Purine nucleoside phosphorylase DeoD-type

Details

Name
Purine nucleoside phosphorylase DeoD-type
Synonyms
  • 2.4.2.1
  • Inosine phosphorylase
  • PNP
  • pup
Gene Name
deoD
Organism
Escherichia coli (strain K12)
Amino acid sequence
>lcl|BSEQ0016645|Purine nucleoside phosphorylase DeoD-type
MATPHINAEMGDFADVVLMPGDPLRAKYIAETFLEDAREVNNVRGMLGFTGTYKGRKISV
MGHGMGIPSCSIYTKELITDFGVKKIIRVGSCGAVLPHVKLRDVVIGMGACTDSKVNRIR
FKDHDFAAIADFDMVRNAVDAAKALGIDARVGNLFSADLFYSPDGEMFDVMEKYGILGVE
MEAAGIYGVAAEFGAKALTICTVSDHIRTHEQTTAAERQTTFNDMIKIALESVLLGDKE
Number of residues
239
Molecular Weight
25949.68
Theoretical pI
5.35
GO Classification
Functions
identical protein binding / purine-nucleoside phosphorylase activity
Processes
cellular response to DNA damage stimulus / purine nucleoside catabolic process / purine nucleoside interconversion
Components
cytosol / membrane
General Function
Purine-nucleoside phosphorylase activity
Specific Function
Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.
Pfam Domain Function
Transmembrane Regions
Not Available
Cellular Location
Not Available
Gene sequence
>lcl|BSEQ0016646|Purine nucleoside phosphorylase DeoD-type (deoD)
ATGGCTACCCCACACATTAATGCAGAAATGGGCGATTTCGCTGACGTAGTTTTGATGCCA
GGCGACCCGCTGCGTGCGAAGTATATTGCTGAAACTTTCCTTGAAGATGCCCGTGAAGTG
AACAACGTTCGCGGTATGCTGGGCTTCACCGGTACTTACAAAGGCCGCAAAATTTCCGTA
ATGGGTCACGGTATGGGTATCCCGTCCTGCTCCATCTACACCAAAGAACTGATCACCGAT
TTCGGCGTGAAGAAAATTATCCGCGTGGGTTCCTGTGGCGCAGTTCTGCCGCACGTAAAA
CTGCGCGACGTCGTTATCGGTATGGGTGCCTGCACCGATTCCAAAGTTAACCGCATCCGT
TTTAAAGACCATGACTTTGCCGCTATCGCTGACTTCGACATGGTGCGTAACGCAGTAGAT
GCAGCTAAAGCACTGGGTATTGATGCTCGCGTGGGTAACCTGTTCTCCGCTGACCTGTTC
TACTCTCCGGACGGCGAAATGTTCGACGTGATGGAAAAATACGGCATTCTCGGCGTGGAA
ATGGAAGCGGCTGGTATCTACGGCGTCGCTGCAGAATTTGGCGCGAAAGCCCTGACCATC
TGCACCGTATCTGACCACATCCGCACTCACGAGCAGACCACTGCCGCTGAGCGTCAGACT
ACCTTCAACGACATGATCAAAATCGCACTGGAATCCGTTCTGCTGGGCGATAAAGAGTAA
Chromosome Location
Not Available
Locus
Not Available
External Identifiers
ResourceLink
UniProtKB IDP0ABP8
UniProtKB Entry NameDEOD_ECOLI
GenBank Protein ID147309
GenBank Gene IDM60917
General References
  1. Hershfield MS, Chaffee S, Koro-Johnson L, Mary A, Smith AA, Short SA: 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. 1991 Aug 15;88(16):7185-9. [Article]
  2. Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
  3. Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
  4. Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
  5. Henzel WJ, Billeci TM, Stults JT, Wong SC, Grimley C, Watanabe C: Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc Natl Acad Sci U S A. 1993 Jun 1;90(11):5011-5. [Article]
  6. Larsen JE, Albrechtsen B, Valentin-Hansen P: 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. 1987 Jul 10;15(13):5125-40. [Article]
  7. Zhang J, Sprung R, Pei J, Tan X, Kim S, Zhu H, Liu CF, Grishin NV, Zhao Y: Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli. Mol Cell Proteomics. 2009 Feb;8(2):215-25. doi: 10.1074/mcp.M800187-MCP200. Epub 2008 Aug 23. [Article]
  8. 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. 1997 Oct 15;5(10):1373-83. [Article]
  9. Koellner G, Luic M, Shugar D, Saenger W, Bzowska A: 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. 1998 Jul 3;280(1):153-66. [Article]
  10. Koellner G, Bzowska A, Wielgus-Kutrowska B, Luic M, Steiner T, Saenger W, Stepinski J: Open and closed conformation of the E. coli purine nucleoside phosphorylase active center and implications for the catalytic mechanism. J Mol Biol. 2002 Jan 18;315(3):351-71. [Article]

Drug Relations

Drug Relations
DrugBank IDNameDrug groupPharmacological action?ActionsDetails
DB02066N7-Methyl-Formycin AexperimentalunknownDetails
DB021136-MethylpurineexperimentalunknownDetails
DB02896MethylthioinosineexperimentalunknownDetails
DB029349-(6-deoxy-alpha-L-talofuranosyl)-6-methylpurineexperimentalunknownDetails
DB029472-Fluoro-2'-DeoxyadenosineexperimentalunknownDetails
DB03172TubercidinexperimentalunknownDetails
DB035289-Beta-D-Xylofuranosyl-AdenineexperimentalunknownDetails
DB037359-(2-Deoxy-Beta-D-Ribofuranosyl)-6-MethylpurineexperimentalunknownDetails
DB039529-(6-deoxy-beta-D-allofuranosyl)-6-methylpurineexperimentalunknownDetails
DB039866-methyl-formycin AexperimentalunknownDetails
DB04198Formycin BexperimentalunknownDetails
DB044412-FluoroadenosineexperimentalunknownDetails
DB04335Inosineexperimental, investigationalunknownDetails