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Protein

Purine nucleoside phosphorylase

Gene

PNP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 5 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.1 Publication

Catalytic activityi

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

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 sitei33Phosphate1 Publication1
Binding sitei64Phosphate1 Publication1
Binding sitei116Phosphate; via amide nitrogen1 Publication1
Binding sitei201Purine nucleoside1 Publication1
Binding sitei220Phosphate1 Publication1
Binding sitei243Purine nucleoside1 Publication1

GO - Molecular functioni

  • purine-nucleoside phosphorylase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Enzyme and pathway databases

BRENDAi2.4.2.1. 908.
ReactomeiR-BTA-6798695. Neutrophil degranulation.
R-BTA-74217. Purine salvage.
R-BTA-74259. Purine catabolism.
SABIO-RKP55859.
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:PNP
Synonyms:NP
OrganismiBos taurus (Bovine)
Taxonomic identifieri9913 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos
Proteomesi
  • UP000009136 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

Pathology & Biotechi

Chemistry databases

ChEMBLiCHEMBL2935.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001845351 – 289Purine nucleoside phosphorylaseAdd BLAST289

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineBy similarity1
Modified residuei251PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiP55859.
PeptideAtlasiP55859.
PRIDEiP55859.

Expressioni

Gene expression databases

BgeeiENSBTAG00000012317.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016346.

Chemistry databases

BindingDBiP55859.

Structurei

Secondary structure

1289
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi7 – 20Combined sources14
Beta strandi26 – 31Combined sources6
Helixi36 – 41Combined sources6
Beta strandi43 – 49Combined sources7
Helixi50 – 52Combined sources3
Beta strandi62 – 64Combined sources3
Beta strandi67 – 73Combined sources7
Beta strandi76 – 83Combined sources8
Helixi87 – 89Combined sources3
Helixi93 – 96Combined sources4
Helixi98 – 106Combined sources9
Beta strandi110 – 119Combined sources10
Beta strandi129 – 137Combined sources9
Helixi138 – 141Combined sources4
Turni153 – 155Combined sources3
Helixi168 – 181Combined sources14
Beta strandi188 – 194Combined sources7
Helixi203 – 211Combined sources9
Beta strandi215 – 221Combined sources7
Helixi222 – 230Combined sources9
Beta strandi234 – 244Combined sources11
Beta strandi248 – 250Combined sources3
Helixi257 – 278Combined sources22
Helixi279 – 281Combined sources3
Beta strandi284 – 287Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A9OX-ray2.00A1-289[»]
1A9PX-ray2.40A1-289[»]
1A9QX-ray2.00A1-282[»]
1A9RX-ray2.00A1-282[»]
1A9SX-ray2.00A1-289[»]
1A9TX-ray2.00A1-284[»]
1B8NX-ray2.00A1-284[»]
1B8OX-ray1.50A1-284[»]
1FXUX-ray2.20A1-289[»]
1LV8X-ray2.30A/B/C/D/E/F1-289[»]
1LVUX-ray2.05A/B/C/D/E/F1-289[»]
1PBNX-ray2.00A1-289[»]
1V48X-ray2.20A1-289[»]
1VFNX-ray2.15A4-284[»]
2AI1X-ray2.00A1-289[»]
2AI2X-ray1.70A1-289[»]
2AI3X-ray1.70A1-289[»]
2QPLX-ray2.10A3-284[»]
3FUCX-ray1.45A/B/C1-284[»]
3PNPX-ray1.60A1-289[»]
4PNPX-ray1.80A1-289[»]
ProteinModelPortaliP55859.
SMRiP55859.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55859.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni84 – 86Phosphate binding1 Publication3

