ID DEOD_BUCAI Reviewed; 234 AA. AC P57606; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 1. DT 27-MAR-2024, entry version 114. 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}; OrderedLocusNames=BU541; OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon OS pisum symbiotic bacterium). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Erwiniaceae; Buchnera. OX NCBI_TaxID=107806; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=APS; RX PubMed=10993077; DOI=10.1038/35024074; RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.; RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera RT sp. APS."; RL Nature 407:81-86(2000). 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; BA000003; BAB13233.1; -; Genomic_DNA. DR RefSeq; NP_240347.1; NC_002528.1. DR RefSeq; WP_010896154.1; NC_002528.1. DR AlphaFoldDB; P57606; -. DR SMR; P57606; -. DR STRING; 563178.BUAP5A_534; -. DR EnsemblBacteria; BAB13233; BAB13233; BAB13233. DR KEGG; buc:BU541; -. DR PATRIC; fig|107806.10.peg.545; -. DR eggNOG; COG0813; Bacteria. DR HOGENOM; CLU_068457_2_0_6; -. DR Proteomes; UP000001806; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProt. 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..234 FT /note="Purine nucleoside phosphorylase DeoD-type" FT /id="PRO_0000063123" FT ACT_SITE 205 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627" FT BINDING 5 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 21 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 25 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 44 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 88..91 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 180..182 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 204..205 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 218 FT /note="Important for catalytic activity" FT /evidence="ECO:0000255|HAMAP-Rule:MF_01627" SQ SEQUENCE 234 AA; 26426 MW; 670FC41BE0EB41FA CRC64; MSTPHINSKK DDFSDIVLMP GDPVRAKYIA EKYLSNFVQV NDTRLMLAYT GFYKNRKISI MSHGIGIPSA SLYTRELIIE FNVKKIIRIG TCGAVRDDIK LRDIVISMGA STDSKVNRIR FNDHDFAAIA DFDMIYNIVS ISKKMKIKVS IGNFFTTDSF YNDDKKMLNI LKKYNIIGVD METAGIYGVA SELKVQALSI CTVSDHITNK EFLSSKERES SFNDMIELAL ESVL //