Home | Contact

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.

December 2004 / Pattern and text revised.

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

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

Consensus pattern: [LIVM]-x-[LIVM](2)-[HEA]-[TI]-x-D-x-H-[GSA]-x-[LIVMF] Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00785 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00785 • Scan Swiss-Prot/TrEMBL entries against PS00785 • view ligand binding statistics

Matching PDB structures: 1HO5 1HP1 1HPU 1OI8 ... [ALL]

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

Consensus pattern: [FYPH]-x(4)-[LIVM]-G-N-H-E-F-[DN] Sequences known to belong to this class detected by the pattern: ALL Other sequence(s) detected in Swiss-Prot: NONE.

• Retrieve an alignment of Swiss-Prot true positive hits:   Clustal format, color, condensed view  / Clustal format, color  / Clustal format, plain text  / Fasta format • Retrieve the sequence logo from the alignment • Taxonomic tree view of all Swiss-Prot/TrEMBL entries matching PS00786 • Retrieve a list of all Swiss-Prot/TrEMBL entries matching PS00786 • Scan Swiss-Prot/TrEMBL entries against PS00786 • view ligand binding statistics

Matching PDB structures: 1HO5 1HP1 1HPU 1OI8 ... [ALL]

1	Authors	Zimmermann H.
	Title	5'-Nucleotidase: molecular structure and functional aspects.
	Source	Biochem. J. 285:345-365(1992).
	PubMed ID	1637327

2	Authors	Champagne D.E., Smartt C.T., Ribeiro J.M.C., James A.A.
	Title	The salivary gland-specific apyrase of the mosquito Aedes aegypti is a member of the 5'-nucleotidase family.
	Source	Proc. Natl. Acad. Sci. U.S.A. 92:694-698(1995).
	PubMed ID	7846038

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.


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

SIB Swiss Institute of Bioinformatics | Disclaimer