ID A0A8E5JHS7_SALEN Unreviewed; 94 AA. AC A0A8E5JHS7; DT 19-JAN-2022, integrated into UniProtKB/TrEMBL. DT 19-JAN-2022, sequence version 1. DT 03-MAY-2023, entry version 6. 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 ECO:0000313|EMBL:QUZ92097.1}; GN ORFNames=JYM99_17305 {ECO:0000313|EMBL:QUZ92097.1}; OS Salmonella enterica subsp. enterica serovar Enteritidis str. 607307-2. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Salmonella. OX NCBI_TaxID=887070 {ECO:0000313|EMBL:QUZ92097.1}; RN [1] {ECO:0000313|EMBL:QUZ92097.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=607307-2 {ECO:0000313|EMBL:QUZ92097.1}; RA Hoffmann M., Balkey M., Luo Y.; RT "Whole genome PacBio Sequel sequence of Salmonella enterica subsp. RT enterica."; RL Submitted (MAY-2021) 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 --------------------------------------------------------------------------- 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; CP074238; QUZ92097.1; -; Genomic_DNA. DR RefSeq; WP_000941953.1; NZ_ALGO01000020.1. DR SMR; A0A8E5JHS7; -. 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 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; 10189 MW; 7B43FE679F0C4A93 CRC64; MLQSNEYFSG KVKSIGFTSS STGRASVGVM AEGEYTFGTA EPEEMTVVSG ALKVLLPGTV EWKVYTAGEV FNVPGHSEFH LQVAEPTSYL CRYL //