ID PNPH_BOVIN STANDARD; PRT; 289 AA. AC P55859; DT 01-NOV-1997 (Rel. 35, Created) DT 15-JUL-1998 (Rel. 36, Last sequence update) DT 16-OCT-2001 (Rel. 40, Last annotation update) DE Purine nucleoside phosphorylase (EC 2.4.2.1) (Inosine phosphorylase) DE (PNP). GN NP OR PNP. OS Bos taurus (Bovine). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Cetartiodactyla; Ruminantia; Pecora; Bovoidea; OC Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP SEQUENCE. RC TISSUE=Spleen; RX MEDLINE=95331377; PubMed=7607309; RA Bzowska A., Luic M., Schroeder W., Shugar D., Saenger W., Koellner G.; RT "Calf spleen purine nucleoside phosphorylase: purification, sequence RT and crystal structure of its complex with an N(7)-acycloguanosine RT inhibitor."; RL FEBS Lett. 367:214-218(1995). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RC TISSUE=Spleen; RX MEDLINE=97173115; PubMed=9020983; RA Koellner G., Luic M., Shugar D., Saenger W., Bzowska A.; RT "Crystal structure of calf spleen purine nucleoside phosphorylase in RT a complex with hypoxanthine at 2.15-A resolution."; RL J. Mol. Biol. 265:202-216(1997). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RA Mao C., Zhou M., Ealick S., Federov A.A., Almo S.C.; RL Submitted (JUL-1995) to the PDB data bank. RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC TISSUE=Spleen; RX MEDLINE=98254498; PubMed=9585525; 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 RT substrates and substrate analogues."; RL Biochemistry 37:7135-7146(1998). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RC TISSUE=Spleen; RA Pugmire M.J., Mao C., Ealick S.E.; RT "The high resolution crystal structure of bovine spleen purine RT nucleoside phosphorylase in complex forms with phosphate and 9- RT deazainosine."; RL Submitted (MAR-1998) to the PDB data bank. CC -!- CATALYTIC ACTIVITY: PURINE NUCLEOSIDE + ORTHOPHOSPHATE = PURINE + CC ALPHA-D-RIBOSE 1-PHOSPHATE. CC -!- SUBUNIT: HOMOTRIMER. CC -!- SIMILARITY: BELONGS TO THE PNP/MTAP FAMILY 2 OF PHOSPHORYLASES. 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 PDB; 1VFN; 12-NOV-97. DR PDB; 1PBN; 14-NOV-95. DR PDB; 1A9O; 15-JUL-98. DR PDB; 1A9P; 15-JUL-98. DR PDB; 1A9Q; 15-JUL-98. DR PDB; 1A9R; 15-JUL-98. DR PDB; 1A9S; 15-JUL-98. DR PDB; 1A9T; 17-JUN-98. DR PDB; 1B8N; 16-FEB-99. DR PDB; 1B8O; 16-FEB-99. DR PDB; 3PNP; 30-MAR-99. DR PDB; 4PNP; 30-MAR-99. DR InterPro; IPR001369; Mtap_PNP. DR Pfam; PF00896; Mtap_PNP; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. KW Transferase; Glycosyltransferase; 3D-structure. SQ SEQUENCE 289 AA; 32093 MW; 62D243C3016E8EE9 CRC64; MQNGYTYEDY 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 //