ID PUNA_CELSP STANDARD; PRT; 282 AA. AC P81989; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2000, sequence version 1. DT 07-FEB-2006, entry version 35. DE Purine nucleoside phosphorylase (EC 2.4.2.1) (Inosine phosphorylase) DE (PNP). GN Name=punA; OS Cellulomonas sp. OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Micrococcineae; Cellulomonadaceae; Cellulomonas. OX NCBI_TaxID=40001; RN [1] RP PROTEIN SEQUENCE, AND X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=20069945; PubMed=10600382; DOI=10.1006/jmbi.1999.3327; RA Tebbe J., Bzowska A., Wielgus-Kutrowska B., Schroeder W., RA Kazimierczuk Z., Shugar D., Saenger W., Koellner G.; RT "Crystal structure of the purine nucleoside phosphorylase (PNP) from RT Cellulomonas sp. and its implication for the mechanism of trimeric RT PNPs."; RL J. Mol. Biol. 294:1239-1255(1999). CC -!- FUNCTION: Cleavage of guanosine or inosine to respective bases and CC sugar-1-phosphate molecules. CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. CC -!- PATHWAY: Purine nucleoside salvage. CC -!- SUBUNIT: Homotrimer. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR PDB; 1C3X; X-ray; A/B/C=9-282. DR PDB; 1QE5; X-ray; A/B/C=9-282. DR InterPro; IPR001369; Mtap_PNP. DR InterPro; IPR011268; PNPHPUNA_XAPA. DR InterPro; IPR011269; PUNP. DR PANTHER; PTHR11904; Mtap_PNP; 1. DR Pfam; PF00896; Mtap_PNP; 1. DR PIRSF; PIRSF000477; PurNPase; 1. DR TIGRFAMs; TIGR01697; PNPH-PUNA-XAPA; 1. DR TIGRFAMs; TIGR01698; PUNP; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. KW 3D-structure; Direct protein sequencing; Glycosyltransferase; KW Transferase. FT CHAIN 1 282 Purine nucleoside phosphorylase. FT /FTId=PRO_0000184541. FT COMPBIAS 1 4 Poly-Thr. FT ACT_SITE 204 204 Potential. FT TURN 11 12 FT STRAND 13 13 FT TURN 14 15 FT STRAND 16 16 FT HELIX 18 33 FT STRAND 36 36 FT STRAND 39 43 FT TURN 46 47 FT TURN 49 54 FT STRAND 55 55 FT STRAND 57 63 FT HELIX 64 66 FT STRAND 67 67 FT TURN 68 69 FT STRAND 81 88 FT TURN 90 91 FT STRAND 92 92 FT STRAND 94 99 FT STRAND 102 102 FT HELIX 106 108 FT STRAND 109 110 FT HELIX 112 115 FT STRAND 116 116 FT HELIX 117 124 FT TURN 125 126 FT STRAND 129 138 FT TURN 141 142 FT STRAND 143 143 FT TURN 145 146 FT STRAND 148 156 FT STRAND 158 159 FT STRAND 162 162 FT STRAND 165 166 FT TURN 172 173 FT STRAND 174 175 FT HELIX 177 186 FT TURN 188 189 FT STRAND 192 197 FT STRAND 201 202 FT HELIX 206 215 FT TURN 216 216 FT STRAND 218 224 FT HELIX 225 233 FT TURN 234 235 FT STRAND 237 247 FT TURN 249 251 FT STRAND 253 254 FT HELIX 258 280 FT TURN 281 281 SQ SEQUENCE 282 AA; 29021 MW; 65F468DACC43D360 CRC64; TTTTPPSTPP LDDPATDPFL VARAAADHIA QATGVEGHDM ALVLGSGWGG AAELLGEVVA EVPTHEIPGF SAPAVAGHLS VTRSIRVERA DGSVRHALVL GSRTHLYEGK GVRAVVHGVR TAAATGAETL ILTNGCGGLN QEWGAGTPVL LSDHINLTAR SPLEGPTFVD LTDVYSPRLR ELAHRVDPTL PEGVYAQFPG PHYETPAEVR MAGILGADLV GMSTTLEAIA ARHCGLEVLG VSLVTNLAAG ISPTPLSHAE VIEAGQAAGP RISALLADIA KR //