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P50389 (PNPH_SULSO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 97. 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):
5'-methylthioadenosine phosphorylase I
Short name=MTA phosphorylase I
Short name=MTAPI
Gene names
Ordered Locus Names:SSO2706
OrganismSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) [Reference proteome] [HAMAP]
Taxonomic identifier273057 [NCBI]
Taxonomic lineageArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus

Protein attributes

Sequence length236 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cleavage of guanosine or inosine to respective bases and sugar-1-phosphate molecules. Cleaves inosine, guanosine, and adenosine with a better efficiency than MTA. Ref.3 Ref.4

Catalytic activity

S-methyl-5'-thioadenosine + phosphate = adenine + S-methyl-5-thio-alpha-D-ribose 1-phosphate.

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

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

Pathway

Purine metabolism; purine nucleoside salvage.

Subunit structure

Homohexamer; disulfide-linked. Trimer of homodimers, with three symmetric intersubunit disulfide bonds linking the dimers to one another. Ref.3

Sequence similarities

Belongs to the PNP/UDP phosphorylase family.

Biophysicochemical properties

Kinetic parameters:

KM=154 µM for S-methyl-5'-thioadenosine Ref.4

KM=25.4 µM for adenosine

KM=84 µM for inosine

KM=113.6 µM for guanosine

Temperature dependence:

Optimum temperature is 120 degrees Celsius. Highly thermostable.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 236236Purine nucleoside phosphorylase
PRO_0000063195

Regions

Region86 – 894Phosphate binding
Region180 – 1823Substrate binding
Region204 – 2052Substrate binding

Sites

Binding site51Substrate; shared with dimeric partner
Binding site211Phosphate; via amide nitrogen
Binding site251Phosphate
Binding site431Phosphate; shared with dimeric partner
Binding site1631Substrate

Amino acid modifications

Disulfide bond125Interchain

Secondary structure

...................................... 236
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P50389 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: F1570ECE8AA3D51B

FASTA23625,738
        10         20         30         40         50         60 
MNPVHILAKK GEVAERVLVV GDPGRARLLS TLLQNPKLTN ENRGFLVYTG KYNGETVSIA 

        70         80         90        100        110        120 
THGIGGPSIA IVLEELAMLG ANVFIRYGTT GALVPYINLG EYIIVTGASY NQGGLFYQYL 

       130        140        150        160        170        180 
RDNACVASTP DFELTNKLVT SFSKRNLKYY VGNVFSSDAF YAEDEEFVKK WSSRGNIAVE 

       190        200        210        220        230 
MECATLFTLS KVKGWKSATV LVVSDNLAKG GIWITKEELE KSVMDGAKAV LDTLTS 

« Hide

References

« Hide 'large scale' references
[1]"Extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Gene cloning and amino acid sequence determination."
Cacciapuoti G., Porcelli M., Bertoldo C., Fusco S., De Rosa M., Zappia V.
Eur. J. Biochem. 239:632-637(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[2]"The complete genome of the crenarchaeon Sulfolobus solfataricus P2."
She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J., Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G., Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J., Medina N., Peng X. expand/collapse author list , Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C., Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T., Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.
Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
[3]"Purification and characterization of extremely thermophilic and thermostable 5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus. Purine nucleoside phosphorylase activity and evidence for intersubunit disulfide bonds."
Cacciapuoti G., Porcelli M., Bertoldo C., de Rosa M., Zappia V.
J. Biol. Chem. 269:24762-24769(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-26, FUNCTION, SUBUNIT.
[4]"A novel hyperthermostable 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Sulfolobus solfataricus."
Cacciapuoti G., Forte S., Moretti M.A., Brio A., Zappia V., Porcelli M.
FEBS J. 272:1886-1899(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.
[5]"Three-dimensional structure of a hyperthermophilic 5'-deoxy-5'-methylthioadenosine phosphorylase from Sulfolobus solfataricus."
Appleby T.C., Mathews I.I., Porcelli M., Cacciapuoti G., Ealick S.E.
J. Biol. Chem. 276:39232-39242(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH SUBSTRATES AND SUBSTRATE ANALOGS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z50181 Genomic DNA. Translation: CAA90560.1.
AE006641 Genomic DNA. Translation: AAK42818.1.
PIRS58291.
RefSeqNP_344028.1. NC_002754.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1JDSX-ray1.80A/B/C/D/E/F1-236[»]
1JDTX-ray2.00A/B/C1-236[»]
1JDUX-ray2.50A/B/C1-236[»]
1JDVX-ray2.00A/B/C/D/E/F1-236[»]
1JDZX-ray2.00A/B/C1-236[»]
1JE0X-ray1.60A/B/C1-236[»]
1JE1X-ray1.80A/B/C/D/E/F1-236[»]
1JP7X-ray1.80A/B/C1-236[»]
1JPVX-ray1.80A/B/C1-236[»]
ProteinModelPortalP50389.
SMRP50389. Positions 2-236.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273057.SSO2706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK42818; AAK42818; SSO2706.
GeneID1452737.
KEGGsso:SSO2706.

Phylogenomic databases

eggNOGCOG2820.
HOGENOMHOG000274897.
KOK00772.
OMAGEPDRAN.

Enzyme and pathway databases

BioCycSSOL273057:GCH2-2504-MONOMER.
BRENDA2.4.2.28. 6163.
UniPathwayUPA00606.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
InterProIPR018017. Nucleoside_phosphorylase.
IPR018016. Nucleoside_phosphorylase_CS.
IPR000845. Nucleoside_phosphorylase_d.
[Graphical view]
PANTHERPTHR21234. PTHR21234. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
PROSITEPS01232. PNP_UDP_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP50389.

Entry information

Entry namePNPH_SULSO
AccessionPrimary (citable) accession number: P50389
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 14, 2014
This is version 97 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