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 23-FEB-2022, entry version 71. DE RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE EC=2.4.2.1 {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 AltName: Full=Inosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537}; DE AltName: Full=Uridine phosphorylase {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}; 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., Gwinn Giglio M., RA Madupu R., Nelson W.C., Rosovitz M.J., Sullivan S.A., Crabtree J., RA Creasy T., Davidsen T.M., Haft D.H., Zafar N., Zhou L., Halpin R., RA Holley T., Khouri H.M., Feldblyum T.V., White O., Fraser C.M., RA Chatterjee A.K., Cartinhour S., Schneider D., Mansfield J.W., Collmer A., RA Buell R.; RT "Whole-genome sequence analysis of Pseudomonas syringae pv. phaseolicola RT 1448A reveals divergence among pathovars in genes involved in virulence and RT transposition."; RL J. Bacteriol. 187:6488-6498(2005). CC -!- FUNCTION: Catalyzes the phosphorolysis of diverse nucleosides, yielding CC D-ribose 1-phosphate and the respective free bases. Can use uridine, CC adenosine, guanosine, cytidine, thymidine, inosine and xanthosine as CC substrates. Also catalyzes the reverse reactions. {ECO:0000255|HAMAP- CC Rule:MF_01537}. 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_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1-phosphate; CC Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, ChEBI:CHEBI:16708, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine + phosphate = alpha-D-ribose 1-phosphate + cytosine; CC Xref=Rhea:RHEA:52540, ChEBI:CHEBI:16040, ChEBI:CHEBI:17562, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + guanine; CC Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, ChEBI:CHEBI:16750, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; CC 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; EC=2.4.2.1; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1-phosphate + CC thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, ChEBI:CHEBI:17821, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; EC=2.4.2.2; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01537}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + uracil; CC Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, ChEBI:CHEBI:17568, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.2; CC 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, ChEBI:CHEBI:18107, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; EC=2.4.2.1; 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 GeneID; 61869221; -. DR KEGG; psp:PSPPH_1791; -. DR eggNOG; COG3123; Bacteria. DR HOGENOM; CLU_157874_0_0_6; -. 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 Glycosyltransferase; Transferase. FT CHAIN 1..93 FT /note="Pyrimidine/purine nucleoside phosphorylase" FT /id="PRO_0000298713" SQ SEQUENCE 93 AA; 10344 MW; 1B94ABE3BF874D6B CRC64; MFKVNEYFDG TVKSIAFSQV DGQATIGVMA AGEYEFGTAQ REIMHVISGE LNVKLPDSTD WETFSTGSQF NVPANSKFQL KVSVDTAYLC EYR //