PPNP_ECOLI
ID PPNP_ECOLI Reviewed; 94 AA.
AC P0C037; P36768; P77343; Q2MC34;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Pyrimidine/purine nucleoside phosphorylase {ECO:0000255|HAMAP-Rule:MF_01537, ECO:0000303|PubMed:27941785};
DE EC=2.4.2.1 {ECO:0000255|HAMAP-Rule:MF_01537, ECO:0000269|PubMed:27941785};
DE EC=2.4.2.2 {ECO:0000255|HAMAP-Rule:MF_01537, ECO:0000269|PubMed:27941785};
DE AltName: Full=Adenosine phosphorylase {ECO:0000305|PubMed:27941785};
DE AltName: Full=Cytidine phosphorylase {ECO:0000305|PubMed:27941785};
DE AltName: Full=Guanosine phosphorylase {ECO:0000305|PubMed:27941785};
DE AltName: Full=Inosine phosphorylase {ECO:0000305|PubMed:27941785};
DE AltName: Full=Thymidine phosphorylase {ECO:0000305|PubMed:27941785};
DE AltName: Full=Uridine phosphorylase {ECO:0000305|PubMed:27941785};
DE AltName: Full=Xanthosine phosphorylase {ECO:0000305|PubMed:27941785};
GN Name=ppnP {ECO:0000303|PubMed:27941785};
GN Synonyms=yaiE {ECO:0000312|EMBL:AAC73494.1};
GN OrderedLocusNames=b0391, JW0382;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=8807285; DOI=10.1093/genetics/143.3.1101;
RA Ryder L., Sharples G.J., Lloyd R.G.;
RT "Recombination-dependent growth in exonuclease-depleted recBC sbcBC strains
RT of Escherichia coli K-12.";
RL Genetics 143:1101-1114(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=27941785; DOI=10.1038/nmeth.4103;
RA Sevin D.C., Fuhrer T., Zamboni N., Sauer U.;
RT "Nontargeted in vitro metabolomics for high-throughput identification of
RT novel enzymes in Escherichia coli.";
RL Nat. Methods 14:187-194(2017).
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. Is not able to
CC produce D-ribose 1-phosphate from D-ribose and phosphate.
CC {ECO:0000269|PubMed:27941785}.
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a consistent change
CC in xanthine level. {ECO:0000269|PubMed:27941785}.
CC -!- SIMILARITY: Belongs to the nucleoside phosphorylase PpnP family.
CC {ECO:0000255|HAMAP-Rule:MF_01537}.
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DR EMBL; X76979; CAA54286.1; -; Genomic_DNA.
DR EMBL; U73857; AAB18115.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73494.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76172.1; -; Genomic_DNA.
DR PIR; G64767; G64767.
DR RefSeq; NP_414925.1; NC_000913.3.
DR RefSeq; WP_000941942.1; NZ_STEB01000007.1.
DR PDB; 7EYJ; X-ray; 1.38 A; A=1-94.
DR PDB; 7EYK; X-ray; 1.38 A; A=1-94.
DR PDBsum; 7EYJ; -.
DR PDBsum; 7EYK; -.
DR AlphaFoldDB; P0C037; -.
DR SMR; P0C037; -.
DR BioGRID; 4259817; 22.
DR BioGRID; 849437; 8.
DR IntAct; P0C037; 9.
DR STRING; 511145.b0391; -.
DR jPOST; P0C037; -.
DR PaxDb; P0C037; -.
DR PRIDE; P0C037; -.
DR EnsemblBacteria; AAC73494; AAC73494; b0391.
DR EnsemblBacteria; BAE76172; BAE76172; BAE76172.
DR GeneID; 67416534; -.
DR GeneID; 945048; -.
DR KEGG; ecj:JW0382; -.
DR KEGG; eco:b0391; -.
DR PATRIC; fig|511145.12.peg.403; -.
DR EchoBASE; EB2079; -.
DR eggNOG; COG3123; Bacteria.
DR HOGENOM; CLU_157874_0_0_6; -.
DR InParanoid; P0C037; -.
DR OMA; YHYICHF; -.
DR PhylomeDB; P0C037; -.
DR BioCyc; EcoCyc:EG12159-MON; -.
DR BioCyc; MetaCyc:EG12159-MON; -.
DR BRENDA; 2.4.2.2; 2026.
DR BRENDA; 2.4.2.4; 2026.
DR PRO; PR:P0C037; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0047975; F:guanosine phosphorylase activity; IEA:UniProtKB-EC.
DR GO; GO:0004731; F:purine-nucleoside phosphorylase activity; IDA:EcoCyc.
DR GO; GO:0016154; F:pyrimidine-nucleoside phosphorylase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..94
FT /note="Pyrimidine/purine nucleoside phosphorylase"
FT /id="PRO_0000211763"
FT CONFLICT 77..94
FT /note="SEFHLQVAEPTSYLCRYL -> TVSFICKLPNPPLICAAICNSSPSP (in
FT Ref. 1; CAA54286)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 94 AA; 10234 MW; D7EF5C0AFD86D661 CRC64;
MLQSNEYFSG KVKSIGFSSS STGRASVGVM VEGEYTFSTA EPEEMTVISG ALNVLLPDAT
DWQVYEAGSV FNVPGHSEFH LQVAEPTSYL CRYL
