ID PPNP_PSE14 Reviewed; 93 AA. AC Q48KQ0; DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2005, sequence version 1. DT 08-MAY-2019, entry version 64. DE RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE EC=2.4.2.2 {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Adenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Cytidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Guanosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE EC=2.4.2.15 {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Inosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE EC=2.4.2.4 {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Uridine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE EC=2.4.2.3 {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Xanthosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; GN Name=ppnP {ECO:0000255|HAMAP-Rule:MF_01537}; GN OrderedLocusNames=PSPPH_1791; OS Pseudomonas savastanoi pv. phaseolicola (strain 1448A / Race 6) OS (Pseudomonas syringae pv. phaseolicola (strain 1448A / Race 6)). OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=264730; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=1448A / Race 6; RX PubMed=16159782; DOI=10.1128/JB.187.18.6488-6498.2005; RA Joardar V., Lindeberg M., Jackson R.W., Selengut J., Dodson R., RA Brinkac L.M., Daugherty S.C., DeBoy R.T., Durkin A.S., RA Gwinn Giglio M., Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., RA Crabtree J., Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., RA Halpin R., Holley T., Khouri H.M., Feldblyum T.V., White O., RA Fraser C.M., Chatterjee A.K., Cartinhour S., Schneider D., RA Mansfield J.W., Collmer A., Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. RT phaseolicola 1448A reveals divergence among pathovars in genes RT involved in virulence and transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- FUNCTION: Catalyzes the phosphorolysis of diverse nucleosides, CC yielding D-ribose 1-phosphate and the respective free bases. Can CC use uridine, adenosine, guanosine, cytidine, thymidine, inosine CC and xanthosine as substrates. Also catalyzes the reverse CC reactions. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a purine D-ribonucleoside + phosphate = a purine CC nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, CC ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720, CC ChEBI:CHEBI:142355; Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1- CC phosphate; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, CC ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine + phosphate = alpha-D-ribose 1-phosphate + CC cytosine; Xref=Rhea:RHEA:52540, ChEBI:CHEBI:16040, CC ChEBI:CHEBI:17562, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + CC guanine; Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, CC ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC EC=2.4.2.15; Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=inosine + phosphate = alpha-D-ribose 1-phosphate + CC hypoxanthine; Xref=Rhea:RHEA:27646, ChEBI:CHEBI:17368, CC ChEBI:CHEBI:17596, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1- CC phosphate + thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, CC ChEBI:CHEBI:17821, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; CC EC=2.4.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1- CC phosphate + thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, CC ChEBI:CHEBI:17821, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; CC EC=2.4.2.4; Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + CC uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, CC ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC EC=2.4.2.2; Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + CC uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, CC ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC EC=2.4.2.3; Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + xanthosine = alpha-D-ribose 1-phosphate + CC xanthine; Xref=Rhea:RHEA:27638, ChEBI:CHEBI:17712, CC ChEBI:CHEBI:18107, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family. CC {ECO:0000255|HAMAP-Rule:MF_01537}. 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; CP000058; AAZ34394.1; -; Genomic_DNA. DR RefSeq; WP_004658419.1; NC_005773.3. DR SMR; Q48KQ0; -. DR STRING; 264730.PSPPH_1791; -. DR EnsemblBacteria; AAZ34394; AAZ34394; PSPPH_1791. DR KEGG; psp:PSPPH_1791; -. DR eggNOG; ENOG4105NBK; Bacteria. DR eggNOG; COG3123; LUCA. DR HOGENOM; HOG000218057; -. DR KO; K09913; -. DR OMA; YHYICHF; -. DR OrthoDB; 1937865at2; -. DR Proteomes; UP000000551; Chromosome. DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC. DR Gene3D; 2.60.120.10; -; 1. DR HAMAP; MF_01537; Nucleos_phosphorylase_PpnP; 1. DR InterPro; IPR009664; Ppnp. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin_sf. DR PANTHER; PTHR36540; PTHR36540; 1. DR Pfam; PF06865; Ppnp; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Transferase. FT CHAIN 1 93 Pyrimidine/purine nucleoside FT phosphorylase. FT /FTId=PRO_0000298713. SQ SEQUENCE 93 AA; 10344 MW; 1B94ABE3BF874D6B CRC64; MFKVNEYFDG TVKSIAFSQV DGQATIGVMA AGEYEFGTAQ REIMHVISGE LNVKLPDSTD WETFSTGSQF NVPANSKFQL KVSVDTAYLC EYR //