PPNN_ECOL6
ID PPNN_ECOL6 Reviewed; 454 AA.
AC P0ADR9; P37350; Q46921;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase {ECO:0000250|UniProtKB:P0ADR8};
DE EC=3.2.2.- {ECO:0000250|UniProtKB:P0ADR8};
DE EC=3.2.2.10 {ECO:0000250|UniProtKB:P0ADR8};
DE AltName: Full=AMP nucleosidase {ECO:0000250|UniProtKB:P0ADR8};
DE EC=3.2.2.4 {ECO:0000250|UniProtKB:P0ADR8};
DE AltName: Full=CMP nucleosidase {ECO:0000250|UniProtKB:P0ADR8};
DE AltName: Full=GMP nucleosidase {ECO:0000250|UniProtKB:P0ADR8};
DE AltName: Full=IMP nucleosidase {ECO:0000250|UniProtKB:P0ADR8};
DE AltName: Full=UMP nucleosidase {ECO:0000250|UniProtKB:P0ADR8};
DE AltName: Full=dTMP nucleosidase {ECO:0000250|UniProtKB:P0ADR8};
GN Name=ppnN {ECO:0000250|UniProtKB:P0ADR8}; Synonyms=ygdH;
GN OrderedLocusNames=c3361;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=199310;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFT073 / ATCC 700928 / UPEC;
RX PubMed=12471157; DOI=10.1073/pnas.252529799;
RA Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Catalyzes the hydrolysis of the N-glycosidic bond of diverse
CC pyrimidine and purine nucleotide 5'-monophosphates, to form ribose 5-
CC phosphate and the corresponding free base. Can use AMP, GMP, IMP, CMP,
CC dTMP and UMP as substrates. Cannot catalyze the reverse reactions. May
CC contribute to nucleoside pool homeostasis by degrading excess
CC nucleotides and feeding back the ribose moiety to catabolism.
CC {ECO:0000250|UniProtKB:P0ADR8}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a pyrimidine ribonucleoside 5'-phosphate + H2O = a pyrimidine
CC nucleobase + D-ribose 5-phosphate; Xref=Rhea:RHEA:13425,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:26432, ChEBI:CHEBI:78346,
CC ChEBI:CHEBI:138238; EC=3.2.2.10;
CC Evidence={ECO:0000250|UniProtKB:P0ADR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=AMP + H2O = adenine + D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4;
CC Evidence={ECO:0000250|UniProtKB:P0ADR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GMP + H2O = D-ribose 5-phosphate + guanine;
CC Xref=Rhea:RHEA:52708, ChEBI:CHEBI:15377, ChEBI:CHEBI:16235,
CC ChEBI:CHEBI:58115, ChEBI:CHEBI:78346;
CC Evidence={ECO:0000250|UniProtKB:P0ADR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CMP + H2O = cytosine + D-ribose 5-phosphate;
CC Xref=Rhea:RHEA:30075, ChEBI:CHEBI:15377, ChEBI:CHEBI:16040,
CC ChEBI:CHEBI:60377, ChEBI:CHEBI:78346; EC=3.2.2.10;
CC Evidence={ECO:0000250|UniProtKB:P0ADR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + IMP = D-ribose 5-phosphate + hypoxanthine;
CC Xref=Rhea:RHEA:20469, ChEBI:CHEBI:15377, ChEBI:CHEBI:17368,
CC ChEBI:CHEBI:58053, ChEBI:CHEBI:78346;
CC Evidence={ECO:0000250|UniProtKB:P0ADR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + UMP = D-ribose 5-phosphate + uracil;
CC Xref=Rhea:RHEA:52704, ChEBI:CHEBI:15377, ChEBI:CHEBI:17568,
CC ChEBI:CHEBI:57865, ChEBI:CHEBI:78346;
CC Evidence={ECO:0000250|UniProtKB:P0ADR8};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=dTMP + H2O = 2-deoxy-D-ribose 5-phosphate + thymine;
CC Xref=Rhea:RHEA:52712, ChEBI:CHEBI:15377, ChEBI:CHEBI:17821,
CC ChEBI:CHEBI:62877, ChEBI:CHEBI:63528;
CC Evidence={ECO:0000250|UniProtKB:P0ADR8};
CC -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
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DR EMBL; AE014075; AAN81808.1; -; Genomic_DNA.
DR RefSeq; WP_000627995.1; NC_004431.1.
DR AlphaFoldDB; P0ADR9; -.
DR SMR; P0ADR9; -.
DR STRING; 199310.c3361; -.
DR EnsemblBacteria; AAN81808; AAN81808; c3361.
DR GeneID; 67413930; -.
DR KEGG; ecc:c3361; -.
DR eggNOG; COG1611; Bacteria.
DR HOGENOM; CLU_047550_0_0_6; -.
DR OMA; EYKYTKK; -.
DR BioCyc; ECOL199310:C3361-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0008714; F:AMP nucleosidase activity; IEA:UniProtKB-EC.
DR GO; GO:0047723; F:inosinate nucleosidase activity; IEA:RHEA.
DR GO; GO:0047405; F:pyrimidine-5'-nucleotide nucleosidase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.30.1850.10; -; 1.
DR InterPro; IPR021826; DUF3412.
DR InterPro; IPR031100; LOG_fam.
DR InterPro; IPR037153; YgdH-like_sf.
DR InterPro; IPR027820; YgdH_N.
DR Pfam; PF11892; DUF3412; 1.
DR Pfam; PF14793; DUF4478; 1.
DR Pfam; PF03641; Lysine_decarbox; 1.
PE 3: Inferred from homology;
KW Hydrolase.
FT CHAIN 1..454
FT /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT nucleosidase"
FT /id="PRO_0000169336"
SQ SEQUENCE 454 AA; 50972 MW; 39068DCC61DD1CF6 CRC64;
MITHISPLGS MDMLSQLEVD MLKRTASSDL YQLFRNCSLA VLNSGSLTDN SKELLSRFEN
FDINVLRRER GVKLELINPP EEAFVDGRII RALQANLFAV LRDILFVYGQ IHNTVRFPNL
NLDNSVHITN LVFSILRNAR ALHVGEAPNM VVCWGGHSIN ENEYLYARRV GNQLGLRELN
ICTGCGPGAM EAPMKGAAVG HAQQRYKDSR FIGMTEPSII AAEPPNPLVN ELIIMPDIEK
RLEAFVRIAH GIIIFPGGVG TAEELLYLLG ILMNPANKDQ VLPLILTGPK ESADYFRVLD
EFVVHTLGEN ARRHYRIIID DAAEVARQMK KSMPLVKENR RDTGDAYSFN WSMRIAPDLQ
MPFEPSHENM ANLKLYPDQP VEVLAADLRR AFSGIVAGNV KEVGIRAIEE FGPYKINGDK
EIMRRMDDLL QGFVAQHRMK LPGSAYIPCY EICT
