Identification
Name:Purine nucleoside phosphorylase deoD-type
Synonyms:
  • PNP
  • Inosine phosphorylase
Gene Name:deoD
Enzyme Class:
Biological Properties
General Function:Involved in purine-nucleoside phosphorylase activity
Specific Function:Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+alpha-D-Ribose 1-phosphate
Adenosine + PhosphateAdenine + alpha-D-Ribose 1-phosphate
ReactionCard
Thumb+ThumbThumb+alpha-D-Ribose 1-phosphate
Inosine + PhosphateHypoxanthine + alpha-D-Ribose 1-phosphate
ReactionCard
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+alpha-D-Ribose 1-phosphate
Guanosine + PhosphateGuanine + alpha-D-Ribose 1-phosphate
ReactionCard
Thumb+ThumbThumb+alpha-D-Ribose 1-phosphate
Nicotinamide riboside + PhosphateNiacinamide + alpha-D-Ribose 1-phosphate
ReactionCard
Thumb+ThumbThumb+alpha-D-Ribose 1-phosphate
Xanthosine + PhosphateXanthine + alpha-D-Ribose 1-phosphate
ReactionCard
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
N-D-Ribosylpurine+ThumbPurine+alpha-D-Ribose 1-phosphate
N-D-Ribosylpurine + Phosphate ↔ Purine + alpha-D-Ribose 1-phosphate
ReactionCard
Thumb+Thumb+ThumbThumb+Thumb+Thumb
SMPDB Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
EcoCyc Reactions:
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Thumb+ThumbThumb+Thumb
Complex Reactions:
Thumb+ThumbThumb+Thumb
Metabolites:
ECMDB IDNameView
ECMDB00034AdenineMetaboCard
ECMDB00050AdenosineMetaboCard
ECMDB00101DeoxyadenosineMetaboCard
ECMDB00085DeoxyguanosineMetaboCard
ECMDB00071DeoxyinosineMetaboCard
ECMDB01351Deoxyribose 1-phosphateMetaboCard
ECMDB00012DeoxyuridineMetaboCard
ECMDB00132GuanineMetaboCard
ECMDB00133GuanosineMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00157HypoxanthineMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00195InosineMetaboCard
ECMDB01406NiacinamideMetaboCard
ECMDB00855Nicotinamide ribosideMetaboCard
ECMDB01488Nicotinic acidMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB01366PurineMetaboCard
ECMDB23826Purine deoxyribonucleosideMetaboCard
ECMDB23238Purine nucleosideMetaboCard
ECMDB04147Ribose-1-phosphateMetaboCard
ECMDB00300UracilMetaboCard
ECMDB00292XanthineMetaboCard
ECMDB00299XanthosineMetaboCard
GO Classification:
Function
catalytic activity
purine-nucleoside phosphorylase activity
transferase activity
transferase activity, transferring glycosyl groups
transferase activity, transferring pentosyl groups
Process
cellular nitrogen compound metabolic process
metabolic process
nitrogen compound metabolic process
nucleobase, nucleoside and nucleotide metabolic process
nucleobase, nucleoside, nucleotide and nucleic acid metabolic process
nucleoside metabolic process
Gene Properties
Blattner:b4384
Gene OrientationClockwise
Centisome Percentage:99.55
Left Sequence End4618906
Right Sequence End4619625
Gene Sequence:
>720 bp
GTGAATGTCAATTTCTTTGTCACCTGTATTGGTGACGCCCTGAAATCAAGAATGGCACGA
GACTCCGTGCTGCTACTGGAAAAACTCGGCTGTCGCGTAAATTTCCCGGAGAAACAGGGA
TGCTGCGGTCAGCCTGCGATCAATAGCGGTTATATCAAAGAAGCGATTCCAGGGATGAAA
AATCTGATCGCCGCACTGGAGGATAACGACGATCCCATTATTTCACCGGCTGGCTCTTGC
ACCTATGCCGTAAAAAGTTACCCGACGTATCTGGCGGATGAACCTGAATGGGCATCACGT
GCCGCAAAGGTTGCCGCGCGTATGCAGGATCTCACCTCTTTTATTGTTAATAAATTAGGG
GTAGTCGATGTAGGTGCCAGTTTGCAAGGGAGAGCGGTGTATCACCCATCTTGTAGCCTG
GCCCGTAAGCTGGGAGTGAAGGACGAGCCACTTACGCTGCTGAAAAATGTGCGTGGACTG
GAGCTGTTGACCTTTGCTGAACAGGATACCTGCTGCGGATTTGGCGGCACGTTCTCGGTC
AAAATGGCCGAAATATCCGGCGAGATGGTGAAAGAAAAGGTTGCGCACCTGATGGAAGTC
CGCCCTGAGTATTTAATTGGTGCTGACGTGAGTTGCCTGCTAAACATCAGTGGGCGATTA
CAACGGGAAGGGCAGAAAGTCAAAGTGATGCATATTGCTGAAGTGTTGATGAGCCGCTGA
Protein Properties
Pfam Domain Function:
Protein Residues:239
Protein Molecular Weight:25950
Protein Theoretical pI:5
PDB File:1PW7
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Purine nucleoside phosphorylase deoD-type
MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISV
MGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIR
FKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVE
MEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE
References
External Links:
ResourceLink
Uniprot ID:P0ABP8
Uniprot Name:DEOD_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674450
PDB ID:1PW7
Ecogene ID:EG10222
Ecocyc:EG10222
ColiBase:b4384
Kegg Gene:b4384
EchoBASE ID:EB0218
CCDB:DEOD_ECOLI
BacMap:16132201
General Reference:
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Henzel, W. J., Billeci, T. M., Stults, J. T., Wong, S. C., Grimley, C., Watanabe, C. (1993). "Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases." Proc Natl Acad Sci U S A 90:5011-5015. Pubmed: 8506346
  • Hershfield, M. S., Chaffee, S., Koro-Johnson, L., Mary, A., Smith, A. A., Short, S. A. (1991). "Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol." Proc Natl Acad Sci U S A 88:7185-7189. Pubmed: 1714590
  • Koellner, G., Luic, M., Shugar, D., Saenger, W., Bzowska, A. (1998). "Crystal structure of the ternary complex of E. coli purine nucleoside phosphorylase with formycin B, a structural analogue of the substrate inosine, and phosphate (Sulphate) at 2.1 A resolution." J Mol Biol 280:153-166. Pubmed: 9653038
  • Larsen, J. E., Albrechtsen, B., Valentin-Hansen, P. (1987). "Analysis of the terminator region after the deoCABD operon of Escherichia coli K-12 using a new class of single copy number operon-fusion vectors." Nucleic Acids Res 15:5125-5140. Pubmed: 3299264
  • Mao, C., Cook, W. J., Zhou, M., Koszalka, G. W., Krenitsky, T. A., Ealick, S. E. (1997). "The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology." Structure 5:1373-1383. Pubmed: 9351810
  • Zhang, J., Sprung, R., Pei, J., Tan, X., Kim, S., Zhu, H., Liu, C. F., Grishin, N. V., Zhao, Y. (2009). "Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Mol Cell Proteomics 8:215-225. Pubmed: 18723842