ID A0A011A9H6_9BACT Unreviewed; 104 AA. AC A0A011A9H6; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 22-NOV-2017, entry version 12. DE RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000256|SAAS:SAAS00950111}; DE EC=2.4.2.2 {ECO:0000256|SAAS:SAAS00950116}; GN ORFNames=Cloev_0809 {ECO:0000313|EMBL:EXG78681.1}; OS Cloacibacillus evryensis DSM 19522. OC Bacteria; Synergistetes; Synergistia; Synergistales; Synergistaceae; OC Cloacibacillus. OX NCBI_TaxID=866499 {ECO:0000313|EMBL:EXG78681.1, ECO:0000313|Proteomes:UP000023044}; RN [1] {ECO:0000313|EMBL:EXG78681.1, ECO:0000313|Proteomes:UP000023044} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19522 {ECO:0000313|EMBL:EXG78681.1, RC ECO:0000313|Proteomes:UP000023044}; RG DOE Joint Genome Institute; RA Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K., RA Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A., RA Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.; RL Submitted (JUL-2013) to the EMBL/GenBank/DDBJ databases. 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:0000256|SAAS:SAAS00950112}. CC -!- CATALYTIC ACTIVITY: Adenosine + phosphate = adenine + alpha-D- CC ribose 1-phosphate. {ECO:0000256|SAAS:SAAS00950094}. CC -!- CATALYTIC ACTIVITY: Cytidine + phosphate = cytosine + alpha-D- CC ribose 1-phosphate. {ECO:0000256|SAAS:SAAS00950107}. CC -!- CATALYTIC ACTIVITY: Guanosine + phosphate = guanine + alpha-D- CC ribose 1-phosphate. {ECO:0000256|SAAS:SAAS00950109}. CC -!- CATALYTIC ACTIVITY: Inosine + phosphate = hypoxanthine + alpha-D- CC ribose 1-phosphate. {ECO:0000256|SAAS:SAAS00950110}. CC -!- CATALYTIC ACTIVITY: Purine nucleoside + phosphate = purine + CC alpha-D-ribose 1-phosphate. {ECO:0000256|SAAS:SAAS00950101}. CC -!- CATALYTIC ACTIVITY: Thymidine + phosphate = thymine + 2-deoxy- CC alpha-D-ribose 1-phosphate. {ECO:0000256|SAAS:SAAS00950092}. CC -!- CATALYTIC ACTIVITY: Uridine + phosphate = uracil + alpha-D-ribose CC 1-phosphate. {ECO:0000256|SAAS:SAAS00950108}. CC -!- CATALYTIC ACTIVITY: Xanthosine + phosphate = xanthine + alpha-D- CC ribose 1-phosphate. {ECO:0000256|SAAS:SAAS00950079}. CC -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family. CC {ECO:0000256|SAAS:SAAS00950113}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {ECO:0000313|EMBL:EXG78681.1}. 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; JFBR01000001; EXG78681.1; -; Genomic_DNA. DR RefSeq; WP_008710742.1; NZ_KK073872.1. DR EnsemblBacteria; EXG78681; EXG78681; Cloev_0809. DR Proteomes; UP000023044; Unassembled WGS sequence. DR Gene3D; 2.60.120.10; -; 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 {ECO:0000313|Proteomes:UP000023044}; KW Glycosyltransferase {ECO:0000256|SAAS:SAAS00950104}; KW Reference proteome {ECO:0000313|Proteomes:UP000023044}; KW Transferase {ECO:0000256|SAAS:SAAS00950076}. SQ SEQUENCE 104 AA; 11793 MW; 7068D51362F7779D CRC64; MADFINSVDV KTLVNIYCDG KVQSRTLRYP DGKLQTLGVY LPGEFEFHSE GPEKVIMTAG AVEVLFPEDN DWRRVETGEC YDVPADTMFK VRCGVISEYI CDFL //