ADP-ribose pyrophosphatase (Q93K97)

Identification
Name:ADP-ribose pyrophosphatase
Synonyms:
  • ADP-ribose diphosphatase
  • ADP-ribose phosphohydrolase
  • ASPPase
  • Adenosine diphosphoribose pyrophosphatase
  • ADPR-PPase
Gene Name:nudF
Enzyme Class:
Biological Properties
General Function:Involved in hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
Specific Function:Acts on ADP-mannose and ADP-glucose as well as ADP- ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process
Cellular Location:Cytoplasmic
SMPDB Pathways:Not Available
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.0Adenosine diphosphate ribose + 1.0Water ↔ 1.0Adenosine monophosphate + 2.0Hydrogen ion + 1.0D-Ribose-5-phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Adenosine diphosphate ribose + 1.0Water ↔ 1.0Adenosine monophosphate + 1.0D-Ribose-5-phosphate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+2.0Thumb+1.0Thumb
1.0Adenosine diphosphate ribose + 1.0Water ↔ 1.0Adenosine monophosphate + 2.0Hydrogen ion + 1.0D-Ribose-5-phosphate
ReactionCard
Complex Reactions:
1.0Thumb+1.0Thumb → 1.0Thumb+1.0Thumb
1.0Adenosine diphosphate ribose + 1.0Water → 1.0Adenosine monophosphate + 1.0D-Ribose-5-phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01178Adenosine diphosphate riboseMetaboCard
ECMDB00045Adenosine monophosphateMetaboCard
ECMDB02033D-Ribose-5-phosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00494WaterMetaboCard
GO Classification:
Function
binding
catalytic activity
cation binding
hydrolase activity
hydrolase activity, acting on acid anhydrides
hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides
ion binding
metal ion binding
Gene Properties
Blattner:b3034
Gene OrientationCounterclockwise
Centisome Percentage:68.44
Left Sequence End3175303
Right Sequence End3175932
Gene Sequence:
>630 bp
ATGGTTAAGCCAGACAGCCTGCCCGTTACATTTGGCAAAAACGATGTAGAAATTATTGCA
CGAGAAACACTTTATCGCGGCTTTTTTTCATTAGATCTTTATAGATTTCGTCATCGTCTA
TTCAACGGGCAAATGAGTCATGAGGTACGGCGGGAAATTTTTGAGCGCGGTCACGCCGCA
GTCTTGCTACCCTTTGACCCAGTGCGTGATGAAGTTGTGCTGATTGAGCAGATTCGGATT
GCCGCGTACGACACCAGCGAAACCCCCTGGCTACTGGAGATGGTTGCCGGGATGATTGAA
GAGGGTGAAAGTGTGGAAGATGTTGCCCGTCGCGAAGCGATTGAAGAGGCGGGACTGATA
GTCAAACGGACCAAACCGGTGTTAAGTTTCCTGGCAAGCCCGGGGGGCACCAGTGAGCGT
TCGTCAATTATGGTGGGCGAAGTGGACGCCACGACCGCAAGCGGTATTCATGGTCTGGCT
GATGAAAACGAAGATATTCGCGTTCATGTGGTAAGCCGGGAACAGGCATACCAGTGGGTA
GAAGAGGGGAAAATCGACAACGCAGCGTCGGTCATCGCTTTGCAATGGCTGCAGCTGCAT
CATCAAGCGTTAAAAAATGAGTGGGCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:209
Protein Molecular Weight:23667
Protein Theoretical pI:5
PDB File:1G0S
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>ADP-ribose pyrophosphatase
MLKPDNLPVTFGKNDVEIIARETLYRGFFSLDLYRFRHRLFNGQMSHEVRREIFERGHAA
VLLPFDPVRDEVVLIEQIRIAAYDTSETPWLLEMVAGMIEEGESVEDVARREAIEEAGLI
VKRTKPVLSFLASPGGTSERSSIMVGEVDATTASGIHGLADENEDIRVHVVSREQAYQWV
EEGKIDNAASVIALQWLQLHHQALKNEWA
References
External Links:
ResourceLink
Uniprot ID:Q93K97
Uniprot Name:ADPP_ECOLI
GenBank Gene ID:AJ298136
Genebank Protein ID:14627087
PDB ID:1G0S
Ecogene ID:EG12184
Ecocyc:EG12184
ColiBase:b3034
Kegg Gene:b3034
EchoBASE ID:EB2101
CCDB:ADPP_ECOLI
BacMap:16130930
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Dunn, C. A., O'Handley, S. F., Frick, D. N., Bessman, M. J. (1999). "Studies on the ADP-ribose pyrophosphatase subfamily of the nudix hydrolases and tentative identification of trgB, a gene associated with tellurite resistance." J Biol Chem 274:32318-32324. Pubmed: 10542272
  • Gabelli, S. B., Bianchet, M. A., Bessman, M. J., Amzel, L. M. (2001). "The structure of ADP-ribose pyrophosphatase reveals the structural basis for the versatility of the Nudix family." Nat Struct Biol 8:467-472. Pubmed: 11323725
  • Gabelli, S. B., Bianchet, M. A., Ohnishi, Y., Ichikawa, Y., Bessman, M. J., Amzel, L. M. (2002). "Mechanism of the Escherichia coli ADP-ribose pyrophosphatase, a Nudix hydrolase." Biochemistry 41:9279-9285. Pubmed: 12135348
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Imamura, R., Yamanaka, K., Ogura, T., Hiraga, S., Fujita, N., Ishihama, A., Niki, H. (1996). "Identification of the cpdA gene encoding cyclic 3',5'-adenosine monophosphate phosphodiesterase in Escherichia coli." J Biol Chem 271:25423-25429. Pubmed: 8810311
  • Moreno-Bruna, B., Baroja-Fernandez, E., Munoz, F. J., Bastarrica-Berasategui, A., Zandueta-Criado, A., Rodriguez-Lopez, M., Lasa, I., Akazawa, T., Pozueta-Romero, J. (2001). "Adenosine diphosphate sugar pyrophosphatase prevents glycogen biosynthesis in Escherichia coli." Proc Natl Acad Sci U S A 98:8128-8132. Pubmed: 11416161