To improve security and privacy, we are moving our web pages and services from HTTP to HTTPS.
To give users of web services time to transition to HTTPS, we will support separate HTTP and HTTPS services until the end of 2017.
From January 2018 most HTTP traffic will be automatically redirected to HTTPS. [more...]
View this page in https
PROSITE documentation PDOC00627

5'-nucleotidase signatures





Description

5'-nucleotidases (EC 3.1.3.5) [1] are enzymes that catalyze the hydrolysis of phosphate esterified at carbon 5' of the ribose and deoxyribose portions of nucleotide molecules. 5'-nucleotidase is a ubiquitous enzyme found in a wide variety of species and which occurs in different cellular locations. The sequences of the following 5'-nucleotidases are currently known:

  • Extracellular 5'-nucleotidase from mammals and electric ray. This isozyme is a homodimeric disulfide-bonded glycoprotein attached to the membrane by a GPI-anchor. It requires zinc for its activity
  • Vibrio parahaemolyticus 5'-nucleotidase (gene nutA). This isozyme is bound to the membrane by a lipid chain. NutA requires chloride and magnesium ions for its activity. It is involved in degrading extracellular 5'-nucleotides for nutritional needs.
  • Periplasmic bacterial 5'-nucleotidase (gene ushA). This enzyme, also known as UDP-sugar hydrolase (EC 3.6.1.45), can degrade UDP-glucose and other nucleotide diphosphate sugars. It produces sugar-1-phosphate which can then be used by the cell. UshA seems to require cobalt for its activity.

5'-nucleotidases are evolutionary related to the following enzyme:

  • Periplasmic bacterial 2',3'-cyclic-nucleotide 2'-phosphodiesterase (EC 3.1. 4.16) (gene cpdB). This bifunctional enzyme catalyzes two consecutive reactions: it first converts 2',3'-cyclic-nucleotide to 3'-nucleotide and then acts as a 3'-nucleotidase.
  • Mosquito apyrase (EC 3.6.1.5) (ATP-diphosphohydrolase) [2]. This enzyme catalyzes the hydrolysis of ATP into AMP and facilitates hematophagy by preventing ADP-dependent platelet aggregation in the host.

All these proteins share a number of regions of sequence similarity, of which we selected two as signature patterns. Both regions are located in the N-terminal section of these enzymes. The second pattern contains a perfectly conserved pentapeptide.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

5_NUCLEOTIDASE_1, PS00785; 5'-nucleotidase signature 1  (PATTERN)

5_NUCLEOTIDASE_2, PS00786; 5'-nucleotidase signature 2  (PATTERN)


References

1AuthorsZimmermann H.
Title5'-Nucleotidase: molecular structure and functional aspects.
SourceBiochem. J. 285:345-365(1992).
PubMed ID1637327

2AuthorsChampagne D.E., Smartt C.T., Ribeiro J.M.C., James A.A.
TitleThe salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5'-nucleotidase family.
SourceProc. Natl. Acad. Sci. U.S.A. 92:694-698(1995).
PubMed ID7846038



PROSITE is copyright. It is produced by the SIB Swiss Institute Bioinformatics. There are no restrictions on its use by non-profit institutions as long as its content is in no way modified. Usage by and for commercial entities requires a license agreement. For information about the licensing scheme send an email to
Prosite License or see: prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)