ID DEOD_CLOTE Reviewed; 235 AA. AC Q894Z3; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 113. DE RecName: Full=Purine nucleoside phosphorylase DeoD-type {ECO:0000255|HAMAP-Rule:MF_01627}; DE Short=PNP {ECO:0000255|HAMAP-Rule:MF_01627}; DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01627}; GN Name=deoD {ECO:0000255|HAMAP-Rule:MF_01627}; GN OrderedLocusNames=CTC_01388; OS Clostridium tetani (strain Massachusetts / E88). OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; OC Clostridium. OX NCBI_TaxID=212717; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Massachusetts / E88; RX PubMed=12552129; DOI=10.1073/pnas.0335853100; RA Brueggemann H., Baeumer S., Fricke W.F., Wiezer A., Liesegang H., RA Decker I., Herzberg C., Martinez-Arias R., Merkl R., Henne A., RA Gottschalk G.; RT "The genome sequence of Clostridium tetani, the causative agent of tetanus RT disease."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003). CC -!- FUNCTION: Catalyzes the reversible phosphorolytic breakdown of the N- CC glycosidic bond in the beta-(deoxy)ribonucleoside molecules, with the CC formation of the corresponding free purine bases and pentose-1- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_01627}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a purine D-ribonucleoside + phosphate = a purine nucleobase + CC alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, ChEBI:CHEBI:26386, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, ChEBI:CHEBI:142355; EC=2.4.2.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01627}; 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:0000255|HAMAP-Rule:MF_01627}; CC -!- SUBUNIT: Homohexamer; trimer of homodimers. {ECO:0000255|HAMAP- CC Rule:MF_01627}. CC -!- SIMILARITY: Belongs to the PNP/UDP phosphorylase family. CC {ECO:0000255|HAMAP-Rule:MF_01627}. 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; AE015927; AAO35947.1; -; Genomic_DNA. DR RefSeq; WP_011099609.1; NC_004557.1. DR AlphaFoldDB; Q894Z3; -. DR SMR; Q894Z3; -. DR STRING; 212717.CTC_01388; -. DR GeneID; 24254680; -. DR KEGG; ctc:CTC_01388; -. DR HOGENOM; CLU_068457_2_0_9; -. DR OrthoDB; 9782889at2; -. DR Proteomes; UP000001412; Chromosome. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009164; P:nucleoside catabolic process; IEA:UniProt. DR GO; GO:0042278; P:purine nucleoside metabolic process; IEA:UniProtKB-UniRule. DR CDD; cd09006; PNP_EcPNPI-like; 1. DR Gene3D; 3.40.50.1580; Nucleoside phosphorylase domain; 1. DR HAMAP; MF_01627; Pur_nucleosid_phosp; 1. DR InterPro; IPR004402; DeoD-type. DR InterPro; IPR018016; Nucleoside_phosphorylase_CS. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR035994; Nucleoside_phosphorylase_sf. DR NCBIfam; TIGR00107; deoD; 1. DR PANTHER; PTHR43691:SF11; FI09636P-RELATED; 1. DR PANTHER; PTHR43691; URIDINE PHOSPHORYLASE; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; Purine and uridine phosphorylases; 1. DR PROSITE; PS01232; PNP_UDP_1; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Reference proteome; Transferase. FT CHAIN 1..235 FT /note="Purine nucleoside phosphorylase DeoD-type" FT /id="PRO_0000063127" FT ACT_SITE 204 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627" FT BINDING 4 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 20 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 24 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 43 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 87..90 FT /ligand="phosphate" FT /ligand_id="ChEBI:CHEBI:43474" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 179..181 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P50389" FT BINDING 203..204 FT /ligand="a purine D-ribonucleoside" FT /ligand_id="ChEBI:CHEBI:142355" FT /ligand_note="ligand shared between dimeric partners" FT /note="in other chain" FT /evidence="ECO:0000250|UniProtKB:P50389" FT SITE 217 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627" SQ SEQUENCE 235 AA; 25795 MW; 232E419240F986DD CRC64; MSIHINAPEG AIAESILLPG DPLRAKFIAD TFLEDVVCYN EVRGMYGFTG TYKGKRVSVQ GTGMGIPSMS IYATELIESY GVKNLIRVGT CGSYVEKVKV RDLIIAMSAC TNSNINLVPF KGRTFAPTAS FDLLKPAYDI AVEKGFEPKV GSIYSSDIFY DDDKEDWKTW AKYGCLGVEM ETAALYTIAA KYGVNALTLL TVSDHFVTHE VTSAEERQTT FKAMMEVALD TIVNL //