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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, inosine, 2'-deoxyguanosine and 2'-deoxyinosine.1 Publication

Catalytic activityi

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

Pathwayi: purine nucleoside salvage

This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.
View all proteins of this organism that are known to be involved in the pathway purine nucleoside salvage and in Purine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei46PhosphateBy similarity1
Binding sitei78PhosphateBy similarity1
Active sitei204Sequence analysis1
Binding sitei204Purine nucleosideBy similarity1
Binding sitei223PhosphateBy similarity1
Binding sitei246Purine nucleosideBy similarity1

GO - Molecular functioni

GO - Biological processi

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
Short name:
Pu-NPase
Alternative name(s):
Inosine phosphorylase
Inosine-guanosine phosphorylase
Gene namesi
Name:punA
OrganismiCellulomonas sp.
Taxonomic identifieri40001 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaMicrococcalesCellulomonadaceaeCellulomonas

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001845411 – 282Purine nucleoside phosphorylaseAdd BLAST282

Interactioni

Subunit structurei

Homotrimer.1 Publication

Structurei

Secondary structure

1282
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 33Combined sources16
Beta strandi39 – 43Combined sources5
Turni49 – 54Combined sources6
Beta strandi57 – 63Combined sources7
Helixi64 – 66Combined sources3
Beta strandi81 – 88Combined sources8
Beta strandi94 – 99Combined sources6
Helixi106 – 108Combined sources3
Helixi112 – 115Combined sources4
Helixi117 – 124Combined sources8
Beta strandi129 – 138Combined sources10
Beta strandi148 – 156Combined sources9
Helixi177 – 186Combined sources10
Beta strandi192 – 197Combined sources6
Helixi206 – 215Combined sources10
Beta strandi218 – 224Combined sources7
Helixi225 – 233Combined sources9
Beta strandi237 – 247Combined sources11
Turni249 – 251Combined sources3
Beta strandi252 – 254Combined sources3
Helixi258 – 280Combined sources23

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP81989.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni103 – 105Phosphate bindingBy similarity3

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1 – 4Poly-Thr4

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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C3XX-ray2.40A/B/C9-282[»]
1QE5X-ray2.20A/B/C9-282[»]
ProteinModelPortaliP81989.
SMRiP81989.
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...

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 2, 2016
This is version 76 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

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 one 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.