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InterPro: IPR000845 Nucleoside phosphorylase

Protein matchesHelp
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UniProtKB
Matches:
5954 proteins
AccessionHelp
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IPR000845 Nucleoside_phosphorylase
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Domain
SignaturesHelp
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InterPro RelationshipsHelp
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Children IPR001369 Purine phosphorylase, family 2
IPR017831 Hopanoid-associated phosphorylase HpnG
IPR018017 Nucleoside phosphorylase, family 1
Found in IPR010050 5-methylthioadenosine/S-adenosylhomocysteine nucleosidase, putative
IPR011271 AMP nucleosidase
Contains IPR018016 Nucleoside phosphorylase, conserved site
IPR018099 Purine phosphorylase, family 2, conserved site
GO Term annotationHelp
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Process GO:0009116 nucleoside metabolic process
Function GO:0003824 catalytic activity
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp
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Phosphorylases in this entry include:

  • 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].
  • 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 [4].
  • 5'-methylthioadenosine phosphorylase (EC:2.4.2.28) (MTA phosphorylase) from eukaryotes [5].
Structural linksHelp
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PDB - click here
1a69 , 1a9o , 1a9p , 1a9q , 1a9r , 1a9s , 1a9t , 1b8n , 1b8o , 1c3x , 1cb0 , 1cg6 , 1ecp , 1fxu , 1g2o , 1i80 , 1jds , 1jdt , 1jdu , 1jdv , 1jdz , 1je0 , 1je1 , 1jp7 , 1jpv , 1jys , 1k27 , 1k3f , 1k9s , 1lv8 , 1lvu , 1lx7 , 1m73 , 1n3i , 1nc1 , 1nc3 , 1nw4 , 1odi , 1odj , 1odk , 1odl , 1otx , 1oty , 1ou4 , 1oum , 1ov6 , 1ovg , 1pbn , 1pf7 , 1pk7 , 1pk9 , 1pke , 1pr0 , 1pr1 , 1pr2 , 1pr4 , 1pr5 , 1pr6 , 1pw7 , 1pwy , 1q1g , 1qe5 , 1rct , 1rfg , 1rr6 , 1rsz , 1rt9 , 1rxc , 1rxs , 1rxu , 1rxy , 1ryz , 1sd1 , 1sd2 , 1sj9 , 1sq6 , 1t0u , 1t8r , 1t8s , 1t8w , 1t8y , 1tcu , 1tcv , 1td1 , 1tgv , 1tgy , 1u1c , 1u1d , 1u1e , 1u1f , 1u1g , 1ula , 1ulb , 1v2h , 1v3q , 1v41 , 1v45 , 1v48 , 1v4n , 1vfn , 1vhj , 1vhw , 1vmk , 1wta , 1xe3 , 1y1q , 1y1r , 1y1s , 1y1t , 1y6q , 1y6r , 1ybf , 1yqq , 1yqu , 1yr3 , 1yry , 1z5n , 1z5o , 1z5p , 1zl2 , 1zos , 2a0w , 2a0x , 2a0y , 2a8y , 2ac7 , 2ai1 , 2ai2 , 2ai3 , 2b94 , 2bsx , 2guw , 2hn9 , 2hrd , 2hsw , 2hwu , 2i4t , 2i8a , 2iq5 , 2isc , 2oc4 , 2oc9 , 2oec , 2on6 , 2oxf , 2p4s , 2pga , 2q7o , 2qpl , 3bgs , 3pnp , 4pnp
SCOP: c.56.2.1
CATH: 3.40.50.1580
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PDBe-motif: PS01232
PROSITE doc: PDOC00946
PANDIT: PF01048
Blocks: IPB000845

Taxonomic coverageHelp
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Overlapping InterPro entriesHelp
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IPR000845 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
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P00491 Purine nucleoside phosphorylase

P23492 Purine nucleoside phosphorylase

Q05788 Purine nucleoside phosphorylase

Q09438 Putative S-methyl-5'-thioadenosine phosphorylase

Q9V813 Putative S-methyl-5'-thioadenosine phosphorylase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001369 Purine phosphorylase, family 2
IPR000845 Nucleoside phosphorylase
IPR018099 Purine phosphorylase, family 2, conserved site
IPR010044 Methylthioadenosine phosphorylase
IPR011270 Purine nucleoside phosphorylase I, inosine/guanosine-specific
IPR011268 Inosine guanosine/xanthosine phosphorylase
SWISS-MODEL
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
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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
4. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE Jr.
Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.
J. Biol. Chem. 265 1812-20 1990 [PubMed: 2104852]
http://intl.jbc.org/cgi/content/abstract/265/3/1812
5. Della Ragione F, Takabayashi K, Mastropietro S, Mercurio C, Oliva A, Russo GL, Della Pietra V, Borriello A, Nobori T, Carson DA, Zappia V.
Purification and characterization of recombinant human 5'-methylthioadenosine phosphorylase: definite identification of coding cDNA.
Biochem. Biophys. Res. Commun. 223 514-9 1996 [PubMed: 8687427]
http://dx.doi.org/10.1006/bbrc.1996.0926

Additional ReadingHelp
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Rinaldo-Matthis A, Murkin AS, Ramagopal UA, Clinch K, Mee SP, Evans GB, Tyler PC, Furneaux RH, Almo SC, Schramm VL.
L-Enantiomers of transition state analogue inhibitors bound to human purine nucleoside phosphorylase.
J. Am. Chem. Soc. 130 2008 842-4 [PubMed: 18154341]
http://dx.doi.org/10.1021/ja710733g
Taylor EA, Rinaldo-Matthis A, Li L, Ghanem M, Hazleton KZ, Cassera MB, Almo SC, Schramm VL.
Anopheles gambiae purine nucleoside phosphorylase: catalysis, structure, and inhibition.
Biochemistry 46 2007 12405-15 [PubMed: 17918964]
http://dx.doi.org/10.1021/bi7010256
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
Pereira HM, Berdini V, Cleasby A, Garratt RC.
Crystal structure of calf spleen purine nucleoside phosphorylase complexed to a novel purine analogue.
FEBS Lett. 581 2007 5082-6 [PubMed: 17927987]
http://dx.doi.org/10.1016/j.febslet.2007.09.051
Mao C, Cook WJ, Zhou M, Koszalka GW, Krenitsky TA, Ealick SE.
The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology.
Structure 5 1997 1373-83 [PubMed: 9351810]
http://dx.doi.org/10.1016/S0969-2126(97)00287-6
Murkin AS, Birck MR, Rinaldo-Matthis A, Shi W, Taylor EA, Almo SC, Schramm VL.
Neighboring group participation in the transition state of human purine nucleoside phosphorylase.
Biochemistry 46 2007 5038-49 [PubMed: 17407325]
http://dx.doi.org/10.1021/bi700147b
Mushegian AR, Koonin EV.
Unexpected sequence similarity between nucleosidases and phosphoribosyltransferases of different specificity.
Protein Sci. 3 1994 1081-8 [PubMed: 7920254]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=7920254&action=stream&blobtype=pdf
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