Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Purine nucleoside phosphorylase

Gene

CG31115

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Purine nucleoside phosphorylase involved in purine salvage.UniRule annotation

Catalytic activityi

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

Pathway:ipurine nucleoside salvage

This protein is involved in the pathway purine nucleoside salvage, which is part of Purine metabolism.UniRule annotation
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)LengthDescriptionGraphical viewFeature identifierActions
Sitei186 – 1861Important for substrate specificityUniRule annotation
Binding sitei204 – 2041Substrate; via amide nitrogenUniRule annotation
Binding sitei205 – 2051PhosphateUniRule annotation
Sitei241 – 2411Important for substrate specificityUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Glycosyltransferase, Transferase

Keywords - Biological processi

Purine salvage

Enzyme and pathway databases

ReactomeiREACT_335690. Methionine salvage pathway.
SignaLinkiQ8IMU4.
UniPathwayiUPA00606.

Names & Taxonomyi

Protein namesi
Recommended name:
Purine nucleoside phosphorylaseUniRule annotation (EC:2.4.2.1UniRule annotation)
Short name:
PNPUniRule annotation
Gene namesi
ORF Names:CG31115
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0051115. CG31115.

Subcellular locationi

  • Cytoplasm UniRule annotation
  • Nucleus UniRule annotation

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Purine nucleoside phosphorylasePRO_0000415088Add
BLAST

Expressioni

Gene expression databases

BgeeiQ8IMU4.
ExpressionAtlasiQ8IMU4. differential.
GenevisibleiQ8IMU4. DM.

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Protein-protein interaction databases

STRINGi7227.FBpp0288492.

Structurei

3D structure databases

ProteinModelPortaliQ8IMU4.
SMRiQ8IMU4. Positions 18-279.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 692Phosphate bindingUniRule annotation

Sequence similaritiesi

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

Phylogenomic databases

GeneTreeiENSGT00550000074874.
InParanoidiQ8IMU4.
OMAiMEGPRFE.
OrthoDBiEOG771270.
PhylomeDBiQ8IMU4.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.

Sequencei

Sequence statusi: Complete.

Q8IMU4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEADLEVQSE LEKDTIPIKI GIIGEANLDK PIYLAERMEY AVCTPFGKPS
60 70 80 90 100
DVIIDGQIEG VNVCLLSRNG RNHDIMPSNI NYRANVWAMR KMGCTHILVT
110 120 130 140 150
NTFSSLRDTF QPGHLVVPND VIDYTSRRAQ TFYDGAVGSP LGVCHVPMNP
160 170 180 190 200
TFCERTRQHL LSAAEELGFP TGSSGTVLTL EGPRYSTVAE NNMFRKWGAD
210 220 230 240 250
LLSMTLCPEA ILAKEAGIPY ASLGLVTNME CWCAKQPNAT THEIIYIFKK
260 270 280 290
QSENLQKVLI TAIRNMAAED WAEDILKAKI LVCSNFANSK
Length:290
Mass (Da):32,132
Last modified:March 3, 2009 - v2
Checksum:i04E88DFC26FF39B6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAN14032.2.
RefSeqiNP_733068.2. NM_170189.3.
UniGeneiDm.16514.

Genome annotation databases

EnsemblMetazoaiFBtr0290053; FBpp0288492; FBgn0051115.
GeneIDi318597.
KEGGidme:Dmel_CG31115.
UCSCiCG31115-RB. d. melanogaster.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE014297 Genomic DNA. Translation: AAN14032.2.
RefSeqiNP_733068.2. NM_170189.3.
UniGeneiDm.16514.

3D structure databases

ProteinModelPortaliQ8IMU4.
SMRiQ8IMU4. Positions 18-279.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0288492.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0290053; FBpp0288492; FBgn0051115.
GeneIDi318597.
KEGGidme:Dmel_CG31115.
UCSCiCG31115-RB. d. melanogaster.

Organism-specific databases

FlyBaseiFBgn0051115. CG31115.

Phylogenomic databases

GeneTreeiENSGT00550000074874.
InParanoidiQ8IMU4.
OMAiMEGPRFE.
OrthoDBiEOG771270.
PhylomeDBiQ8IMU4.

Enzyme and pathway databases

UniPathwayiUPA00606.
ReactomeiREACT_335690. Methionine salvage pathway.
SignaLinkiQ8IMU4.

Miscellaneous databases

GenomeRNAii318597.
NextBioi845587.
PROiQ8IMU4.

Gene expression databases

BgeeiQ8IMU4.
ExpressionAtlasiQ8IMU4. differential.
GenevisibleiQ8IMU4. DM.

Family and domain databases

Gene3Di3.40.50.1580. 1 hit.
HAMAPiMF_01963. MTAP.
InterProiIPR010044. MTAP.
IPR000845. Nucleoside_phosphorylase_d.
IPR001369. PNP/MTAP.
[Graphical view]
PANTHERiPTHR11904. PTHR11904. 1 hit.
PfamiPF01048. PNP_UDP_1. 1 hit.
[Graphical view]
SUPFAMiSSF53167. SSF53167. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  2. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.

Entry informationi

Entry nameiPNPH_DROME
AccessioniPrimary (citable) accession number: Q8IMU4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 25, 2012
Last sequence update: March 3, 2009
Last modified: June 24, 2015
This is version 83 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Although this enzyme belongs to the family of MTA phosphorylases based on sequence homology, it lacks several conserved amino acids in the substrate binding pocket that confer specificity towards MTA.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  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.