ID PPNP_LEPIN Reviewed; 106 AA. AC Q8F7H3; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 13-SEP-2023, entry version 87. 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=LA_0973; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain OS 56601). OC Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae; OC Leptospira. OX NCBI_TaxID=189518; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=56601; RX PubMed=12712204; DOI=10.1038/nature01597; RA Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X., RA Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X., RA Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F., RA Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y., RA Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I., RA Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira interrogans RT revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). 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; AE010300; AAN48171.1; -; Genomic_DNA. DR RefSeq; NP_711153.1; NC_004342.2. DR RefSeq; WP_000077234.1; NC_004342.2. DR AlphaFoldDB; Q8F7H3; -. DR SMR; Q8F7H3; -. DR STRING; 189518.LA_0973; -. DR PaxDb; Q8F7H3; -. DR EnsemblBacteria; AAN48171; AAN48171; LA_0973. DR GeneID; 61142561; -. DR KEGG; lil:LA_0973; -. DR PATRIC; fig|189518.3.peg.973; -. DR HOGENOM; CLU_157874_1_0_12; -. DR InParanoid; Q8F7H3; -. DR OMA; YHYICHF; -. DR OrthoDB; 9793848at2; -. DR Proteomes; UP000001408; Chromosome I. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IBA:GO_Central. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IBA:GO_Central. DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0004850; F:uridine phosphorylase activity; IEA:UniProtKB-EC. DR CDD; cd20296; cupin_PpnP-like; 1. DR Gene3D; 2.60.120.10; Jelly Rolls; 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; PYRIMIDINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1. DR PANTHER; PTHR36540:SF1; PYRIMIDINE/PURINE NUCLEOSIDE PHOSPHORYLASE; 1. DR Pfam; PF06865; Ppnp; 1. DR SUPFAM; SSF51182; RmlC-like cupins; 1. PE 3: Inferred from homology; KW Glycosyltransferase; Reference proteome; Transferase. FT CHAIN 1..106 FT /note="Pyrimidine/purine nucleoside phosphorylase" FT /id="PRO_0000211769" SQ SEQUENCE 106 AA; 12014 MW; C3943FEB07F842AC CRC64; MSQFENVTII KKANVYYDGK VTSRSILFQD GSKKTLGILM PGQYDFGTDE KEIMEILDGE LLVKLPGQEV WSEIKGGQSF EVPAKSRFQM DVKKISDYCC SYIQNS //