PPNP_RALPJ
ID PPNP_RALPJ Reviewed; 105 AA.
AC B2UBA2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 25-MAY-2022, entry version 79.
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=Rpic_2828;
OS Ralstonia pickettii (strain 12J).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Ralstonia.
OX NCBI_TaxID=402626;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12J;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Meincke L., Brettin T., Detter J.C.,
RA Han C., Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Mikhailova N., Marsh T., Richardson P.;
RT "Complete sequence of chromosome 1 of Ralstonia pickettii 12J.";
RL Submitted (MAY-2008) 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: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; CP001068; ACD27951.1; -; Genomic_DNA.
DR RefSeq; WP_004631764.1; NC_010682.1.
DR AlphaFoldDB; B2UBA2; -.
DR SMR; B2UBA2; -.
DR STRING; 402626.Rpic_2828; -.
DR EnsemblBacteria; ACD27951; ACD27951; Rpic_2828.
DR GeneID; 61390714; -.
DR KEGG; rpi:Rpic_2828; -.
DR eggNOG; COG3123; Bacteria.
DR HOGENOM; CLU_157874_1_0_4; -.
DR OMA; YHYICHF; -.
DR OrthoDB; 1937865at2; -.
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..105
FT /note="Pyrimidine/purine nucleoside phosphorylase"
FT /id="PRO_1000198672"
SQ SEQUENCE 105 AA; 11359 MW; 8110603D4655B099 CRC64;
MTTETFDGVR LTTKANVYFD GKCVSHSFTL PDGTKKSVGV VLPATLTFGT AAAEIMECVG
GSCEYKLDGT DEWKTSGAGD SFQVPANSKF DIRVTEAYHY ICHYA
