ID D8A4F5_ECOMS Unreviewed; 94 AA. AC D8A4F5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 08-NOV-2023, entry version 49. DE RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE EC=2.4.2.1 {ECO:0000256|HAMAP-Rule:MF_01537}; DE EC=2.4.2.2 {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Adenosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Cytidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Guanosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Inosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Thymidine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Uridine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Xanthosine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; GN Name=ppnP {ECO:0000256|HAMAP-Rule:MF_01537}; GN ORFNames=HMPREF9530_01393 {ECO:0000313|EMBL:EFK21973.1}; OS Escherichia coli (strain MS 21-1). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=749527 {ECO:0000313|EMBL:EFK21973.1, ECO:0000313|Proteomes:UP000005688}; RN [1] {ECO:0000313|EMBL:EFK21973.1, ECO:0000313|Proteomes:UP000005688} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MS 21-1 {ECO:0000313|EMBL:EFK21973.1, RC ECO:0000313|Proteomes:UP000005688}; RA Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L., RA Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C., RA Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A., RA Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W., RA Chinwalla A., Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) 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. {ECO:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_01537}; CC -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family. CC {ECO:0000256|HAMAP-Rule:MF_01537}. 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:EFK21973.1}. 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; ADTR01000128; EFK21973.1; -; Genomic_DNA. DR RefSeq; WP_000941942.1; NZ_GG772658.1. DR AlphaFoldDB; D8A4F5; -. DR SMR; D8A4F5; -. DR EnsemblBacteria; EFK21973; EFK21973; HMPREF9530_01393. DR GeneID; 82262794; -. DR HOGENOM; CLU_157874_0_0_6; -. DR Proteomes; UP000005688; Unassembled WGS sequence. 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 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 {ECO:0000256|ARBA:ARBA00022676, ECO:0000256|HAMAP- KW Rule:MF_01537}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_01537}. SQ SEQUENCE 94 AA; 10234 MW; D7EF5C0AFD86D661 CRC64; MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL //