence={ECO:0000255|HAMAP-Rule:MF_00199};
CC   -!- SIMILARITY: Belongs to the Ap4A hydrolase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00199}.
DR   EMBL; CP001600; ACR67916.1; -; Genomic_DNA.
DR   RefSeq; WP_015870109.1; NC_012779.2.
DR   SMR; C5B7N9; -.
DR   EnsemblBacteria; ACR67916; ACR67916; NT01EI_0694.
DR   GeneID; 7962028; -.
DR   KEGG; eic:NT01EI_0694; -.
DR   PATRIC; fig|634503.3.peg.625; -.
DR   eggNOG; ENOG4105DDT; Bacteria.
DR   eggNOG; COG0639; LUCA.
DR   HOGENOM; HOG000251871; -.
DR   KO; K01525; -.
DR   OMA; MPWFDVP; -.
DR   OrthoDB; 900869at2; -.
DR   BioCyc; EICT634503:G1GVC-644-MONOMER; -.
DR   Proteomes; UP000001485; 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   TIGRFAMs; TIGR00668; apaH; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5B7N9.
DR   SWISS-2DPAGE; C5B7N9.
KW   Complete proteome; Hydrolase; Reference proteome.
FT   CHAIN         1    279       Bis(5'-nucleosyl)-tetraphosphatase,
FT                                symmetrical.
FT                                /FTId=PRO_1000204085.
SQ   SEQUENCE   279 AA;  31043 MW;  4D3D938A44498653 CRC64;
     MSTLLIGDVH GCYHELRDLL SLADFDPARD TLWLTGDLVA RGPDSLAVLR YVKSLGDSAR
     LVLGNHDLHL LAIYAGISRN KPKDKLTPLL EAPDADSLIN WLRRQPVLQV DNDLCLVMAH
     AGISPQWDLT TAQRCAREVE AMLASDSYPF FLNAMYGDMP NNWSESLSGL ARLRFTTNAL
     TRMRYCFPGG ELDMICKDAP EDAPAPLRPW FDLDSPVREA GYSIAFGHWA SLEGRSTPPQ
     VYALDTGCCW GGTLTALRWE DRHSFSVPSR RASRHAKAE
//

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