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InterPro: IPR018017 Nucleoside phosphorylase, family 1

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UniProtKB

Matches:

3855 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
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Accession List
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Accession

IPR018017 Nucleoside_phosphorylase_1

Type

Region

Signatures Help

Database	ID	Name	Proteins
PANTHER	PTHR21234	PNP_UDP	3855
Signatures in BioMart

InterPro Relationships Help

Parent

IPR000845 Nucleoside phosphorylase

Children

IPR004402 Purine nucleoside phosphorylase
IPR010049 MTA/SAH nucleosidase
IPR010058 Uridine phosphorylase
IPR010059 Uridine phosphorylase, eukaryotic
IPR010944 AMP nucleosidase, putative
IPR019963 Futalosine nucleosidase

Found in

IPR011271 AMP nucleosidase

Contains

IPR018016 Nucleoside phosphorylase, conserved site

InterPro annotation

Entry Details in BioMart

Abstract

The following phosphorylases belong to the same family:

Purine nucleoside phosphorylase (EC:2.4.2.1) (PNP) from most bacteria (gene deoD), which catalyses the cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules [1].
Uridine phosphorylase (EC:2.4.2.3) (UdRPase) from bacteria (gene udp) and mammals, which catalyses the cleavage of uridine into uracil and ribose-1-phosphate, the products of the reaction are used either as carbon and energy sources or in the rescue of pyrimidine bases for nucleotide synthesis [2].
5'-methylthioadenosine phosphorylase (EC:2.4.2.28) (MTA phosphorylase) from Sulfolobus solfataricus [3].

It should be noted that mammalian and some bacterial PNP as well as eukaryotic MTA phosphorylase belong to a different family of phosphorylases.

Structural links Help

PDB - click here

SCOP: c.56.2.1

CATH: 3.40.50.1580

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018017

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P0A1F6 Uridine phosphorylase

P50389 S-methyl-5'-thioadenosine phosphorylase

P52624 Uridine phosphorylase 1

Q07469 Bark storage protein A

Q16831 Uridine phosphorylase 1

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR010059	Uridine phosphorylase, eukaryotic
IPR018017	Nucleoside phosphorylase, family 1
IPR018016	Nucleoside phosphorylase, conserved site
IPR000845	Nucleoside phosphorylase
IPR010058	Uridine phosphorylase
	SWISS-MODEL
	PDB Chain
	ModBase
	CATH Domain
	SCOP Domain

Publications Open in usermanual
1.	Takehara M, Ling F, Izawa S, Inoue Y, Kimura A. Molecular cloning and nucleotide sequence of purine nucleoside phosphorylase and uridine phosphorylase genes from Klebsiella sp. Biosci. Biotechnol. Biochem. 59 1987-90 1995 [PubMed: 8534998]
2.	Watanabe S, Hino A, Wada K, Eliason JF, Uchida T. Purification, cloning, and expression of murine uridine phosphorylase. J. Biol. Chem. 270 12191-6 1995 [PubMed: 7744869] http://dx.doi.org/10.1074/jbc.270.20.12191
3.	Cacciapuoti G, Porcelli M, Bertoldo C, De Rosa M, Zappia V. Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds. J. Biol. Chem. 269 24762-9 1994 [PubMed: 7929153] http://intl.jbc.org/cgi/reprint/269/40/24762.pdf

Additional Reading Open in usermanual
	Rinaldo-Matthis A, Wing C, Ghanem M, Deng H, Wu P, Gupta A, Tyler PC, Evans GB, Furneaux RH, Almo SC, Wang CC, Schramm VL. Inhibition and structure of Trichomonas vaginalis purine nucleoside phosphorylase with picomolar transition state analogues. Biochemistry 46 2007 659-68 [PubMed: 17223688] http://dx.doi.org/10.1021/bi061515r
	Dontsova MV, Gabdoulkhakov AG, Molchan OK, Lashkov AA, Garber MB, Mironov AS, Zhukhlistova NE, Morgunova EY, Voelter W, Betzel C, Zhang Y, Ealick SE, Mikhailov AM. Preliminary investigation of the three-dimensional structure of Salmonella typhimurium uridine phosphorylase in the crystalline state. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 61 2005 337-40 [PubMed: 16511035] http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=16511035
	Lee JE, Singh V, Evans GB, Tyler PC, Furneaux RH, Cornell KA, Riscoe MK, Schramm VL, Howell PL. Structural rationale for the affinity of pico- and femtomolar transition state analogues of Escherichia coli 5'-methylthioadenosine/S-adenosylhomocysteine nucleosidase. J. Biol. Chem. 280 2005 18274-82 [PubMed: 15746096] http://dx.doi.org/10.1074/jbc.M414471200
	Schnick C, Robien MA, Brzozowski AM, Dodson EJ, Murshudov GN, Anderson L, Luft JR, Mehlin C, Hol WG, Brannigan JA, Wilkinson AJ. Structures of Plasmodium falciparum purine nucleoside phosphorylase complexed with sulfate and its natural substrate inosine. Acta Crystallogr. D Biol. Crystallogr. 61 2005 1245-54 [PubMed: 16131758] http://dx.doi.org/10.1107/S0907444905020251
	Bu W, Settembre EC, el Kouni MH, Ealick SE. Structural basis for inhibition of Escherichia coli uridine phosphorylase by 5-substituted acyclouridines. Acta Crystallogr. D Biol. Crystallogr. 61 2005 863-72 [PubMed: 15983408] http://dx.doi.org/10.1107/S0907444905007882

InterPro 24.0