ID PUNA_CELSP Reviewed; 282 AA. AC P81989; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2000, sequence version 1. DT 27-MAR-2024, entry version 95. DE RecName: Full=Purine nucleoside phosphorylase; DE Short=PNP; DE Short=Pu-NPase; DE EC=2.4.2.1; DE AltName: Full=Inosine phosphorylase; DE AltName: Full=Inosine-guanosine phosphorylase; GN Name=punA; OS Cellulomonas sp. OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae; OC Cellulomonas. OX NCBI_TaxID=40001; RN [1] RP PROTEIN SEQUENCE, X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, RP CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=10600382; DOI=10.1006/jmbi.1999.3327; RA Tebbe J., Bzowska A., Wielgus-Kutrowska B., Schroeder W., Kazimierczuk Z., RA 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 PNPs."; RL J. Mol. Biol. 294:1239-1255(1999). 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. Cleaves CC guanosine, inosine, 2'-deoxyguanosine and 2'-deoxyinosine. CC {ECO:0000269|PubMed:10600382}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a purine 2'-deoxy-D-ribonucleoside + phosphate = 2-deoxy- CC alpha-D-ribose 1-phosphate + a purine nucleobase; CC Xref=Rhea:RHEA:36431, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57259, ChEBI:CHEBI:142361; EC=2.4.2.1; CC Evidence={ECO:0000269|PubMed:10600382}; CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:10600382}. 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 PDB; 1C3X; X-ray; 2.40 A; A/B/C=9-282. DR PDB; 1QE5; X-ray; 2.20 A; A/B/C=9-282. DR PDBsum; 1C3X; -. DR PDBsum; 1QE5; -. DR AlphaFoldDB; P81989; -. DR SMR; P81989; -. DR DrugBank; DB02985; 8-iodo-guanine. DR BRENDA; 2.4.2.1; 1235. DR UniPathway; UPA00606; -. DR EvolutionaryTrace; P81989; -. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR CDD; cd09009; PNP-EcPNPII_like; 1. DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR035994; Nucleoside_phosphorylase_sf. DR InterPro; IPR011269; PUNP. DR InterPro; IPR011268; Purine_phosphorylase. DR InterPro; IPR018099; Purine_phosphorylase-2_CS. DR NCBIfam; TIGR01697; PNPH-PUNA-XAPA; 1. DR NCBIfam; TIGR01698; PUNP; 1. DR PANTHER; PTHR11904; METHYLTHIOADENOSINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1. DR PANTHER; PTHR11904:SF9; PURINE NUCLEOSIDE PHOSPHORYLASE-RELATED; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR PIRSF; PIRSF000477; PurNPase; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Direct protein sequencing; Glycosyltransferase; Transferase. FT CHAIN 1..282 FT /note="Purine nucleoside phosphorylase" FT /id="PRO_0000184541" FT ACT_SITE 204 FT /evidence="ECO:0000255" FT BINDING 46 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P9WP01" FT BINDING 78 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P45563" FT BINDING 103..105 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P45563" FT BINDING 204 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /evidence="ECO:0000250|UniProtKB:P45563" FT BINDING 223 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /evidence="ECO:0000250|UniProtKB:P45563" FT BINDING 246 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /evidence="ECO:0000250|UniProtKB:P45563" FT HELIX 18..33 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 39..43 FT /evidence="ECO:0007829|PDB:1QE5" FT TURN 49..54 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 57..63 FT /evidence="ECO:0007829|PDB:1QE5" FT HELIX 64..66 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 81..88 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 94..99 FT /evidence="ECO:0007829|PDB:1QE5" FT HELIX 106..108 FT /evidence="ECO:0007829|PDB:1QE5" FT HELIX 112..115 FT /evidence="ECO:0007829|PDB:1QE5" FT HELIX 117..124 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 129..138 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 148..156 FT /evidence="ECO:0007829|PDB:1QE5" FT HELIX 177..186 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 192..197 FT /evidence="ECO:0007829|PDB:1QE5" FT HELIX 206..215 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 218..224 FT /evidence="ECO:0007829|PDB:1QE5" FT HELIX 225..233 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 237..247 FT /evidence="ECO:0007829|PDB:1QE5" FT TURN 249..251 FT /evidence="ECO:0007829|PDB:1QE5" FT STRAND 252..254 FT /evidence="ECO:0007829|PDB:1C3X" FT HELIX 258..280 FT /evidence="ECO:0007829|PDB:1QE5" 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 //