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Q8U2I1

- PNPH_PYRFU

UniProt

Q8U2I1 - PNPH_PYRFU

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Protein

Probable 6-oxopurine nucleoside phosphorylase

Gene
PF0853
Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Purine nucleoside phosphorylase which is highly specific for 6-oxopurine nucleosides. Cleaves guanosine or inosine to respective bases and sugar-1-phosphate molecules. Involved in purine salvage.2 Publications

Catalytic activityi

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

Kineticsi

  1. KM=322 µM for inosine
  2. KM=122 µM for guanosine
  3. KM=1454 µM for adenosine

pH dependencei

Optimum pH is 7.4. Active from pH 5 to 10.

Temperature dependencei

Optimum temperature is 120 degrees Celsius. Thermostable up to 133 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei10 – 101Phosphate By similarity
Sitei169 – 1691Important for substrate specificity By similarity
Binding sitei187 – 1871Substrate; via amide nitrogen By similarity
Binding sitei188 – 1881Phosphate By similarity
Sitei223 – 2231Important for substrate specificity By similarity

GO - Molecular functioni

  1. phosphorylase activity Source: InterPro
  2. purine-nucleoside phosphorylase activity Source: UniProtKB-EC
  3. S-methyl-5-thioadenosine phosphorylase activity Source: InterPro

GO - Biological processi

  1. purine ribonucleoside salvage Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

BRENDAi2.4.2.1. 321.
UniPathwayiUPA00606.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable 6-oxopurine nucleoside phosphorylase (EC:2.4.2.1)
Alternative name(s):
Purine nucleoside phosphorylase
Short name:
PNP
Short name:
PfPNP
Gene namesi
Ordered Locus Names:PF0853
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
ProteomesiUP000001013: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi169 – 1691E → S: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with D-211, D-213 and A-223. 1 Publication
Mutagenesisi211 – 2111N → D: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with S-169, D-213 and A-223. 1 Publication
Mutagenesisi213 – 2131A → D: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with S-169, D-211 and A-223. 1 Publication
Mutagenesisi223 – 2231H → A: Decreases catalytic activity for insosine and allows the enzyme to phosphorolytically cleave MTA with a catalytic efficiency about 4-fold higher than for inosine; when associated with S-169, D-211, and D-213. 1 Publication
Mutagenesisi254 – 2541C → S: Fully active, but reduces thermodynamic and kinetic stability of the enzyme; when associated with S-256.
Mutagenesisi256 – 2561C → S: Fully active, but reduces thermodynamic and kinetic stability of the enzyme; when associated with S-254.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedUniRule annotation
Chaini2 – 265264Probable 6-oxopurine nucleoside phosphorylaseUniRule annotationPRO_0000415086Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi136 ↔ 2021 Publication
Disulfide bondi162 ↔ 1901 Publication
Disulfide bondi254 ↔ 2561 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiQ8U2I1.

Interactioni

Subunit structurei

Homohexamer. Dimer of a homotrimer.1 Publication

Protein-protein interaction databases

STRINGi186497.PF0853.

Structurei

3D structure databases

ProteinModelPortaliQ8U2I1.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni49 – 502Phosphate binding By similarity
Regioni82 – 832Phosphate binding By similarity
Regioni211 – 2133Substrate binding By similarity

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0005.
HOGENOMiHOG000228987.
KOiK00772.
OMAiCTPFGKP.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
TIGRFAMsiTIGR01694. MTAP. 1 hit.
PROSITEiPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q8U2I1-1 [UniParc]FASTAAdd to Basket

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MPRIAIVGGS GVYDFPAENK REETVKTPYG EVKITVGVVG DEEVAFLARH    50
GKGHSIPPHK INYRANIWAL YELGVERIIA TSAVGSMNPE MKPGDFVILD 100
QIIDFTVSRP RTFYDGEESP HERKFVAHVD FTEPYCPEIR KALITAARNL 150
GLPYHPRGTY VCTEGPRFET AAEIRAYRIL GGDVVGMTQC PEAILARELE 200
MCYATVAIVT NYAAGMSGKK LTHSEVVELM QKKSEDIVKL ILAAIPLIPK 250
ERRCGCKDAL KGATG 265
Length:265
Mass (Da):29,208
Last modified:June 1, 2002 - v1
Checksum:i19BF1EBBB2FEDBB8
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL80977.1.
RefSeqiNP_578582.1. NC_003413.1.
WP_011011984.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL80977; AAL80977; PF0853.
GeneIDi1468711.
KEGGipfu:PF0853.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE009950 Genomic DNA. Translation: AAL80977.1 .
RefSeqi NP_578582.1. NC_003413.1.
WP_011011984.1. NC_003413.1.

3D structure databases

ProteinModelPortali Q8U2I1.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 186497.PF0853.

Proteomic databases

PRIDEi Q8U2I1.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAL80977 ; AAL80977 ; PF0853 .
GeneIDi 1468711.
KEGGi pfu:PF0853.

Phylogenomic databases

eggNOGi COG0005.
HOGENOMi HOG000228987.
KOi K00772.
OMAi CTPFGKP.

Enzyme and pathway databases

UniPathwayi UPA00606 .
BRENDAi 2.4.2.1. 321.

Family and domain databases

Gene3Di 3.40.50.1580. 1 hit.
HAMAPi MF_01963. MTAP.
InterProi IPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
TIGRFAMsi TIGR01694. MTAP. 1 hit.
PROSITEi PS01240. PNP_MTAP_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Biochemical and structural characterization of mammalian-like purine nucleoside phosphorylase from the Archaeon Pyrococcus furiosus."
    Cacciapuoti G., Gorassini S., Mazzeo M.F., Siciliano R.A., Carbone V., Zappia V., Porcelli M.
    FEBS J. 274:2482-2495(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION, SUBUNIT, DISULFIDE BONDS.
  3. "Unraveling the structural and functional differences between purine nucleoside phosphorylase and 5'-deoxy-5'-methylthioadenosine phosphorylase from the archaeon Pyrococcus furiosus."
    Cacciapuoti G., Marabotti A., Fuccio F., Porcelli M.
    Biochim. Biophys. Acta 1814:1358-1366(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, MUTAGENESIS OF GLU-169; ASN-211; ALA-213 AND HIS-223.

Entry informationi

Entry nameiPNPH_PYRFU
AccessioniPrimary (citable) accession number: Q8U2I1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: June 1, 2002
Last modified: September 3, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it has been shown that conserved amino acid substitutions in the substrate binding pocket convert the substrate specificity of this enzyme from 6-aminopurines to 6-oxopurines. It seems that P.furiosus has developed a specific enzyme (PF0853) for the metabolism of 6-oxo-purines, next to the canonical MTA phosphorylase PF0016.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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