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family.Curated

Phylogenomic databases

eggNOGiKOG3984. Eukaryota.
COG0005. LUCA.
GeneTreeiENSGT00550000074740.
HOGENOMiHOG000045183.
HOVERGENiHBG002460.
InParanoidiP55859.
OMAiTIAGHEG.
OrthoDBiEOG091G0GEE.
TreeFamiTF300049.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P55859-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MANGYTYEDY QDTAKWLLSH TEQRPQVAVI CGSGLGGLVN KLTQAQTFDY
60 70 80 90 100
SEIPNFPEST VPGHAGRLVF GILNGRACVM MQGRFHMYEG YPFWKVTFPV
110 120 130 140 150
RVFRLLGVET LVVTNAAGGL NPNFEVGDIM LIRDHINLPG FSGENPLRGP
160 170 180 190 200
NEERFGVRFP AMSDAYDRDM RQKAHSTWKQ MGEQRELQEG TYVMLGGPNF
210 220 230 240 250
ETVAECRLLR NLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE
260 270 280
SQGKANHEEV LEAGKQAAQK LEQFVSLLMA SIPVSGHTG
Length:289
Mass (Da):32,037
Last modified:February 5, 2008 - v3
Checksum:i7ECF84CCA494DEED
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti2A → Q AA sequence (PubMed:7607309).Curated1
Sequence conflicti25P → S in AAX46392 (PubMed:16305752).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021545 mRNA. Translation: AAX46392.1.
BC103291 mRNA. Translation: AAI03292.2.
PIRiS66203.
UniGeneiBt.65253.

Genome annotation databases

EnsembliENSBTAT00000016346; ENSBTAP00000016346; ENSBTAG00000012317.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BT021545 mRNA. Translation: AAX46392.1.
BC103291 mRNA. Translation: AAI03292.2.
PIRiS66203.
UniGeneiBt.65253.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1A9OX-ray2.00A1-289[»]
1A9PX-ray2.40A1-289[»]
1A9QX-ray2.00A1-282[»]
1A9RX-ray2.00A1-282[»]
1A9SX-ray2.00A1-289[»]
1A9TX-ray2.00A1-284[»]
1B8NX-ray2.00A1-284[»]
1B8OX-ray1.50A1-284[»]
1FXUX-ray2.20A1-289[»]
1LV8X-ray2.30A/B/C/D/E/F1-289[»]
1LVUX-ray2.05A/B/C/D/E/F1-289[»]
1PBNX-ray2.00A1-289[»]
1V48X-ray2.20A1-289[»]
1VFNX-ray2.15A4-284[»]
2AI1X-ray2.00A1-289[»]
2AI2X-ray1.70A1-289[»]
2AI3X-ray1.70A1-289[»]
2QPLX-ray2.10A3-284[»]
3FUCX-ray1.45A/B/C1-284[»]
3PNPX-ray1.60A1-289[»]
4PNPX-ray1.80A1-289[»]
ProteinModelPortaliP55859.
SMRiP55859.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016346.

Chemistry databases

BindingDBiP55859.
ChEMBLiCHEMBL2935.

Proteomic databases

PaxDbiP55859.
PeptideAtlasiP55859.
PRIDEiP55859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016346; ENSBTAP00000016346; ENSBTAG00000012317.

Phylogenomic databases

eggNOGiKOG3984. Eukaryota.
COG0005. LUCA.
GeneTreeiENSGT00550000074740.
HOGENOMiHOG000045183.
HOVERGENiHBG002460.
InParanoidiP55859.
OMAiTIAGHEG.
OrthoDBiEOG091G0GEE.
TreeFamiTF300049.

Enzyme and pathway databases

UniPathwayiUPA00606.
BRENDAi2.4.2.1. 908.
ReactomeiR-BTA-6798695. Neutrophil degranulation.
R-BTA-74217. Purine salvage.
R-BTA-74259. Purine catabolism.
SABIO-RKP55859.

Miscellaneous databases

EvolutionaryTraceiP55859.

Gene expression databases

BgeeiENSBTAG00000012317.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
InterProiIPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR011270. Pur_Nuc_Pase_Ino/Guo-sp.
IPR011268. Purine_phosphorylase.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
PIRSFiPIRSF000477. PurNPase. 1 hit.
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01700. PNPH. 1 hit.
TIGR01697. PNPH-PUNA-XAPA. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPNPH_BOVIN
AccessioniPrimary (citable) accession number: P55859
Secondary accession number(s): Q3ZBH6, Q58DQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 5, 2008
Last modified: November 30, 2016
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

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.