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Protein

Purine nucleoside phosphorylase

Gene

PNP

Organism
Bos taurus (Bovine)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Pathway:ipurine 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.

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.
ReactomeiREACT_289815. Purine catabolism.
REACT_307801. Purine salvage.
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
ProteomesiUP000009136 Componenti: Chromosome 10

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 289289Purine nucleoside phosphorylasePRO_0000184535Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiP55859.
PRIDEiP55859.

Interactioni

Subunit structurei

Homotrimer.

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016346.

Structurei

Secondary structure

1
289
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 2014Combined sources
Beta strandi26 – 316Combined sources
Helixi36 – 416Combined sources
Beta strandi43 – 497Combined sources
Helixi50 – 523Combined sources
Beta strandi62 – 643Combined sources
Beta strandi67 – 737Combined sources
Beta strandi76 – 838Combined sources
Helixi87 – 893Combined sources
Helixi93 – 964Combined sources
Helixi98 – 1069Combined sources
Beta strandi110 – 11910Combined sources
Beta strandi129 – 1379Combined sources
Helixi138 – 1414Combined sources
Turni153 – 1553Combined sources
Helixi168 – 18114Combined sources
Beta strandi188 – 1947Combined sources
Helixi203 – 2119Combined sources
Beta strandi215 – 2217Combined sources
Helixi222 – 2309Combined sources
Beta strandi234 – 24411Combined sources
Beta strandi248 – 2503Combined sources
Helixi257 – 27822Combined sources
Helixi279 – 2813Combined sources
Beta strandi284 – 2874Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 3-282.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP55859.

Family & Domainsi

Sequence similaritiesi

Belongs to the PNP/MTAP phosphorylase family.Curated

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074740.
HOGENOMiHOG000045183.
HOVERGENiHBG002460.
InParanoidiP55859.
OMAiAEYRMLK.
OrthoDBiEOG73RBBZ.
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)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti2 – 21A → Q AA sequence (PubMed:7607309).Curated
Sequence conflicti25 – 251P → S in AAX46392 (PubMed:16305752).Curated

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
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. Positions 3-282.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9913.ENSBTAP00000016346.

Chemistry

BindingDBiP55859.
ChEMBLiCHEMBL2935.

Proteomic databases

PaxDbiP55859.
PRIDEiP55859.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSBTAT00000016346; ENSBTAP00000016346; ENSBTAG00000012317.

Phylogenomic databases

eggNOGiCOG0005.
GeneTreeiENSGT00550000074740.
HOGENOMiHOG000045183.
HOVERGENiHBG002460.
InParanoidiP55859.
OMAiAEYRMLK.
OrthoDBiEOG73RBBZ.
TreeFamiTF300049.

Enzyme and pathway databases

UniPathwayiUPA00606.
BRENDAi2.4.2.1. 908.
ReactomeiREACT_289815. Purine catabolism.
REACT_307801. Purine salvage.
SABIO-RKP55859.

Miscellaneous databases

EvolutionaryTraceiP55859.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Calf spleen purine nucleoside phosphorylase: purification, sequence and crystal structure of its complex with an N(7)-acycloguanosine inhibitor."
    Bzowska A., Luic M., Schroeder W., Shugar D., Saenger W., Koellner G.
    FEBS Lett. 367:214-218(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, FUNCTION.
    Tissue: Spleen.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. NIH - Mammalian Gene Collection (MGC) project
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Hereford.
    Tissue: Uterus.
  4. "Crystal structure of calf spleen purine nucleoside phosphorylase in a complex with hypoxanthine at 2.15-A resolution."
    Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.
    J. Mol. Biol. 265:202-216(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
    Tissue: Spleen.
  5. Mao C., Zhou M., Ealick S., Federov A.A., Almo S.C.
    Submitted (JUL-1995) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS).
  6. "Calf spleen purine nucleoside phosphorylase complexed with substrates and substrate analogues."
    Mao C., Cook W.J., Zhou M., Federov A.A., Almo S.C., Ealick S.E.
    Biochemistry 37:7135-7146(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
    Tissue: Spleen.
  7. "The high resolution crystal structure of bovine spleen purine nucleoside phosphorylase in complex forms with phosphate and 9-deazainosine."
    Pugmire M.J., Mao C., Ealick S.E.
    Submitted (MAR-1998) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS).
    Tissue: Spleen.

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: July 22, 2015
This is version 120 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

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.