ID PNPH_RAT Reviewed; 289 AA. AC P85973; A6KEC5; DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 24-JAN-2024, entry version 93. DE RecName: Full=Purine nucleoside phosphorylase {ECO:0000250|UniProtKB:P00491}; DE Short=PNP {ECO:0000250|UniProtKB:P00491}; DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P00491}; DE AltName: Full=Inosine phosphorylase {ECO:0000250|UniProtKB:P00491}; DE AltName: Full=Inosine-guanosine phosphorylase; GN Name=Pnp; Synonyms=Np; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] {ECO:0000305} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY. RX PubMed=19343716; DOI=10.1002/pmic.200800664; RA Maurya D.K., Sundaram C.S., Bhargava P.; RT "Proteome profile of the mature rat olfactory bulb."; RL Proteomics 9:2593-2599(2009). CC -!- FUNCTION: Catalyzes the phosphorolytic breakdown of the N-glycosidic CC bond in the beta-(deoxy)ribonucleoside molecules, with the formation of CC the corresponding free purine bases and pentose-1-phosphate (By CC similarity). Preferentially acts on 6-oxopurine nucleosides including CC inosine and guanosine (By similarity). {ECO:0000250|UniProtKB:P00491}. CC -!- CATALYTIC ACTIVITY: CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; CC Evidence={ECO:0000250|UniProtKB:P00491}; CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine; CC Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; CC Evidence={ECO:0000250|UniProtKB:P00491}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyguanosine + phosphate = 2-deoxy-alpha-D-ribose 1- CC phosphate + guanine; Xref=Rhea:RHEA:27738, ChEBI:CHEBI:16235, CC ChEBI:CHEBI:17172, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1; CC Evidence={ECO:0000250|UniProtKB:P23492}; CC -!- CATALYTIC ACTIVITY: CC Reaction=2'-deoxyinosine + phosphate = 2-deoxy-alpha-D-ribose 1- CC phosphate + hypoxanthine; Xref=Rhea:RHEA:27750, ChEBI:CHEBI:17368, CC ChEBI:CHEBI:28997, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.1; CC Evidence={ECO:0000250|UniProtKB:P23492}; CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC {ECO:0000250|UniProtKB:P00491}. CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P00491}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P00491}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. CC {ECO:0000255}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CH474040; EDL88431.1; -; Genomic_DNA. DR RefSeq; XP_006251919.1; XM_006251857.3. DR AlphaFoldDB; P85973; -. DR SMR; P85973; -. DR STRING; 10116.ENSRNOP00000013582; -. DR BindingDB; P85973; -. DR ChEMBL; CHEMBL2395; -. DR GlyGen; P85973; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; P85973; -. DR PhosphoSitePlus; P85973; -. DR jPOST; P85973; -. DR PaxDb; 10116-ENSRNOP00000013582; -. DR Ensembl; ENSRNOT00000013582.7; ENSRNOP00000013582.6; ENSRNOG00000009982.7. DR Ensembl; ENSRNOT00055041821; ENSRNOP00055034060; ENSRNOG00055024319. DR Ensembl; ENSRNOT00060050985; ENSRNOP00060042413; ENSRNOG00060029318. DR Ensembl; ENSRNOT00065055615; ENSRNOP00065045781; ENSRNOG00065032290. DR UCSC; RGD:1597189; rat. DR AGR; RGD:1597189; -. DR CTD; 4860; -. DR RGD; 1597189; Pnp. DR eggNOG; KOG3984; Eukaryota. DR GeneTree; ENSGT00950000182991; -. DR HOGENOM; CLU_054456_1_2_1; -. DR InParanoid; P85973; -. DR OMA; EGVYAQF; -. DR OrthoDB; 5475828at2759; -. DR PhylomeDB; P85973; -. DR TreeFam; TF300049; -. DR BRENDA; 2.4.2.1; 5301. DR Reactome; R-RNO-6798695; Neutrophil degranulation. DR Reactome; R-RNO-74217; Purine salvage. DR Reactome; R-RNO-74259; Purine catabolism. DR Reactome; R-RNO-9755088; Ribavirin ADME. DR UniPathway; UPA00606; -. DR PRO; PR:P85973; -. DR Proteomes; UP000002494; Chromosome 15. DR Proteomes; UP000234681; Chromosome 15. DR Bgee; ENSRNOG00000009982; Expressed in lung and 19 other cell types or tissues. DR GO; GO:0005737; C:cytoplasm; ISO:RGD. DR GO; GO:0005829; C:cytosol; IEA:Ensembl. DR GO; GO:0005576; C:extracellular region; IDA:RGD. DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:RHEA. DR GO; GO:0042802; F:identical protein binding; ISO:RGD. DR GO; GO:0001882; F:nucleoside binding; ISO:RGD. DR GO; GO:0042301; F:phosphate ion binding; ISO:RGD. DR GO; GO:0002060; F:purine nucleobase binding; ISO:RGD. