ID DEOD_ACTSZ Reviewed; 238 AA. AC A6VM01; DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 21-AUG-2007, sequence version 1. DT 27-MAR-2024, entry version 84. 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=Asuc_0624; OS Actinobacillus succinogenes (strain ATCC 55618 / DSM 22257 / CCUG 43843 / OS 130Z). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales; OC Pasteurellaceae; Actinobacillus. OX NCBI_TaxID=339671; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 55618 / DSM 22257 / CCUG 43843 / 130Z; RX PubMed=21118570; DOI=10.1186/1471-2164-11-680; RA McKinlay J.B., Laivenieks M., Schindler B.D., McKinlay A.A., RA Siddaramappa S., Challacombe J.F., Lowry S.R., Clum A., Lapidus A.L., RA Burkhart K.B., Harkins V., Vieille C.; RT "A genomic perspective on the potential of Actinobacillus succinogenes for RT industrial succinate production."; RL BMC Genomics 11:680-680(2010). 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; CP000746; ABR73998.1; -; Genomic_DNA. DR AlphaFoldDB; A6VM01; -. DR SMR; A6VM01; -. DR STRING; 339671.Asuc_0624; -. DR KEGG; asu:Asuc_0624; -. DR eggNOG; COG0813; Bacteria. DR HOGENOM; CLU_068457_2_0_6; -. DR OrthoDB; 9782889at2; -. DR Proteomes; UP000001114; 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: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..238 FT /note="Purine nucleoside phosphorylase DeoD-type" FT /id="PRO_1000073638" 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 238 AA; 25866 MW; 2958F4D87D42B0CE CRC64; MTPHINAPAG AFADVVLMPG DPLRAKYIAE TFLDQPELVT DVRNMLGYTG SYKGRRISVM GHGMGIPSCS IYSKELITEY GVKKIIRVGS CGAVRQDVHV RDVIIGLGAC TDSKVNRIRF RDNDFAAIAD FGMAQAAVQA AKNKKIKVHV GNLFSADLFY TPDVEMFDVM EKYGILGVEM EAAGIYGVAA EFGAKALSIC TVSDHIRSGE QTSSEERQTT FNEMIEIALE SVLLGDND //