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Protein

Purine nucleoside phosphorylase DeoD-type

Gene

deoD

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

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

Catalytic activityi

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei5Purine nucleoside; shared with dimeric partnerBy similarity1
Binding sitei21Phosphate; via amide nitrogen1 Publication1
Binding sitei25Phosphate1 Publication1
Binding sitei44Phosphate; shared with dimeric partner1 Publication1

GO - Molecular functioni

  • identical protein binding Source: IntAct
  • purine-nucleoside phosphorylase activity Source: EcoCyc

GO - Biological processi

  • cellular response to DNA damage stimulus Source: EcoliWiki
  • purine nucleoside catabolic process Source: EcoCyc
  • purine nucleoside interconversion Source: EcoCyc

Keywordsi

Molecular functionGlycosyltransferase, Transferase

Enzyme and pathway databases

BioCyciEcoCyc:DEOD-MONOMER
MetaCyc:DEOD-MONOMER
BRENDAi2.4.2.1 2026

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphorylase DeoD-type (EC:2.4.2.11 Publication)
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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10222 deoD

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: EcoCyc
  • membrane Source: UniProtKB

Pathology & Biotechi

Chemistry databases

DrugBankiDB02947 2-Fluoro-2'-Deoxyadenosine
DB04441 2-Fluoroadenosine
DB03986 6-Methyl-Formycin A
DB02113 6-Methylpurine
DB03735 9-(2-Deoxy-Beta-D-Ribofuranosyl)-6-Methylpurine
DB02934 9-(6-Deoxy-Alpha-L-Talofuranosyl)-6-Methylpurine
DB03952 9-(6-Deoxy-Beta-D-Allofuranosyl)-6-Methylpurine
DB03528 9-Beta-D-Xylofuranosyl-Adenine
DB04198 Formycin B
DB04335 Inosine
DB02896 Methylthioinosine
DB02066 N7-Methyl-Formycin A
DB03172 Tubercidin

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00000631302 – 239Purine nucleoside phosphorylase DeoD-typeAdd BLAST238

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei27N6-acetyllysine1 Publication1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP0ABP8
PaxDbiP0ABP8
PRIDEiP0ABP8

2D gel databases

SWISS-2DPAGEiP0ABP8

PTM databases

iPTMnetiP0ABP8

Interactioni

Subunit structurei

Homohexamer.2 Publications

Binary interactionsi

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

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi4263006, 10 interactors
DIPiDIP-36195N
IntActiP0ABP8, 2 interactors
MINTiP0ABP8
STRINGi316385.ECDH10B_4542

Structurei

Secondary structure

1239
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi15 – 19Combined sources5
Helixi23 – 33Combined sources11
Beta strandi35 – 41Combined sources7
Helixi43 – 45Combined sources3
Beta strandi48 – 53Combined sources6
Beta strandi56 – 61Combined sources6
Helixi67 – 80Combined sources14
Beta strandi85 – 94Combined sources10
Beta strandi96 – 99Combined sources4
Beta strandi104 – 113Combined sources10
Helixi116 – 120Combined sources5
Turni121 – 123Combined sources3
Helixi132 – 145Combined sources14
Beta strandi149 – 156Combined sources8
Helixi167 – 173Combined sources7
Beta strandi178 – 182Combined sources5
Helixi183 – 193Combined sources11
Beta strandi196 – 206Combined sources11
Turni207 – 209Combined sources3
Helixi215 – 220Combined sources6
Helixi223 – 237Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB 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[»]
4TS3X-ray2.30A/B/C/D/E/F2-238[»]
4TS9X-ray1.77A/B/C2-238[»]
4TTAX-ray2.00A/B/C/D/E/F2-238[»]
4TTIX-ray1.89A/B/C/D/E/F2-238[»]
4TTJX-ray1.87A/B/D2-238[»]
5I3CX-ray2.32A/B/C2-238[»]
5IU6X-ray2.51A/B/C2-238[»]
ProteinModelPortaliP0ABP8
SMRiP0ABP8
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABP8

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 91Phosphate binding1 Publication4
Regioni180 – 182Purine nucleoside bindingBy similarity3
Regioni204 – 205Purine nucleoside bindingBy similarity2

Sequence similaritiesi

Belongs to the PNP/UDP phosphorylase family.Curated

Phylogenomic databases

eggNOGiENOG4105D3A Bacteria
COG0813 LUCA
HOGENOMiHOG000274896
InParanoidiP0ABP8
KOiK03784
OMAiPQCLLCG
PhylomeDBiP0ABP8

Family and domain databases

HAMAPiMF_01627 Pur_nucleosid_phosp, 1 hit
InterProiView protein in InterPro
IPR004402 DeoD-type
IPR018016 Nucleoside_phosphorylase_CS
IPR000845 Nucleoside_phosphorylase_d
IPR035994 Nucleoside_phosphorylase_sf
PANTHERiPTHR43691:SF2 PTHR43691:SF2, 1 hit
PfamiView protein in Pfam
PF01048 PNP_UDP_1, 1 hit
SUPFAMiSSF53167 SSF53167, 1 hit
TIGRFAMsiTIGR00107 deoD, 1 hit
PROSITEiView protein in PROSITE
PS01232 PNP_UDP_1, 1 hit

Sequencei

Sequence statusi: Complete.

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

P0ABP8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATPHINAEM GDFADVVLMP GDPLRAKYIA ETFLEDAREV NNVRGMLGFT
60 70 80 90 100
GTYKGRKISV MGHGMGIPSC SIYTKELITD FGVKKIIRVG SCGAVLPHVK
110 120 130 140 150
LRDVVIGMGA CTDSKVNRIR FKDHDFAAIA DFDMVRNAVD AAKALGIDAR
160 170 180 190 200
VGNLFSADLF YSPDGEMFDV MEKYGILGVE MEAAGIYGVA AEFGAKALTI
210 220 230
CTVSDHIRTH EQTTAAERQT TFNDMIKIAL ESVLLGDKE
Length:239
Mass (Da):25,950
Last modified:January 23, 2007 - v2
Checksum:i71D3DFAA5A176970
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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
WP_000224877.1, NZ_LN832404.1

Genome annotation databases

EnsemblBacteriaiAAC77337; AAC77337; b4384
BAE78373; BAE78373; BAE78373
GeneIDi945654
KEGGiecj:JW4347
eco:b4384
PATRICifig|1411691.4.peg.2301

Similar proteinsi

Entry informationi

Entry nameiDEOD_ECOLI
AccessioniPrimary (citable) accession number: P0ABP8
Secondary accession number(s): P09743, Q2M5T3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 8, 2005
Last sequence update: January 23, 2007
Last modified: March 28, 2018
This is version 110 of the entry and version 2 of the sequence. See 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

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