SubmitCancel

Skip Header

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

Q8IMU4

- PNPH_DROME

UniProt

Q8IMU4 - PNPH_DROME

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Purine nucleoside phosphorylase

Gene
CG31115
Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 3 out of 5 - Protein inferred from homologyi

Functioni

Purine nucleoside phosphorylase involved in purine salvage By similarity.UniRule annotation

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei186 – 1861Important for substrate specificity By similarity
Binding sitei204 – 2041Substrate; via amide nitrogen By similarity
Binding sitei205 – 2051Phosphate By similarity
Sitei241 – 2411Important 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

ReactomeiREACT_180809. Methionine salvage pathway.
SignaLinkiQ8IMU4.
UniPathwayiUPA00606.

Names & Taxonomyi

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

Organism-specific databases

FlyBaseiFBgn0051115. CG31115.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. nucleus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Purine nucleoside phosphorylaseUniRule annotationPRO_0000415088Add
BLAST

Expressioni

Gene expression databases

BgeeiQ8IMU4.

Interactioni

Subunit structurei

Homotrimer By similarity.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ8IMU4.
SMRiQ8IMU4. Positions 18-279.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni68 – 692Phosphate binding By similarity

Sequence similaritiesi

Phylogenomic databases

GeneTreeiENSGT00550000074874.
InParanoidiQ8IMU4.
OMAiCTPFGKP.
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

MEADLEVQSE LEKDTIPIKI GIIGEANLDK PIYLAERMEY AVCTPFGKPS    50
DVIIDGQIEG VNVCLLSRNG RNHDIMPSNI NYRANVWAMR KMGCTHILVT 100
NTFSSLRDTF QPGHLVVPND VIDYTSRRAQ TFYDGAVGSP LGVCHVPMNP 150
TFCERTRQHL LSAAEELGFP TGSSGTVLTL EGPRYSTVAE NNMFRKWGAD 200
LLSMTLCPEA ILAKEAGIPY ASLGLVTNME CWCAKQPNAT THEIIYIFKK 250
QSENLQKVLI TAIRNMAAED WAEDILKAKI LVCSNFANSK 290
Length:290
Mass (Da):32,132
Last modified:March 3, 2009 - v2
Checksum:i04E88DFC26FF39B6
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
Links Updated
AE014297 Genomic DNA. Translation: AAN14032.2 .
RefSeqi NP_733068.2. NM_170189.3.
UniGenei Dm.16514.

3D structure databases

ProteinModelPortali Q8IMU4.
SMRi Q8IMU4. Positions 18-279.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblMetazoai FBtr0290053 ; FBpp0288492 ; FBgn0051115 .
GeneIDi 318597.
KEGGi dme:Dmel_CG31115.
UCSCi CG31115-RB. d. melanogaster.

Organism-specific databases

FlyBasei FBgn0051115. CG31115.

Phylogenomic databases

GeneTreei ENSGT00550000074874.
InParanoidi Q8IMU4.
OMAi CTPFGKP.
OrthoDBi EOG771270.
PhylomeDBi Q8IMU4.

Enzyme and pathway databases

UniPathwayi UPA00606 .
Reactomei REACT_180809. Methionine salvage pathway.
SignaLinki Q8IMU4.

Miscellaneous databases

GenomeRNAii 318597.
NextBioi 845587.

Gene expression databases

Bgeei Q8IMU4.

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.
[Graphical view ]
PANTHERi PTHR11904. PTHR11904. 1 hit.
Pfami PF01048. PNP_UDP_1. 1 hit.
[Graphical view ]
SUPFAMi SSF53167. SSF53167. 1 hit.
ProtoNeti Search...

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: September 3, 2014
This is version 76 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 By similarity.

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