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P0ABP8 (DEOD_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 82. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Purine nucleoside phosphorylase DeoD-type

Short name=PNP
EC=2.4.2.1
Alternative name(s):
Inosine phosphorylase
Gene names
Name:deoD
Synonyms:pup
Ordered Locus Names:b4384, JW4347
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length239 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. HAMAP-Rule MF_01627

Catalytic activity

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01627

Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01627

Subunit structure

Homohexamer.

Sequence similarities

Belongs to the PNP/UDP phosphorylase family.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

itself3EBI-907568,EBI-907568

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 239238Purine nucleoside phosphorylase DeoD-type HAMAP-Rule MF_01627
PRO_0000063130

Amino acid modifications

Modified residue271N6-acetyllysine Ref.7

Secondary structure

...................................... 239
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0ABP8 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 71D3DFAA5A176970

FASTA23925,950
        10         20         30         40         50         60 
MATPHINAEM GDFADVVLMP GDPLRAKYIA ETFLEDAREV NNVRGMLGFT GTYKGRKISV 

        70         80         90        100        110        120 
MGHGMGIPSC SIYTKELITD FGVKKIIRVG SCGAVLPHVK LRDVVIGMGA CTDSKVNRIR 

       130        140        150        160        170        180 
FKDHDFAAIA DFDMVRNAVD AAKALGIDAR VGNLFSADLF YSPDGEMFDV MEKYGILGVE 

       190        200        210        220        230 
MEAAGIYGVA AEFGAKALTI CTVSDHIRTH EQTTAAERQT TFNDMIKIAL ESVLLGDKE 

« Hide

References

« Hide 'large scale' references
[1]"Use of site-directed mutagenesis to enhance the epitope-shielding effect of covalent modification of proteins with polyethylene glycol."
Hershfield M.S., Chaffee S., Koro-Johnson L., Mary A., Smith A.A., Short S.A.
Proc. Natl. Acad. Sci. U.S.A. 88:7185-7189(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[3]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, 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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases."
Henzel W.J., Billeci T.M., Stults J.T., Wong S.C., Grimley C., Watanabe C.
Proc. Natl. Acad. Sci. U.S.A. 90:5011-5015(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21.
[6]"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."
Larsen J.E.L., Albrechtsen B., Valentin-Hansen P.
Nucleic Acids Res. 15:5125-5140(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 225-239.
Strain: K12.
[7]"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli."
Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y.
Mol. Cell. Proteomics 8:215-225(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
[8]"The crystal structure of Escherichia coli purine nucleoside phosphorylase: a comparison with the human enzyme reveals a conserved topology."
Mao C., Cook W.J., Zhou M., Koszalka G.W., Krenitsky T.A., Ealick S.E.
Structure 5:1373-1383(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]"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."
Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.
J. Mol. Biol. 280:153-166(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M60917 Genomic DNA. Translation: AAA24401.1.
U14003 Genomic DNA. Translation: AAA97280.1.
U00096 Genomic DNA. Translation: AAC77337.1.
AP009048 Genomic DNA. Translation: BAE78373.1.
X05629 Genomic DNA. Translation: CAA29114.1.
PIRA27854. A41143.
RefSeqNP_418801.1. NC_000913.3.
YP_492514.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A69X-ray2.10A/B/C2-239[»]
1ECPX-ray2.00A/B/C/D/E/F2-239[»]
1K9SX-ray2.00A/B/C/D/E/F2-237[»]
1OTXX-ray2.70A/B/C2-238[»]
1OTYX-ray2.50A/B/C2-238[»]
1OU4X-ray2.50A/B/C2-238[»]
1OUMX-ray2.40A/B/C2-238[»]
1OV6X-ray2.40A/B/C2-238[»]
1OVGX-ray2.20A/B/C2-238[»]
3ONVX-ray1.89A/B/C2-238[»]
3OOEX-ray2.00A/B/C/D/E/F2-238[»]
3OOHX-ray2.90A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R2-238[»]
3OPVX-ray2.40A/B/C/D/E/F/G/H/I/J/K/L2-238[»]
3UT6X-ray1.90A/B/C2-238[»]
ProteinModelPortalP0ABP8.
SMRP0ABP8. Positions 2-238.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-36195N.
IntActP0ABP8. 2 interactions.
MINTMINT-8328110.
STRING511145.b4384.

Chemistry

DrugBankDB00194. Vidarabine.

2D gel databases

SWISS-2DPAGEP0ABP8.

Proteomic databases

PaxDbP0ABP8.
PRIDEP0ABP8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77337; AAC77337; b4384.
BAE78373; BAE78373; BAE78373.
GeneID12934012.
945654.
KEGGecj:Y75_p4268.
eco:b4384.
PATRIC32124384. VBIEscCol129921_4532.

Organism-specific databases

EchoBASEEB0218.
EcoGeneEG10222. deoD.

Phylogenomic databases

eggNOGCOG0813.
HOGENOMHOG000274896.
KOK03784.
OMASFETHAF.
OrthoDBEOG6BKJC5.
PhylomeDBP0ABP8.
ProtClustDBPRK05819.

Enzyme and pathway databases

BioCycEcoCyc:DEOD-MONOMER.
ECOL316407:JW4347-MONOMER.
MetaCyc:DEOD-MONOMER.

Gene expression databases

GenevestigatorP0ABP8.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
HAMAPMF_01627. Pur_nucleosid_phosp.
InterProIPR004402. DeoD-type.
IPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERPTHR21234. PTHR21234. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR00107. deoD. 1 hit.
PROSITEPS01232. PNP_UDP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP0ABP8.
PROP0ABP8.

Entry information

Entry nameDEOD_ECOLI
AccessionPrimary (citable) accession number: P0ABP8
Secondary accession number(s): P09743, Q2M5T3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 82 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene