PPNP_SYNC1
ID PPNP_SYNC1 Reviewed; 104 AA.
AC Q3A4X0;
DT 21-AUG-2007, integrated into UniProtKB/Swiss-Prot.
DT 22-NOV-2005, sequence version 1.
DT 25-MAY-2022, entry version 75.
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=Pcar_1338;
OS Syntrophotalea carbinolica (strain DSM 2380 / NBRC 103641 / GraBd1)
OS (Pelobacter carbinolicus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Syntrophotaleaceae; Syntrophotalea.
OX NCBI_TaxID=338963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2380 / NBRC 103641 / GraBd1;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Chertkov O., Schmutz J., Larimer F.,
RA Land M., Kyrpides N., Ivanova N., Richardson P.;
RT "Complete sequence of Pelobacter carbinolicus DSM 2380.";
RL Submitted (OCT-2005) 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; CP000142; ABA88587.1; -; Genomic_DNA.
DR RefSeq; WP_011341063.1; NC_007498.2.
DR AlphaFoldDB; Q3A4X0; -.
DR SMR; Q3A4X0; -.
DR STRING; 338963.Pcar_1338; -.
DR EnsemblBacteria; ABA88587; ABA88587; Pcar_1338.
DR KEGG; pca:Pcar_1338; -.
DR eggNOG; COG3123; Bacteria.
DR HOGENOM; CLU_157874_1_0_7; -.
DR OMA; YHYICHF; -.
DR OrthoDB; 1937865at2; -.
DR Proteomes; UP000002534; Chromosome.
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; Reference proteome; Transferase.
FT CHAIN 1..104
FT /note="Pyrimidine/purine nucleoside phosphorylase"
FT /id="PRO_0000298703"
SQ SEQUENCE 104 AA; 11552 MW; 687F4B7EF6677DB3 CRC64;
MSEFKNVTLI KKANVYYDGK VTSRTVIFAD GTKKTLGIMM PGEYTFDTAA AEVMEMLGGS
MEVLLPGAET WQSFHEGQSF EVPANSQFSL KIKEVADYCC SYLK
