PPNP_PECAS
ID PPNP_PECAS Reviewed; 94 AA.
AC Q6D871;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, 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=ECA1104;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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; BX950851; CAG74014.1; -; Genomic_DNA.
DR RefSeq; WP_005975968.1; NC_004547.2.
DR AlphaFoldDB; Q6D871; -.
DR SMR; Q6D871; -.
DR STRING; 218491.ECA1104; -.
DR EnsemblBacteria; CAG74014; CAG74014; ECA1104.
DR GeneID; 51388595; -.
DR GeneID; 57241283; -.
DR GeneID; 66803675; -.
DR KEGG; eca:ECA1104; -.
DR eggNOG; COG3123; Bacteria.
DR HOGENOM; CLU_157874_0_0_6; -.
DR OMA; YHYICHF; -.
DR OrthoDB; 1937865at2; -.
DR Proteomes; UP000007966; 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..94
FT /note="Pyrimidine/purine nucleoside phosphorylase"
FT /id="PRO_0000211766"
SQ SEQUENCE 94 AA; 10175 MW; 97BA4F00255A3D5D CRC64;
MLNVNEYFAG KVKSIGFEGD SIGRASVGVM DAGEYTFGTG QPEEMTVITG ALKVLLPGAP
DWQVFTPGET FFVPGKSEFN LQVVEPTSYL CKYL
