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 28-FEB-2018, entry version 70. 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=LA_0973; OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai OS (strain 56601). OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; 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., RA Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., RA Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., RA Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., RA Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., RA Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., RA Xu J.-G., Zhao G.-P.; RT "Unique physiological and pathogenic features of Leptospira RT interrogans revealed by whole-genome sequencing."; RL Nature 422:888-893(2003). 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: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: Adenosine + phosphate = adenine + alpha-D- CC ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: Cytidine + phosphate = cytosine + alpha-D- CC ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: Guanosine + phosphate = guanine + alpha-D- CC ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: Inosine + phosphate = hypoxanthine + alpha-D- CC ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy- CC alpha-D-ribose 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: Uridine + phosphate = uracil + alpha-D-ribose CC 1-phosphate. {ECO:0000255|HAMAP-Rule:MF_01537}. CC -!- CATALYTIC ACTIVITY: Xanthosine + phosphate = xanthine + alpha-D- CC ribose 1-phosphate. {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 ProteinModelPortal; Q8F7H3; -. DR SMR; Q8F7H3; -. DR STRING; 189518.LA_0973; -. DR EnsemblBacteria; AAN48171; AAN48171; LA_0973. DR GeneID; 1150315; -. DR KEGG; lil:LA_0973; -. DR PATRIC; fig|189518.3.peg.973; -. DR eggNOG; ENOG4105NBK; Bacteria. DR eggNOG; COG3123; LUCA. DR HOGENOM; HOG000218057; -. DR InParanoid; Q8F7H3; -. DR KO; K09913; -. DR OMA; YHYICHF; -. DR BioCyc; LINT189518:G1GL4-782-MONOMER; -. DR Proteomes; UP000001408; Chromosome I. DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IEA:UniProtKB-EC. 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; DUF1255; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 106 Pyrimidine/purine nucleoside FT phosphorylase. FT /FTId=PRO_0000211769. SQ SEQUENCE 106 AA; 12014 MW; C3943FEB07F842AC CRC64; MSQFENVTII KKANVYYDGK VTSRSILFQD GSKKTLGILM PGQYDFGTDE KEIMEILDGE LLVKLPGQEV WSEIKGGQSF EVPAKSRFQM DVKKISDYCC SYIQNS //