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:RGD. DR GO; GO:0000255; P:allantoin metabolic process; ISO:RGD. DR GO; GO:0046059; P:dAMP catabolic process; ISO:RGD. DR GO; GO:0006157; P:deoxyadenosine catabolic process; ISO:RGD. DR GO; GO:0006149; P:deoxyinosine catabolic process; ISO:RGD. DR GO; GO:0006955; P:immune response; ISO:RGD. DR GO; GO:0006204; P:IMP catabolic process; ISO:RGD. DR GO; GO:0006148; P:inosine catabolic process; ISO:RGD. DR GO; GO:0006738; P:nicotinamide riboside catabolic process; ISO:RGD. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; ISO:RGD. DR GO; GO:0009165; P:nucleotide biosynthetic process; ISO:RGD. DR GO; GO:0046638; P:positive regulation of alpha-beta T cell differentiation; ISO:RGD. DR GO; GO:0032743; P:positive regulation of interleukin-2 production; ISO:RGD. DR GO; GO:0042102; P:positive regulation of T cell proliferation; ISO:RGD. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. DR GO; GO:0043101; P:purine-containing compound salvage; ISO:RGD. DR GO; GO:0009410; P:response to xenobiotic stimulus; ISO:RGD. DR GO; GO:0034418; P:urate biosynthetic process; ISO:RGD. DR CDD; cd09009; PNP-EcPNPII_like; 1. DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR035994; Nucleoside_phosphorylase_sf. DR InterPro; IPR011270; Pur_Nuc_Pase_Ino/Guo-sp. DR InterPro; IPR011268; Purine_phosphorylase. DR InterPro; IPR018099; Purine_phosphorylase-2_CS. DR NCBIfam; TIGR01700; PNPH; 1. DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1. DR PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1. DR PANTHER; PTHR11904:SF12; PURINE NUCLEOSIDE PHOSPHORYLASE; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR PIRSF; PIRSF000477; PurNPase; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. DR World-2DPAGE; 0004:P85973; -. DR Genevisible; P85973; RN. PE 1: Evidence at protein level; KW Acetylation; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1..289 FT /note="Purine nucleoside phosphorylase" FT /id="PRO_0000349126" FT BINDING 33 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 64 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 84..86 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 88 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 116 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 201 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 219 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 220 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 243 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /evidence="ECO:0000250|UniProtKB:P55859" FT BINDING 257 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /evidence="ECO:0000250|UniProtKB:P55859" FT SITE 243 FT /note="Important for substrate specificity" FT /evidence="ECO:0000250|UniProtKB:P00491" FT MOD_RES 1 FT /note="N-acetylmethionine" FT /evidence="ECO:0000250|UniProtKB:P00491" SQ SEQUENCE 289 AA; 32302 MW; 004486E55848749B CRC64; MENEFTYEDY QRTAEWLRSH TKHRPQVAVI CGSGLGGLTA KLTQPQAFDY NEIPNFPQST VQGHAGRLVF GFLNGRSCVM MQGRFHMYEG YSLSKVTFPV RVFHLLGVDT LVVTNAAGGL NPKFEVGDIM LIRDHINLPG FCGQNPLRGP NDERFGVRFP AMSDAYDRDM RQKAFNAWKQ MGEQRELQEG TYIMSAGPTF ETVAESCLLR MLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVVMDYN NLEKASHQEV LEAGKAAAQK LEQFVSILME SIPPRERAN //