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 05-DEC-2018, entry version 137. 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 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) 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] 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 (2.00 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 RT and substrate analogues."; RL Biochemistry 37:7135-7146(1998). RN [7] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE AND RP 9-DEAZAINOSINE. 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 {ECO:0000269|PubMed:7607309}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a purine D-ribonucleoside + phosphate = a purine CC nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, CC ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, CC ChEBI:CHEBI:142355; EC=2.4.2.1; CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC -!- SUBUNIT: Homotrimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. 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 UniGene; Bt.65253; -. 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 ProteinModelPortal; P55859; -. DR SMR; P55859; -. DR STRING; 9913.ENSBTAP00000016346; -. DR BindingDB; P55859; -. DR ChEMBL; CHEMBL2935; -. DR PaxDb; P55859; -. DR PeptideAtlas; P55859; -. DR PRIDE; P55859; -. DR Ensembl; ENSBTAT00000016346; ENSBTAP00000016346; ENSBTAG00000012317. DR eggNOG; KOG3984; Eukaryota. DR eggNOG; COG0005; LUCA. DR GeneTree; ENSGT00550000074740; -. DR HOGENOM; HOG000045183; -. DR HOVERGEN; HBG002460; -. DR InParanoid; P55859; -. DR OMA; VLISDHI; -. DR OrthoDB; EOG091G0GEE; -. DR TreeFam; TF300049; -. DR BRENDA; 2.4.2.1; 908. DR Reactome; R-BTA-6798695; Neutrophil degranulation. DR Reactome; R-BTA-74217; Purine salvage. DR Reactome; R-BTA-74259; Purine catabolism. DR SABIO-RK; P55859; -. DR UniPathway; UPA00606; -. DR EvolutionaryTrace; P55859; -. DR Proteomes; UP000009136; Chromosome 10. DR Bgee; ENSBTAG00000012317; Expressed in 9 organ(s), highest expression level in lung. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. 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; 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; Complete proteome; Cytoplasm; Cytoskeleton; KW Direct protein sequencing; Glycosyltransferase; Phosphoprotein; KW Reference proteome; Transferase. FT CHAIN 1 289 Purine nucleoside phosphorylase. FT /FTId=PRO_0000184535. FT REGION 84 86 Phosphate binding. FT {ECO:0000269|PubMed:9585525}. FT BINDING 33 33 Phosphate. {ECO:0000269|PubMed:9585525}. FT BINDING 64 64 Phosphate. {ECO:0000269|PubMed:9585525}. FT BINDING 116 116 Phosphate; via amide nitrogen. FT {ECO:0000269|PubMed:9585525}. FT BINDING 201 201 Purine nucleoside. FT {ECO:0000269|PubMed:9585525}. FT BINDING 220 220 Phosphate. {ECO:0000269|PubMed:9585525}. FT BINDING 243 243 Purine nucleoside. FT {ECO:0000269|PubMed:9585525}. FT MOD_RES 1 1 N-acetylmethionine. FT {ECO:0000250|UniProtKB:P00491}. FT MOD_RES 251 251 Phosphoserine. FT {ECO:0000250|UniProtKB:P00491}. FT CONFLICT 2 2 A -> Q (in Ref. 1; AA sequence). FT {ECO:0000305}. FT CONFLICT 25 25 P -> S (in Ref. 2; AAX46392). FT {ECO:0000305}. FT HELIX 7 20 {ECO:0000244|PDB:3FUC}. FT STRAND 26 31 {ECO:0000244|PDB:3FUC}. FT HELIX 36 41 {ECO:0000244|PDB:3FUC}. FT STRAND 43 49 {ECO:0000244|PDB:3FUC}. FT HELIX 50 52 {ECO:0000244|PDB:3FUC}. FT STRAND 62 64 {ECO:0000244|PDB:1A9O}. FT STRAND 67 73 {ECO:0000244|PDB:3FUC}. FT STRAND 76 83 {ECO:0000244|PDB:3FUC}. FT HELIX 87 89 {ECO:0000244|PDB:3FUC}. FT HELIX 93 96 {ECO:0000244|PDB:3FUC}. FT HELIX 98 106 {ECO:0000244|PDB:3FUC}. FT STRAND 110 119 {ECO:0000244|PDB:3FUC}. FT STRAND 129 137 {ECO:0000244|PDB:3FUC}. FT HELIX 138 141 {ECO:0000244|PDB:3FUC}. FT TURN 153 155 {ECO:0000244|PDB:3FUC}. FT HELIX 168 181 {ECO:0000244|PDB:3FUC}. FT STRAND 188 194 {ECO:0000244|PDB:3FUC}. FT HELIX 203 211 {ECO:0000244|PDB:3FUC}. FT STRAND 215 221 {ECO:0000244|PDB:3FUC}. FT HELIX 222 230 {ECO:0000244|PDB:3FUC}. FT STRAND 234 244 {ECO:0000244|PDB:3FUC}. FT STRAND 248 250 {ECO:0000244|PDB:1A9O}. FT HELIX 257 278 {ECO:0000244|PDB:3FUC}. FT HELIX 279 281 {ECO:0000244|PDB:3FUC}. FT STRAND 284 287 {ECO:0000244|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 //