ECMDB

Identification

Name:

Purine nucleoside phosphorylase deoD-type

Synonyms:

PNP
Inosine phosphorylase

Gene Name:

deoD

Enzyme Class:

2.4.2.1

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:

Pyrimidine metabolism PW000942
adenine and adenosine salvage I PW002069
adenine and adenosine salvage II PW002071
adenosine nucleotides degradation PW002091
guanine and guanosine salvage PW002074
purine deoxyribonucleosides degradation PW002077
purine ribonucleosides degradation PW002076

KEGG Pathways:

Metabolic pathways eco01100
Nicotinate and nicotinamide metabolism ec00760
Purine metabolism ec00230
Pyrimidine metabolism ec00240

KEGG Reactions:

1.0

↔

1.0

1.0Deoxyinosine + 1.0Phosphate ↔ 1.0Deoxyribose 1-phosphate + 1.0Hypoxanthine
ReactionCard

1.0

↔

1.0

1.0Deoxyguanosine + 1.0Phosphate ↔ 1.0Deoxyribose 1-phosphate + 1.0Guanine
ReactionCard

1.0

↔

1.0

1.0Deoxyuridine + 1.0Phosphate ↔ 1.0Deoxyribose 1-phosphate + 1.0Uracil
ReactionCard

1.0

↔

1.0

1.0Deoxyadenosine + 1.0Phosphate ↔ 1.0Deoxyribose 1-phosphate + 1.0Adenine
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1.0

↔

1.0

1.0alpha-D-Ribose 1-phosphate

1.0Adenosine + 1.0Phosphate ↔ 1.0Adenine + 1.0alpha-D-Ribose 1-phosphate
ReactionCard

1.0

↔

1.0

1.0alpha-D-Ribose 1-phosphate

1.0Inosine + 1.0Phosphate ↔ 1.0Hypoxanthine + 1.0alpha-D-Ribose 1-phosphate
ReactionCard

1.0

↔

1.0

1.0alpha-D-Ribose 1-phosphate

1.0Guanosine + 1.0Phosphate ↔ 1.0Guanine + 1.0alpha-D-Ribose 1-phosphate
ReactionCard

1.0

↔

1.0

1.0alpha-D-Ribose 1-phosphate

1.0Nicotinamide riboside + 1.0Phosphate ↔ 1.0Niacinamide + 1.0alpha-D-Ribose 1-phosphate
ReactionCard

1.0

↔

1.0

1.0alpha-D-Ribose 1-phosphate

1.0Xanthosine + 1.0Phosphate ↔ 1.0Xanthine + 1.0alpha-D-Ribose 1-phosphate
ReactionCard

1.0N-D-Ribosylpurine

1.0

↔

1.0Purine

1.0alpha-D-Ribose 1-phosphate

1.0N-D-Ribosylpurine + 1.0Phosphate ↔ 1.0Purine + 1.0alpha-D-Ribose 1-phosphate
ReactionCard

1.0

↔

1.0

1.0Purine nucleoside + 1.0Phosphate + 1.0Purine deoxyribonucleoside ↔ 1.0Purine + 1.0Ribose-1-phosphate + 1.0Deoxyribose 1-phosphate
ReactionCard

SMPDB Reactions:

1.0

→

1.0

1.0Adenine + 1.0Ribose-1-phosphate → 1.0Phosphate + 1.0Adenosine
ReactionCard

1.0

→

1.0

1.0Inosine + 1.0Phosphate → 1.0Ribose-1-phosphate + 1.0Hypoxanthine
ReactionCard

1.0

→

1.0

1.0Guanosine + 1.0Phosphate → 1.0Ribose-1-phosphate + 1.0Guanine
ReactionCard

1.0

→

1.0

1.0Adenosine + 1.0Phosphate → 1.0Adenine + 1.0Ribose-1-phosphate
ReactionCard

1.0

→

1.0

1.0Deoxyadenosine + 1.0Phosphate → 1.0Adenine + 1.0Deoxyribose 1-phosphate
ReactionCard

EcoCyc Reactions:

