ID D8A4F5_ECOMS Unreviewed; 94 AA. AC D8A4F5; DT 05-OCT-2010, integrated into UniProtKB/TrEMBL. DT 05-OCT-2010, sequence version 1. DT 05-DEC-2018, entry version 33. 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 EC=2.4.2.15 {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 EC=2.4.2.4 {ECO:0000256|HAMAP-Rule:MF_01537}; DE AltName: Full=Uridine phosphorylase {ECO:0000256|HAMAP-Rule:MF_01537}; DE EC=2.4.2.3 {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; Proteobacteria; 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., RA Courtney L., Fronick C., Harrison M., Strong C., Farmer C., RA Delahaunty K., Markovic C., Hall O., Minx P., Tomlinson C., RA Mitreva M., Hou S., Chen J., Wollam A., Pepin K.H., Johnson M., RA Bhonagiri V., Zhang X., Suruliraj S., Warren W., Chinwalla A., RA Mardis E.R., Wilson R.K.; RL Submitted (JUN-2010) 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|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088094}. CC -!- CATALYTIC ACTIVITY: CC Reaction=a purine D-ribonucleoside + phosphate = a purine CC nucleobase + alpha-D-ribose 1-phosphate; Xref=Rhea:RHEA:19805, CC ChEBI:CHEBI:142355, ChEBI:CHEBI:26386, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:57720; EC=2.4.2.1; Evidence={ECO:0000256|HAMAP- CC Rule:MF_01537, ECO:0000256|SAAS:SAAS01088097}; CC -!- CATALYTIC ACTIVITY: CC Reaction=adenosine + phosphate = adenine + alpha-D-ribose 1- CC phosphate; Xref=Rhea:RHEA:27642, ChEBI:CHEBI:16335, CC ChEBI:CHEBI:16708, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC EC=2.4.2.1; Evidence={ECO:0000256|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088089}; CC -!- CATALYTIC ACTIVITY: CC Reaction=cytidine + phosphate = alpha-D-ribose 1-phosphate + CC cytosine; Xref=Rhea:RHEA:52540, ChEBI:CHEBI:16040, CC ChEBI:CHEBI:17562, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088095}; CC -!- CATALYTIC ACTIVITY: CC Reaction=guanosine + phosphate = alpha-D-ribose 1-phosphate + CC guanine; Xref=Rhea:RHEA:13233, ChEBI:CHEBI:16235, CC ChEBI:CHEBI:16750, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088084}; 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 EC=2.4.2.1; Evidence={ECO:0000256|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088096}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + thymidine = 2-deoxy-alpha-D-ribose 1- CC phosphate + thymine; Xref=Rhea:RHEA:16037, ChEBI:CHEBI:17748, CC ChEBI:CHEBI:17821, ChEBI:CHEBI:43474, ChEBI:CHEBI:57259; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088088}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + uridine = alpha-D-ribose 1-phosphate + CC uracil; Xref=Rhea:RHEA:24388, ChEBI:CHEBI:16704, CC ChEBI:CHEBI:17568, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC Evidence={ECO:0000256|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088093}; CC -!- CATALYTIC ACTIVITY: CC Reaction=phosphate + xanthosine = alpha-D-ribose 1-phosphate + CC xanthine; Xref=Rhea:RHEA:27638, ChEBI:CHEBI:17712, CC ChEBI:CHEBI:18107, ChEBI:CHEBI:43474, ChEBI:CHEBI:57720; CC EC=2.4.2.1; Evidence={ECO:0000256|HAMAP-Rule:MF_01537, CC ECO:0000256|SAAS:SAAS01088090}; CC -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family. CC {ECO:0000256|HAMAP-Rule:MF_01537, ECO:0000256|SAAS:SAAS01088098}. 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: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 ProteinModelPortal; D8A4F5; -. DR SMR; D8A4F5; -. DR EnsemblBacteria; EFK21973; EFK21973; HMPREF9530_01393. 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 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; Ppnp; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000005688}; KW Glycosyltransferase {ECO:0000256|HAMAP-Rule:MF_01537, KW ECO:0000256|SAAS:SAAS01088087}; KW Transferase {ECO:0000256|HAMAP-Rule:MF_01537, KW ECO:0000256|SAAS:SAAS01088085}. SQ SEQUENCE 94 AA; 10234 MW; D7EF5C0AFD86D661 CRC64; MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL //