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P81989 (PUNA_CELSP) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 67. 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·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Purine nucleoside phosphorylase

Short name=PNP
EC=2.4.2.1
Alternative name(s):
Inosine phosphorylase
Inosine-guanosine phosphorylase
Gene names
Name:punA
OrganismCellulomonas sp.
Taxonomic identifier40001 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The purine nucleoside phosphorylases catalyze the phosphorolytic breakdown of the N-glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the formation of the corresponding free purine bases and pentose-1-phosphate. Cleaves guanosine and inosine. Ref.1

Catalytic activity

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

Pathway

Purine metabolism; purine nucleoside salvage.

Subunit structure

Homotrimer.

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family.

Ontologies

Keywords
   Molecular functionGlycosyltransferase
Transferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processnucleoside metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functionpurine-nucleoside phosphorylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Purine nucleoside phosphorylase
PRO_0000184541

Regions

Compositional bias1 – 44Poly-Thr

Sites

Active site2041 Potential

Secondary structure

........................................ 282
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P81989 [UniParc].

Last modified June 1, 2000. Version 1.
Checksum: 65F468DACC43D360

FASTA28229,021
        10         20         30         40         50         60 
TTTTPPSTPP LDDPATDPFL VARAAADHIA QATGVEGHDM ALVLGSGWGG AAELLGEVVA 

        70         80         90        100        110        120 
EVPTHEIPGF SAPAVAGHLS VTRSIRVERA DGSVRHALVL GSRTHLYEGK GVRAVVHGVR 

       130        140        150        160        170        180 
TAAATGAETL ILTNGCGGLN QEWGAGTPVL LSDHINLTAR SPLEGPTFVD LTDVYSPRLR 

       190        200        210        220        230        240 
ELAHRVDPTL PEGVYAQFPG PHYETPAEVR MAGILGADLV GMSTTLEAIA ARHCGLEVLG 

       250        260        270        280 
VSLVTNLAAG ISPTPLSHAE VIEAGQAAGP RISALLADIA KR 

« Hide

References

[1]"Crystal structure of the purine nucleoside phosphorylase (PNP) from Cellulomonas sp. and its implication for the mechanism of trimeric PNPs."
Tebbe J., Bzowska A., Wielgus-Kutrowska B., Schroeder W., Kazimierczuk Z., Shugar D., Saenger W., Koellner G.
J. Mol. Biol. 294:1239-1255(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION.

Cross-references

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3XX-ray2.40A/B/C9-282[»]
1QE5X-ray2.20A/B/C9-282[»]
ProteinModelPortalP81989.
SMRP81989. Positions 9-282.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.4.2.1. 1235.
UniPathwayUPA00606.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
InterProIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011269. PUNP.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFPIRSF000477. PurNPase. 1 hit.
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01697. PNPH-PUNA-XAPA. 1 hit.
TIGR01698. PUNP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP81989.

Entry information

Entry namePUNA_CELSP
AccessionPrimary (citable) accession number: P81989
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 2000
Last modified: April 16, 2014
This is version 67 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways