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Protein

Purine nucleoside phosphorylase

Gene

punA

Organism
Cellulomonas sp.
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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.1 Publication

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei204 – 2041Sequence Analysis

GO - Molecular functioni

  1. purine-nucleoside phosphorylase activity Source: UniProtKB-EC

GO - Biological processi

  1. nucleoside metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.2.1. 1235.
UniPathwayiUPA00606.

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphorylase (EC:2.4.2.1)
Short name:
PNP
Alternative name(s):
Inosine phosphorylase
Inosine-guanosine phosphorylase
Gene namesi
Name:punA
OrganismiCellulomonas sp.
Taxonomic identifieri40001 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaActinobacteridaeActinomycetalesMicrococcineaeCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 282282Purine nucleoside phosphorylasePRO_0000184541Add
BLAST

Interactioni

Subunit structurei

Homotrimer.

Structurei

Secondary structure

1
282
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 3316Combined sources
Beta strandi39 – 435Combined sources
Turni49 – 546Combined sources
Beta strandi57 – 637Combined sources
Helixi64 – 663Combined sources
Beta strandi81 – 888Combined sources
Beta strandi94 – 996Combined sources
Helixi106 – 1083Combined sources
Helixi112 – 1154Combined sources
Helixi117 – 1248Combined sources
Beta strandi129 – 13810Combined sources
Beta strandi148 – 1569Combined sources
Helixi177 – 18610Combined sources
Beta strandi192 – 1976Combined sources
Helixi206 – 21510Combined sources
Beta strandi218 – 2247Combined sources
Helixi225 – 2339Combined sources
Beta strandi237 – 24711Combined sources
Turni249 – 2513Combined sources
Beta strandi252 – 2543Combined sources
Helixi258 – 28023Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3XX-ray2.40A/B/C9-282[»]
1QE5X-ray2.20A/B/C9-282[»]
ProteinModelPortaliP81989.
SMRiP81989. Positions 9-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81989.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi1 – 44Poly-Thr

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family.Curated

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011269. PUNP.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01697. PNPH-PUNA-XAPA. 1 hit.
TIGR01698. PUNP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81989-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
TTTTPPSTPP LDDPATDPFL VARAAADHIA QATGVEGHDM ALVLGSGWGG
60 70 80 90 100
AAELLGEVVA EVPTHEIPGF SAPAVAGHLS VTRSIRVERA DGSVRHALVL
110 120 130 140 150
GSRTHLYEGK GVRAVVHGVR TAAATGAETL ILTNGCGGLN QEWGAGTPVL
160 170 180 190 200
LSDHINLTAR SPLEGPTFVD LTDVYSPRLR ELAHRVDPTL PEGVYAQFPG
210 220 230 240 250
PHYETPAEVR MAGILGADLV GMSTTLEAIA ARHCGLEVLG VSLVTNLAAG
260 270 280
ISPTPLSHAE VIEAGQAAGP RISALLADIA KR
Length:282
Mass (Da):29,021
Last modified:June 1, 2000 - v1
Checksum:i65F468DACC43D360
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1C3XX-ray2.40A/B/C9-282[»]
1QE5X-ray2.20A/B/C9-282[»]
ProteinModelPortaliP81989.
SMRiP81989. Positions 9-282.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

UniPathwayiUPA00606.
BRENDAi2.4.2.1. 1235.

Miscellaneous databases

EvolutionaryTraceiP81989.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011269. PUNP.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PTHR11904:SF9. PTHR11904:SF9. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01697. PNPH-PUNA-XAPA. 1 hit.
TIGR01698. PUNP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPUNA_CELSP
AccessioniPrimary (citable) accession number: P81989
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: June 1, 2000
Last modified: November 26, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.