Home ScanProsite ProRule Documents Downloads Links Funding
	PROSITE documentation PDOC00954

Purine and other phosphorylases family 2 signature

The following phosphorylases belongs to the same family:

• Purine nucleoside phosphorylase (EC 2.4.2.1) (PNP) from mammals as well as from some bacteria (gene deoD). This enzyme catalyzes the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [1].
• 5'-methylthioadenosine phosphorylase (EC 2.4.2.28) (MTA phosphorylase) from eukaryotes [2].
• Xanthosine phosphorylase (EC 2.4.2.-) from Escherichia coli (gene xapA). This enzyme can degrade all purine nucleosides except adenosine and deoxyadenosine [3].

This family also includes the following uncharacterized proteins:

• Yeast hypothetical protein YLR017w.
• Fission yeast hypothetical protein SpAC16C9.02c.
• Methanococcus jannaschii hypothetical protein MJ0060.
• Rhodospirillum rubrum hypothetical protein in petC 3'region.

As a signature pattern, we selected a conserved region in the central part of these enzymes.

Note:

It should be noted that most bacterial PNP as well as archaebacterial MTA phosphorylase belong to a different family of phosphorylases (see <PDOC00946>).

Last update:

December 2004 / Pattern and text revised.

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

PNP_MTAP_2, PS01240; Purine and other phosphorylases family 2 signature  (PATTERN)

• Consensus pattern:
  [LIVF]-x(3)-[GS]-x(2)-H-x-[LIVMFY]-x(4)-[LIVMF]-x(3)-[ATV]-x(1,2)-[LIVM]-x-[ATV]-x(4)-[GN]-x(3,4)-[LIVMF](2)-x(2)-[STN]-[SAGT]-x-G-[GS]-[LIVM]
• Sequences in UniProtKB/Swiss-Prot known to belong to this class: 95
  • detected by PS01240: 72 (true positives)
  • undetected by PS01240: 23 (23 false negatives and 0 'partial')
• Other sequence(s) in UniProtKB/Swiss-Prot detected by PS01240:
  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 PS01240
• Retrieve a list of all UniProtKB (Swiss-Prot + TrEMBL) entries matching PS01240
• Scan UniProtKB (Swiss-Prot and/or TrEMBL) entries against PS01240
• View ligand binding statistics of PS01240
• Matching PDB structures: 1A9O 1A9P 1A9Q 1A9R ... [ALL]

1	Authors	Ealick S.E., Rule S.A., Carter D.C., Greenhough T.J., Babu Y.S., Cook W.J., Habash J., Helliwell J.R., Stoeckler J.D., Parks R.E. Jr. Chen S.-F., Bugg C.E.
	Title	Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.
	Source	J. Biol. Chem. 265:1812-1820(1990).
	PubMed ID	2104852

2	Authors	Della Ragione F., Takabayashi K., Mastropietro S., Mercurio C., Oliva A., Russo G.L., Della Pietra V., Borriello A., Nobori T., Carson D.A., Zappia V.
	Title	Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA.
	Source	Biochem. Biophys. Res. Commun. 223:514-519(1996).
	PubMed ID	8687427

3	Authors	Seeger C., Poulsen C., Dandanell G.
	Title	Identification and characterization of genes (xapA, xapB, and xapR) involved in xanthosine catabolism in Escherichia coli.
	Source	J. Bacteriol. 177:5506-5516(1995).
	PubMed ID	7559336

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)