PNPH_RAT
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 03-AUG-2022, entry version 86.
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}.
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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 iPTMnet; P85973; -.
DR PhosphoSitePlus; P85973; -.
DR World-2DPAGE; 0004:P85973; -.
DR jPOST; P85973; -.
DR PaxDb; P85973; -.
DR PRIDE; P85973; -.
DR Ensembl; ENSRNOT00000013582; ENSRNOP00000013582; ENSRNOG00000009982.
DR GeneID; 290029; -.
DR UCSC; RGD:1597189; rat.
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; 1078969at2759; -.
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 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 tissues.
DR Genevisible; P85973; RN.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0005576; C:extracellular region; IDA:RGD.
DR GO; GO:0005634; C:nucleus; 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:0042278; P:purine nucleoside metabolic process; IDA: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; -; 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 PANTHER; PTHR11904; PTHR11904; 1.
DR Pfam; PF01048; PNP_UDP_1; 1.
DR PIRSF; PIRSF000477; PurNPase; 1.
DR SUPFAM; SSF53167; SSF53167; 1.
DR TIGRFAMs; TIGR01700; PNPH; 1.
DR TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1.
DR PROSITE; PS01240; PNP_MTAP_2; 1.
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
