ID A0A011A9H6_9BACT Unreviewed; 104 AA. AC A0A011A9H6; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 11-DEC-2019, entry version 18. DE RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000256|SAAS:SAAS01088086}; DE EC=2.4.2.2 {ECO:0000256|SAAS:SAAS01088092}; 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, 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. CC {ECO:0000256|SAAS:SAAS01088094}. 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; CC Evidence={ECO:0000256|SAAS:SAAS01122746}; 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; CC Evidence={ECO:0000256|SAAS:SAAS01122736}; 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; CC Evidence={ECO:0000256|SAAS:SAAS01122750}; 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=2.4.2.15; CC Evidence={ECO:0000256|SAAS:SAAS01122744}; 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:0000256|SAAS:SAAS01122753}; 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:0000256|SAAS:SAAS01122742}; 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=2.4.2.4; CC Evidence={ECO:0000256|SAAS:SAAS01122737}; 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:0000256|SAAS:SAAS01122739}; 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=2.4.2.3; CC Evidence={ECO:0000256|SAAS:SAAS01122747}; 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; CC Evidence={ECO:0000256|SAAS:SAAS01122751}; CC -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family. CC {ECO:0000256|SAAS:SAAS01088098}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {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 OrthoDB; 1937865at2; -. DR Proteomes; UP000023044; Unassembled WGS sequence. 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 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 {ECO:0000256|SAAS:SAAS01088087}; KW Transferase {ECO:0000256|SAAS:SAAS01088085}. SQ SEQUENCE 104 AA; 11793 MW; 7068D51362F7779D CRC64; MADFINSVDV KTLVNIYCDG KVQSRTLRYP DGKLQTLGVY LPGEFEFHSE GPEKVIMTAG AVEVLFPEDN DWRRVETGEC YDVPADTMFK VRCGVISEYI CDFL //