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 28-NOV-2012, entry version 99. DE RecName: Full=Purine nucleoside phosphorylase; DE Short=PNP; DE EC=2.4.2.1; 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; OC Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia; OC Pecora; Bovidae; Bovinae; Bos. OX NCBI_TaxID=9913; RN [1] RP PROTEIN SEQUENCE, AND FUNCTION. RC TISSUE=Spleen; RX MEDLINE=95331377; 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 RT and crystal structure of its complex with an N(7)-acycloguanosine RT 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] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RC TISSUE=Spleen; RX MEDLINE=97173115; 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] 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 [6] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC TISSUE=Spleen; RX MEDLINE=98254498; 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 RT and substrate analogues."; RL Biochemistry 37:7135-7146(1998). RN [7] 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 -!- FUNCTION: The purine nucleoside phosphorylases catalyze the CC phosphorolytic breakdown of the N-glycosidic bond in the beta- CC (deoxy)ribonucleoside molecules, with the formation of the CC corresponding free purine bases and pentose-1-phosphate. CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity). CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. 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 IPI; IPI00717573; -. DR PIR; S66203; S66203. DR UniGene; Bt.65253; -. DR PDB; 1A9O; X-ray; 2.00 A; A=3-289. DR PDB; 1A9P; X-ray; 2.40 A; A=3-289. DR PDB; 1A9Q; X-ray; 2.00 A; A=3-282. DR PDB; 1A9R; X-ray; 2.00 A; A=3-282. DR PDB; 1A9S; X-ray; 2.00 A; A=3-289. DR PDB; 1A9T; X-ray; 2.00 A; A=1-284. DR PDB; 1B8N; X-ray; 2.00 A; A=3-284. DR PDB; 1B8O; X-ray; 1.50 A; A=3-284. DR PDB; 1FXU; X-ray; 2.20 A; A=3-289. DR PDB; 1LV8; X-ray; 2.30 A; A/B/C/D/E/F=3-289. DR PDB; 1LVU; X-ray; 2.05 A; A/B/C/D/E/F=3-289. DR PDB; 1PBN; X-ray; 2.00 A; A=1-289. DR PDB; 1V48; X-ray; 2.20 A; A=3-289. DR PDB; 1VFN; X-ray; 2.15 A; A=4-284. DR PDB; 2AI1; X-ray; 2.00 A; A=3-289. DR PDB; 2AI2; X-ray; 1.70 A; A=3-289. DR PDB; 2AI3; X-ray; 1.70 A; A=3-289. DR PDB; 2QPL; X-ray; 2.10 A; A=3-284. DR PDB; 3FUC; X-ray; 1.45 A; A/B/C=3-284. 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 ProteinModelPortal; P55859; -. DR SMR; P55859; 3-282. DR STRING; P55859; -. DR PRIDE; P55859; -. DR Ensembl; ENSBTAT00000016346; ENSBTAP00000016346; ENSBTAG00000012317. DR eggNOG; COG0005; -. DR GeneTree; ENSGT00550000074740; -. DR HOGENOM; HOG000045183; -. DR HOVERGEN; HBG002460; -. DR InParanoid; P55859; -. DR OMA; HAGMRCF; -. DR OrthoDB; EOG4CZBGH; -. DR BRENDA; 2.4.2.1; 908. DR UniPathway; UPA00606; -. DR BindingDB; P55859; -. DR ChEMBL; CHEMBL2935; -. DR EvolutionaryTrace; P55859; -. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:UniProtKB. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR001369; PNP/MTAP. 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 PANTHER; PTHR11904:SF9; PTHR11904:SF9; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR PIRSF; PIRSF000477; PurNPase; 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; Complete proteome; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 289 Purine nucleoside phosphorylase. FT /FTId=PRO_0000184535. FT MOD_RES 1 1 N-acetylmethionine (By similarity). FT MOD_RES 95 95 N6-acetyllysine (By similarity). FT CONFLICT 2 2 A -> Q (in Ref. 1; AA sequence). FT CONFLICT 25 25 P -> S (in Ref. 2; AAX46392). FT HELIX 7 20 FT STRAND 26 31 FT HELIX 36 41 FT STRAND 43 49 FT HELIX 50 52 FT STRAND 62 64 FT STRAND 67 73 FT STRAND 76 83 FT HELIX 87 89 FT HELIX 93 96 FT HELIX 98 106 FT STRAND 110 119 FT STRAND 129 137 FT HELIX 138 141 FT TURN 153 155 FT HELIX 168 181 FT STRAND 188 194 FT HELIX 203 211 FT STRAND 215 221 FT HELIX 222 230 FT STRAND 234 244 FT STRAND 248 250 FT HELIX 257 278 FT HELIX 279 281 FT STRAND 284 287 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 //