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Q5JJB8 (PNPH_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 57. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Probable 6-oxopurine nucleoside phosphorylase

EC=2.4.2.1
Alternative name(s):
Purine nucleoside phosphorylase
Short name=PNP
Gene names
Ordered Locus Names:TK1482
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length267 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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 By similarity. HAMAP-Rule MF_01963

Catalytic activity

Purine nucleoside + phosphate = purine + alpha-D-ribose 1-phosphate. HAMAP-Rule MF_01963

Pathway

Purine metabolism; purine nucleoside salvage. HAMAP-Rule MF_01963

Subunit structure

Homohexamer. Dimer of a homotrimer By similarity. HAMAP-Rule MF_01963

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 By similarity.

Sequence similarities

Belongs to the PNP/MTAP phosphorylase family. MTAP subfamily.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 267267Probable 6-oxopurine nucleoside phosphorylase HAMAP-Rule MF_01963
PRO_0000415087

Regions

Region50 – 512Phosphate binding By similarity
Region83 – 842Phosphate binding By similarity
Region212 – 2143Substrate binding By similarity

Sites

Binding site101Phosphate By similarity
Binding site1881Substrate; via amide nitrogen By similarity
Binding site1891Phosphate By similarity
Site1701Important for substrate specificity By similarity
Site2241Important for substrate specificity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5JJB8 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 2E1BA87711CB899B

FASTA26729,804
        10         20         30         40         50         60 
MPRIAIIGGS GVYDPALLTN IREETVETPY GTVKVKIGEY NGEEIVFLAR HGEGHSVPPH 

        70         80         90        100        110        120 
KINYRANIWA LYELGVERIL STSAVGSLNL DMKPGDFVIL DQLMDFTKTR HYTFYDGEES 

       130        140        150        160        170        180 
PHDRKFVAHV DFTEPYCPEL RKALMNAARE LGFTYHPMGT YACMEGPRFE TRAEIRALKI 

       190        200        210        220        230        240 
LGADVVGMTQ CPEAALAREL EMCYASVAIV TNYAAGISPN KLTHTEVVEL MAQKSNEIKL 

       250        260 
LLMKAIEYIP KERRCPCKDA LKGATGE 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD85671.1.
RefSeqYP_183895.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JJB8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ5JJB8. 1 interaction.
MINTMINT-8377038.
STRING69014.TK1482.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD85671; BAD85671; TK1482.
GeneID3234499.
KEGGtko:TK1482.

Phylogenomic databases

eggNOGCOG0005.
HOGENOMHOG000228987.
KOK00772.
OMACPELRKA.

Enzyme and pathway databases

BioCycTKOD69014:GH72-1509-MONOMER.
UniPathwayUPA00606.

Family and domain databases

Gene3D3.40.50.1580. 1 hit.
HAMAPMF_01963. MTAP.
InterProIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
IPR018099. Purine_phosphorylase-2_CS.
[Graphical view]
PANTHERPTHR11904. PTHR11904. 1 hit.
PfamPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMSSF53167. SSF53167. 1 hit.
TIGRFAMsTIGR01694. MTAP. 1 hit.
PROSITEPS01240. PNP_MTAP_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePNPH_THEKO
AccessionPrimary (citable) accession number: Q5JJB8
Entry history
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: February 15, 2005
Last modified: May 14, 2014
This is version 57 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

PATHWAY comments

Index of metabolic and biosynthesis pathways