ID   PNPH_DROPS              Reviewed;         288 AA.
AC   Q297F5;
DT   25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 2.
DT   03-AUG-2022, entry version 76.
DE   RecName: Full=Purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_03155};
DE            Short=PNP {ECO:0000255|HAMAP-Rule:MF_03155};
DE            EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_03155};
GN   ORFNames=GA16019;
OS   Drosophila pseudoobscura pseudoobscura (Fruit fly).
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC   Drosophilidae; Drosophila; Sophophora.
OX   NCBI_TaxID=46245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MV2-25 / Tucson 14011-0121.94;
RX   PubMed=15632085; DOI=10.1101/gr.3059305;
RA   Richards S., Liu Y., Bettencourt B.R., Hradecky P., Letovsky S.,
RA   Nielsen R., Thornton K., Hubisz M.J., Chen R., Meisel R.P., Couronne O.,
RA   Hua S., Smith M.A., Zhang P., Liu J., Bussemaker H.J., van Batenburg M.F.,
RA   Howells S.L., Scherer S.E., Sodergren E., Matthews B.B., Crosby M.A.,
RA   Schroeder A.J., Ortiz-Barrientos D., Rives C.M., Metzker M.L., Muzny D.M.,
RA   Scott G., Steffen D., Wheeler D.A., Worley K.C., Havlak P., Durbin K.J.,
RA   Egan A., Gill R., Hume J., Morgan M.B., Miner G., Hamilton C., Huang Y.,
RA   Waldron L., Verduzco D., Clerc-Blankenburg K.P., Dubchak I., Noor M.A.F.,
RA   Anderson W., White K.P., Clark A.G., Schaeffer S.W., Gelbart W.M.,
RA   Weinstock G.M., Gibbs R.A.;
RT   "Comparative genome sequencing of Drosophila pseudoobscura: chromosomal,
RT   gene, and cis-element evolution.";
RL   Genome Res. 15:1-18(2005).
CC   -!- FUNCTION: Purine nucleoside phosphorylase involved in purine salvage.
CC       {ECO:0000255|HAMAP-Rule:MF_03155}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase +
CC         alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_03155};
CC   -!- PATHWAY: Purine metabolism; purine nucleoside salvage.
CC       {ECO:0000255|HAMAP-Rule:MF_03155}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_03155}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_03155}.
CC       Nucleus {ECO:0000255|HAMAP-Rule:MF_03155}.
CC   -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA
CC       phosphorylases based on sequence homology, it lacks several conserved
CC       amino acids in the substrate binding pocket that confer specificity
CC       towards MTA. {ECO:0000255|HAMAP-Rule:MF_03155}.
CC   -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_03155}.
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DR   EMBL; CM000070; EAL28250.2; -; Genomic_DNA.
DR   RefSeq; XP_001359107.2; XM_001359070.3.
DR   AlphaFoldDB; Q297F5; -.
DR   SMR; Q297F5; -.
DR   STRING; 7237.FBpp0281762; -.
DR   EnsemblMetazoa; FBtr0283324; FBpp0281762; FBgn0076035.
DR   GeneID; 4802126; -.
DR   KEGG; dpo:Dpse_GA16019; -.
DR   eggNOG; KOG3985; Eukaryota.
DR   HOGENOM; CLU_054456_0_0_1; -.
DR   InParanoid; Q297F5; -.
DR   OMA; CTPFGKP; -.
DR   UniPathway; UPA00606; -.
DR   Proteomes; UP000001819; Chromosome 2.
DR   Bgee; FBgn0076035; Expressed in male reproductive system and 2 other tissues.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IEA:InterPro.
DR   GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-UniRule.
DR   CDD; cd09010; MTAP_SsMTAPII_like_MTIP; 1.
DR   Gene3D; 3.40.50.1580; -; 1.
DR   HAMAP; MF_01963; MTAP; 1.
DR   InterPro; IPR010044; MTAP.
DR   InterPro; IPR000845; Nucleoside_phosphorylase_d.
DR   InterPro; IPR035994; Nucleoside_phosphorylase_sf.
DR   PANTHER; PTHR42679; PTHR42679; 1.
DR   Pfam; PF01048; PNP_UDP_1; 1.
DR   SUPFAM; SSF53167; SSF53167; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Glycosyltransferase; Nucleus; Purine salvage;
KW   Reference proteome; Transferase.
FT   CHAIN           1..288
FT                   /note="Purine nucleoside phosphorylase"
FT                   /id="PRO_0000415089"
FT   BINDING         65..66
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         201
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   BINDING         202
FT                   /ligand="phosphate"
FT                   /ligand_id="ChEBI:CHEBI:43474"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            183
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
FT   SITE            238
FT                   /note="Important for substrate specificity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_03155"
SQ   SEQUENCE   288 AA;  32088 MW;  BF5C8F6883BC1B7A CRC64;
     MENNLAPINE DPFPIKIGII GDADLDTTIS LQDRMEYAVC TPFGKPSDII IEGLIDGVKC
     ALLCRNGRLH DIMPTNINYR ANIWAMRKLG CTHILVTHSL SSLREDIMPG DFVVPNDLID
     HTTRRAQTFY DGALGSPFGV CHLPMYPAFC ERTRQHLLNA AQELDLATHS KATVLTLEGP
     RYSTLAENNI YRKWGADLLS MTLSPEATLA KEAGILYASI GLVTNIECWC ANQPIATTHE
     IIYVFKNKVE KLQQVLSKAI ANISKEDWSE DILKAKILVC SNFANRNK