PPNP_ECOBW
ID PPNP_ECOBW Reviewed; 94 AA.
AC C4ZTF0;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01537};
DE EC=2.4.2.2 {ECO:0000255|HAMAP-Rule:MF_01537};
DE AltName: Full=Adenosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE AltName: Full=Cytidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE AltName: Full=Guanosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE AltName: Full=Inosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE AltName: Full=Thymidine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE AltName: Full=Uridine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
DE AltName: Full=Xanthosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537};
GN Name=ppnP {ECO:0000255|HAMAP-Rule:MF_01537}; OrderedLocusNames=BWG_0275;
OS Escherichia coli (strain K12 / MC4100 / BW2952).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=595496;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MC4100 / BW2952;
RX PubMed=19376874; DOI=10.1128/jb.00118-09;
RA Ferenci T., Zhou Z., Betteridge T., Ren Y., Liu Y., Feng L., Reeves P.R.,
RA Wang L.;
RT "Genomic sequencing reveals regulatory mutations and recombinational events
RT in the widely used MC4100 lineage of Escherichia coli K-12.";
RL J. Bacteriol. 191:4025-4029(2009).
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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|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:0000255|HAMAP-Rule:MF_01537};
CC -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family.
CC {ECO:0000255|HAMAP-Rule:MF_01537}.
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DR EMBL; CP001396; ACR62434.1; -; Genomic_DNA.
DR RefSeq; WP_000941942.1; NC_012759.1.
DR AlphaFoldDB; C4ZTF0; -.
DR SMR; C4ZTF0; -.
DR GeneID; 67416534; -.
DR KEGG; ebw:BWG_0275; -.
DR HOGENOM; CLU_157874_0_0_6; -.
DR OMA; YHYICHF; -.
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 Glycosyltransferase; Transferase.
FT CHAIN 1..94
FT /note="Pyrimidine/purine nucleoside phosphorylase"
FT /id="PRO_1000215412"
SQ SEQUENCE 94 AA; 10234 MW; D7EF5C0AFD86D661 CRC64;
MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT
DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL
