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	PROSITE documentation PDOC00627

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.

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 in UniProtKB/Swiss-Prot known to belong to this class: 29
  • detected by PS00785: 27 (true positives)
  • undetected by PS00785: 2 (2 false negatives and 0 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00785:
  2 false positives.
• Retrieve an alignment of UniProtKB/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 distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00785
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00785
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00785
• View ligand binding statistics of PS00785
• 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 in UniProtKB/Swiss-Prot known to belong to this class: 28
  • detected by PS00786: 26 (true positives)
  • undetected by PS00786: 2 (1 false negative and 1 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS00786:
  NONE.
• Retrieve an alignment of UniProtKB/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 distribution of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00786
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS00786
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS00786
• View ligand binding statistics of PS00786
• 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

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