ID PNPH_BOVIN Reviewed; 289 AA. AC P55859; Q3ZBH6; Q58DQ2; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-FEB-2008, sequence version 3. DT 25-MAY-2022, entry version 151. DE RecName: Full=Purine nucleoside phosphorylase; DE Short=PNP; DE EC=2.4.2.1 {ECO:0000250|UniProtKB:P00491}; DE AltName: Full=Inosine phosphorylase; DE AltName: Full=Inosine-guanosine phosphorylase; GN Name=PNP; Synonyms=NP; OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae; OC Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE. RC TISSUE=Spleen; RX PubMed=7607309; DOI=10.1016/0014-5793(95)00540-p; RA Bzowska A., Luic M., Schroeder W., Shugar D., Saenger W., Koellner G.; RT "Calf spleen purine nucleoside phosphorylase: purification, sequence and RT crystal structure of its complex with an N(7)-acycloguanosine inhibitor."; RL FEBS Lett. 367:214-218(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=16305752; DOI=10.1186/1471-2164-6-166; RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L., RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.; RT "Characterization of 954 bovine full-CDS cDNA sequences."; RL BMC Genomics 6:166-166(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=Hereford; TISSUE=Uterus; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases. RN [4] {ECO:0007744|PDB:1VFN} RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 4-284 IN COMPLEX WITH RP HYPOXANTHINE. RC TISSUE=Spleen; RX PubMed=9020983; DOI=10.1006/jmbi.1996.0730; RA Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.; RT "Crystal structure of calf spleen purine nucleoside phosphorylase in a RT complex with hypoxanthine at 2.15-A resolution."; RL J. Mol. Biol. 265:202-216(1997). RN [5] {ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, ECO:0007744|PDB:1PBN} RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 1-282 IN COMPLEXES WITH THE RP SUBSTRATE ANALOGS 9-DEAZAINOSINE; INOSINE; HYPOXANTHINE AND PHOSPHATE. RC TISSUE=Spleen; RX PubMed=9585525; DOI=10.1021/bi9723919; RA Mao C., Cook W.J., Zhou M., Federov A.A., Almo S.C., Ealick S.E.; RT "Calf spleen purine nucleoside phosphorylase complexed with substrates and RT substrate analogues."; RL Biochemistry 37:7135-7146(1998). RN [6] {ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP} RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE. RC TISSUE=Spleen; RA Pugmire M.J., Mao C., Ealick S.E.; RT "The high resolution crystal structure of bovine spleen purine nucleoside RT phosphorylase in complex forms with phosphate and 9-deazainosine."; RL Submitted (MAR-1998) to the PDB data bank. 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:0000305}. 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; BT021545; AAX46392.1; -; mRNA. DR EMBL; BC103291; AAI03292.2; -; mRNA. DR PIR; S66203; S66203. DR PDB; 1A9O; X-ray; 2.00 A; A=1-289. DR PDB; 1A9P; X-ray; 2.40 A; A=1-289. DR PDB; 1A9Q; X-ray; 2.00 A; A=1-282. DR PDB; 1A9R; X-ray; 2.00 A; A=1-282. DR PDB; 1A9S; X-ray; 2.00 A; A=1-289. DR PDB; 1A9T; X-ray; 2.00 A; A=1-284. DR PDB; 1B8N; X-ray; 2.00 A; A=1-284. DR PDB; 1B8O; X-ray; 1.50 A; A=1-284. DR PDB; 1FXU; X-ray; 2.20 A; A=1-289. DR PDB; 1LV8; X-ray; 2.30 A; A/B/C/D/E/F=1-289. DR PDB; 1LVU; X-ray; 2.05 A; A/B/C/D/E/F=1-289. DR PDB; 1PBN; X-ray; 2.00 A; A=1-289. DR PDB; 1V48; X-ray; 2.20 A; A=1-289. DR PDB; 1VFN; X-ray; 2.15 A; A=4-284. DR PDB; 2AI1; X-ray; 2.00 A; A=1-289. DR PDB; 2AI2; X-ray; 1.70 A; A=1-289. DR PDB; 2AI3; X-ray; 1.70 A; A=1-289. DR PDB; 2QPL; X-ray; 2.10 A; A=3-284. DR PDB; 3FUC; X-ray; 1.45 A; A/B/C=1-284. DR PDB; 3PNP; X-ray; 1.60 A; A=1-289. DR PDB; 4PNP; X-ray; 1.80 A; A=1-289. DR PDBsum; 1A9O; -. DR PDBsum; 1A9P; -. DR PDBsum; 1A9Q; -. DR PDBsum; 1A9R; -. DR PDBsum; 1A9S; -. DR PDBsum; 1A9T; -. DR PDBsum; 1B8N; -. DR PDBsum; 1B8O; -. DR PDBsum; 1FXU; -. DR PDBsum; 1LV8; -. DR PDBsum; 1LVU; -. DR PDBsum; 1PBN; -. DR PDBsum; 1V48; -. DR PDBsum; 1VFN; -. DR PDBsum; 2AI1; -. DR PDBsum; 2AI2; -. DR PDBsum; 2AI3; -. DR PDBsum; 2QPL; -. DR PDBsum; 3FUC; -. DR PDBsum; 3PNP; -. DR PDBsum; 4PNP; -. DR AlphaFoldDB; P55859; -. DR SMR; P55859; -. DR STRING; 9913.ENSBTAP00000016346; -. DR BindingDB; P55859; -. DR ChEMBL; CHEMBL2935; -. DR DrugCentral; P55859; -. DR PaxDb; P55859; -. DR PeptideAtlas; P55859; -. DR PRIDE; P55859; -. DR eggNOG; KOG3984; Eukaryota. DR HOGENOM; CLU_054456_1_2_1; -. DR InParanoid; P55859; -. DR TreeFam; TF300049; -. DR BRENDA; 2.4.2.1; 908. DR SABIO-RK; P55859; -. DR UniPathway; UPA00606; -. DR EvolutionaryTrace; P55859; -. DR Proteomes; UP000009136; Unplaced. DR Bgee; ENSBTAG00000012317; Expressed in bone marrow and 98 other tissues. