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P0ABP8

- DEOD_ECOLI

UniProt

P0ABP8 - DEOD_ECOLI

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Protein
Purine nucleoside phosphorylase DeoD-type
Gene
deoD, pup, b4384, JW4347
Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules.UniRule annotation

Catalytic activityi

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate.UniRule annotation
Purine deoxynucleoside + phosphate = purine + 2'-deoxy-alpha-D-ribose 1-phosphate.UniRule annotation

GO - Molecular functioni

  1. identical protein binding Source: IntAct
  2. purine-nucleoside phosphorylase activity Source: EcoCyc

GO - Biological processi

  1. cellular response to DNA damage stimulus Source: EcoliWiki
  2. purine nucleoside catabolic process Source: EcoCyc
  3. purine nucleoside interconversion Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

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

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphorylase DeoD-type (EC:2.4.2.1)
Short name:
PNP
Alternative name(s):
Inosine phosphorylase
Gene namesi
Name:deoD
Synonyms:pup
Ordered Locus Names:b4384, JW4347
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10222. deoD.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: UniProtKB
  2. membrane Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 239238Purine nucleoside phosphorylase DeoD-typeUniRule annotation
PRO_0000063130Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP0ABP8.
PRIDEiP0ABP8.

2D gel databases

SWISS-2DPAGEP0ABP8.

Expressioni

Gene expression databases

GenevestigatoriP0ABP8.

Interactioni

Subunit structurei

Homohexamer.

Binary interactionsi

WithEntry#Exp.IntActNotes
itself7EBI-907568,EBI-907568

Protein-protein interaction databases

DIPiDIP-36195N.
IntActiP0ABP8. 2 interactions.
MINTiMINT-8328110.
STRINGi511145.b4384.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi15 – 195
Helixi23 – 3311
Beta strandi35 – 417
Helixi43 – 453
Beta strandi48 – 536
Beta strandi56 – 616
Helixi67 – 8014
Beta strandi85 – 9410
Beta strandi96 – 994
Beta strandi104 – 11310
Helixi116 – 1205
Turni121 – 1233
Helixi132 – 14413
Beta strandi150 – 1567
Helixi167 – 1737
Beta strandi178 – 1825
Helixi183 – 19311
Beta strandi196 – 20611
Turni207 – 2093
Helixi215 – 23723

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
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/F2-238[»]
1OTXX-ray2.70A/B/C2-239[»]
1OTYX-ray2.50A/B/C2-239[»]
1OU4X-ray2.50A/B/C2-239[»]
1OUMX-ray2.40A/B/C2-239[»]
1OV6X-ray2.40A/B/C2-239[»]
1OVGX-ray2.20A/B/C2-239[»]
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[»]
ProteinModelPortaliP0ABP8.
SMRiP0ABP8. Positions 2-238.

Miscellaneous databases

EvolutionaryTraceiP0ABP8.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0813.
HOGENOMiHOG000274896.
KOiK03784.
OMAiRQTTFSE.
OrthoDBiEOG6BKJC5.
PhylomeDBiP0ABP8.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01627. Pur_nucleosid_phosp.
InterProiIPR004402. DeoD-type.
IPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERiPTHR21234. PTHR21234. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR00107. deoD. 1 hit.
PROSITEiPS01232. PNP_UDP_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0ABP8-1 [UniParc]FASTAAdd to Basket

« Hide

MATPHINAEM GDFADVVLMP GDPLRAKYIA ETFLEDAREV NNVRGMLGFT    50
GTYKGRKISV MGHGMGIPSC SIYTKELITD FGVKKIIRVG SCGAVLPHVK 100
LRDVVIGMGA CTDSKVNRIR FKDHDFAAIA DFDMVRNAVD AAKALGIDAR 150
VGNLFSADLF YSPDGEMFDV MEKYGILGVE MEAAGIYGVA AEFGAKALTI 200
CTVSDHIRTH EQTTAAERQT TFNDMIKIAL ESVLLGDKE 239
Length:239
Mass (Da):25,950
Last modified:January 23, 2007 - v2
Checksum:i71D3DFAA5A176970
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiA41143. A27854.
RefSeqiNP_418801.1. NC_000913.3.
YP_492514.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77337; AAC77337; b4384.
BAE78373; BAE78373; BAE78373.
GeneIDi12934012.
945654.
KEGGiecj:Y75_p4268.
eco:b4384.
PATRICi32124384. VBIEscCol129921_4532.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi A41143. A27854.
RefSeqi NP_418801.1. NC_000913.3.
YP_492514.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1A69 X-ray 2.10 A/B/C 2-239 [» ]
1ECP X-ray 2.00 A/B/C/D/E/F 2-239 [» ]
1K9S X-ray 2.00 A/B/C/D/E/F 2-238 [» ]
1OTX X-ray 2.70 A/B/C 2-239 [» ]
1OTY X-ray 2.50 A/B/C 2-239 [» ]
1OU4 X-ray 2.50 A/B/C 2-239 [» ]
1OUM X-ray 2.40 A/B/C 2-239 [» ]
1OV6 X-ray 2.40 A/B/C 2-239 [» ]
1OVG X-ray 2.20 A/B/C 2-239 [» ]
3ONV X-ray 1.89 A/B/C 2-238 [» ]
3OOE X-ray 2.00 A/B/C/D/E/F 2-238 [» ]
3OOH X-ray 2.90 A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R 2-238 [» ]
3OPV X-ray 2.40 A/B/C/D/E/F/G/H/I/J/K/L 2-238 [» ]
3UT6 X-ray 1.90 A/B/C 2-238 [» ]
ProteinModelPortali P0ABP8.
SMRi P0ABP8. Positions 2-238.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

DIPi DIP-36195N.
IntActi P0ABP8. 2 interactions.
MINTi MINT-8328110.
STRINGi 511145.b4384.

Chemistry

DrugBanki DB00194. Vidarabine.

2D gel databases

SWISS-2DPAGE P0ABP8.

Proteomic databases

PaxDbi P0ABP8.
PRIDEi P0ABP8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77337 ; AAC77337 ; b4384 .
BAE78373 ; BAE78373 ; BAE78373 .
GeneIDi 12934012.
945654.
KEGGi ecj:Y75_p4268.
eco:b4384.
PATRICi 32124384. VBIEscCol129921_4532.

Organism-specific databases

EchoBASEi EB0218.
EcoGenei EG10222. deoD.

Phylogenomic databases

eggNOGi COG0813.
HOGENOMi HOG000274896.
KOi K03784.
OMAi RQTTFSE.
OrthoDBi EOG6BKJC5.
PhylomeDBi P0ABP8.

Enzyme and pathway databases

BioCyci EcoCyc:DEOD-MONOMER.
ECOL316407:JW4347-MONOMER.
MetaCyc:DEOD-MONOMER.

Miscellaneous databases

EvolutionaryTracei P0ABP8.
PROi P0ABP8.

Gene expression databases

Genevestigatori P0ABP8.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
HAMAPi MF_01627. Pur_nucleosid_phosp.
InterProi IPR004402. DeoD-type.
IPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view ]
PANTHERi PTHR21234. PTHR21234. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR00107. deoD. 1 hit.
PROSITEi PS01232. PNP_UDP_1. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiDEOD_ECOLI
AccessioniPrimary (citable) accession number: P0ABP8
Secondary accession number(s): P09743, Q2M5T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 85 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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