1.0

↔

1.0

1.0Guanosine + 1.0Phosphate ↔ 1.0Guanine + 1.0Ribose-1-phosphate
ReactionCard

1.0

↔

1.0

1.0Inosine + 1.0Phosphate ↔ 1.0Hypoxanthine + 1.0Ribose-1-phosphate
ReactionCard

1.0

↔

1.0

1.0Adenosine + 1.0Phosphate ↔ 1.0Adenine + 1.0Ribose-1-phosphate
ReactionCard

Complex Reactions:

1.0

→

1.0

1.0Purine nucleoside + 1.0Inorganic phosphate → 1.0Purine + 1.0Ribose-1-phosphate
ReactionCard

Metabolites:

ECMDB ID	Name	View
ECMDB00034	Adenine	MetaboCard
ECMDB00050	Adenosine	MetaboCard
ECMDB00101	Deoxyadenosine	MetaboCard
ECMDB00085	Deoxyguanosine	MetaboCard
ECMDB00071	Deoxyinosine	MetaboCard
ECMDB01351	Deoxyribose 1-phosphate	MetaboCard
ECMDB00012	Deoxyuridine	MetaboCard
ECMDB00132	Guanine	MetaboCard
ECMDB00133	Guanosine	MetaboCard
ECMDB21225	Hydrogen ion	MetaboCard
ECMDB00157	Hypoxanthine	MetaboCard
ECMDB21380	Inorganic phosphate	MetaboCard
ECMDB00195	Inosine	MetaboCard
ECMDB01406	Niacinamide	MetaboCard
ECMDB00855	Nicotinamide riboside	MetaboCard
ECMDB01488	Nicotinic acid	MetaboCard
ECMDB01429	Phosphate	MetaboCard
ECMDB01366	Purine	MetaboCard
ECMDB23826	Purine deoxyribonucleoside	MetaboCard
ECMDB23238	Purine nucleoside	MetaboCard
ECMDB04147	Ribose-1-phosphate	MetaboCard
ECMDB00300	Uracil	MetaboCard
ECMDB00292	Xanthine	MetaboCard
ECMDB00299	Xanthosine	MetaboCard

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 Orientation

Clockwise

Centisome Percentage:

99.55

Left Sequence End

4618906

Right Sequence End

4619625

Gene Sequence:

>720 bp
GTGAATGTCAATTTCTTTGTCACCTGTATTGGTGACGCCCTGAAATCAAGAATGGCACGA
GACTCCGTGCTGCTACTGGAAAAACTCGGCTGTCGCGTAAATTTCCCGGAGAAACAGGGA
TGCTGCGGTCAGCCTGCGATCAATAGCGGTTATATCAAAGAAGCGATTCCAGGGATGAAA
AATCTGATCGCCGCACTGGAGGATAACGACGATCCCATTATTTCACCGGCTGGCTCTTGC
ACCTATGCCGTAAAAAGTTACCCGACGTATCTGGCGGATGAACCTGAATGGGCATCACGT
GCCGCAAAGGTTGCCGCGCGTATGCAGGATCTCACCTCTTTTATTGTTAATAAATTAGGG
GTAGTCGATGTAGGTGCCAGTTTGCAAGGGAGAGCGGTGTATCACCCATCTTGTAGCCTG
GCCCGTAAGCTGGGAGTGAAGGACGAGCCACTTACGCTGCTGAAAAATGTGCGTGGACTG
GAGCTGTTGACCTTTGCTGAACAGGATACCTGCTGCGGATTTGGCGGCACGTTCTCGGTC
AAAATGGCCGAAATATCCGGCGAGATGGTGAAAGAAAAGGTTGCGCACCTGATGGAAGTC
CGCCCTGAGTATTTAATTGGTGCTGACGTGAGTTGCCTGCTAAACATCAGTGGGCGATTA
CAACGGGAAGGGCAGAAAGTCAAAGTGATGCATATTGCTGAAGTGTTGATGAGCCGCTGA

Protein Properties

Pfam Domain Function:

PNP_UDP_1 (PF01048 )

Protein Residues:

239

Protein Molecular Weight:

25950

Protein Theoretical pI:

PDB File:

1PW7

Signaling Regions:

None

Transmembrane Regions:

None

Protein Sequence:

>Purine nucleoside phosphorylase deoD-type
MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISV
MGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIR
FKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVE
MEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE

References

External Links:

Resource	Link
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

Purine nucleoside phosphorylase deoD-type (P0ABP8)