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:RHEA. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. 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 3D-structure; Acetylation; Cytoplasm; Direct protein sequencing; KW Glycosyltransferase; Phosphoprotein; Purine salvage; Reference proteome; KW Transferase. FT CHAIN 1..289 FT /note="Purine nucleoside phosphorylase" FT /id="PRO_0000184535" FT REGION 84..86 FT /note="Phosphate binding" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP" FT BINDING 33 FT /note="Phosphate" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP" FT BINDING 64 FT /note="Phosphate" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9T, FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP" FT BINDING 88 FT /note="Purine nucleoside" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, FT ECO:0007744|PDB:1A9T" FT BINDING 116 FT /note="Phosphate; via amide nitrogen" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP" FT BINDING 201 FT /note="Purine nucleoside" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0000305|PubMed:9020983, ECO:0007744|PDB:1A9P, FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, FT ECO:0007744|PDB:1VFN" FT BINDING 219 FT /note="Purine nucleoside" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, FT ECO:0007744|PDB:1A9T" FT BINDING 220 FT /note="Phosphate" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9O, ECO:0007744|PDB:1A9P, FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, FT ECO:0007744|PDB:1A9S, ECO:0007744|PDB:1A9T, FT ECO:0007744|PDB:3PNP, ECO:0007744|PDB:4PNP" FT BINDING 243 FT /note="Purine nucleoside" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0000305|PubMed:9020983, ECO:0007744|PDB:1A9P, FT ECO:0007744|PDB:1A9Q, ECO:0007744|PDB:1A9R, FT ECO:0007744|PDB:1VFN" FT BINDING 257 FT /note="Purine nucleoside" FT /evidence="ECO:0000269|PubMed:9585525, FT ECO:0007744|PDB:1A9P, ECO:0007744|PDB:1A9S, FT ECO:0007744|PDB:1A9T" 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" FT MOD_RES 251 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P00491" FT CONFLICT 2 FT /note="A -> Q (in Ref. 1; AA sequence)" FT /evidence="ECO:0000305" FT CONFLICT 25 FT /note="P -> S (in Ref. 2; AAX46392)" FT /evidence="ECO:0000305" FT HELIX 7..20 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 36..41 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 43..49 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 50..52 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 62..64 FT /evidence="ECO:0007829|PDB:1A9O" FT STRAND 67..73 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 76..83 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 87..89 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 93..96 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 98..106 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 110..119 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 129..137 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 138..141 FT /evidence="ECO:0007829|PDB:3FUC" FT TURN 153..155 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 168..181 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 188..194 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 203..211 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 215..221 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 222..230 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 234..244 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 248..250 FT /evidence="ECO:0007829|PDB:1A9O" FT HELIX 257..278 FT /evidence="ECO:0007829|PDB:3FUC" FT HELIX 279..281 FT /evidence="ECO:0007829|PDB:3FUC" FT STRAND 284..287 FT /evidence="ECO:0007829|PDB:1A9O" SQ SEQUENCE 289 AA; 32037 MW; 7ECF84CCA494DEED CRC64; MANGYTYEDY QDTAKWLLSH TEQRPQVAVI CGSGLGGLVN KLTQAQTFDY SEIPNFPEST VPGHAGRLVF GILNGRACVM MQGRFHMYEG YPFWKVTFPV RVFRLLGVET LVVTNAAGGL NPNFEVGDIM LIRDHINLPG FSGENPLRGP NEERFGVRFP AMSDAYDRDM RQKAHSTWKQ MGEQRELQEG TYVMLGGPNF ETVAECRLLR NLGADAVGMS TVPEVIVARH CGLRVFGFSL ITNKVIMDYE SQGKANHEEV LEAGKQAAQK LEQFVSLLMA SIPVSGHTG //