ID DEOD1_PHOPR Reviewed; 241 AA. AC Q6LUH1; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 27-MAR-2024, entry version 100. DE RecName: Full=Purine nucleoside phosphorylase DeoD-type 1 {ECO:0000255|HAMAP-Rule:MF_01627}; DE Short=PNP 1 {ECO:0000255|HAMAP-Rule:MF_01627}; DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01627}; GN Name=deoD1 {ECO:0000255|HAMAP-Rule:MF_01627}; GN OrderedLocusNames=PBPRA0633; OS Photobacterium profundum (strain SS9). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae; OC Photobacterium. OX NCBI_TaxID=298386; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1253 / SS9; RX PubMed=15746425; DOI=10.1126/science.1103341; RA Vezzi A., Campanaro S., D'Angelo M., Simonato F., Vitulo N., Lauro F.M., RA Cestaro A., Malacrida G., Simionati B., Cannata N., Romualdi C., RA Bartlett D.H., Valle G.; RT "Life at depth: Photobacterium profundum genome sequence and expression RT analysis."; RL Science 307:1459-1461(2005). 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; CR378664; CAG19054.1; -; Genomic_DNA. DR RefSeq; WP_006230712.1; NC_006370.1. DR AlphaFoldDB; Q6LUH1; -. DR SMR; Q6LUH1; -. DR STRING; 298386.PBPRA0633; -. DR KEGG; ppr:PBPRA0633; -. DR eggNOG; COG0813; Bacteria. DR HOGENOM; CLU_068457_2_0_6; -. DR Proteomes; UP000000593; Chromosome 1. 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:SF2; PURINE NUCLEOSIDE PHOSPHORYLASE DEOD-TYPE; 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..241 FT /note="Purine nucleoside phosphorylase DeoD-type 1" FT /id="PRO_0000063151" 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 241 AA; 26036 MW; 392EDEB2F948B130 CRC64; MATPHINAEM GDFADVVLMP GDPLRAKYIA ETFLQDVKEV CNVRSMFGYT GTYKGRKISV MGHGMGIPSC SIYATELIKD FGVKKIIRVG SCGAVRDDVK LRDVVIGMGA STDSKVNRIR FGGHDFAAIA DFGMVQNAVD AAKAKGIPVK VGNIFSADLF YNPDFEFFKT MDKYGIVGVE MEAAGIYGVA AEFGAKALTI CTVSDHILRG EATTSEERQL TFNEMMEIAL ESVLLGDADE A //