PPNN_ECOLI
ID PPNN_ECOLI Reviewed; 454 AA.
AC P0ADR8; P37350; Q2MA39; Q46921;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Pyrimidine/purine nucleotide 5'-monophosphate nucleosidase {ECO:0000303|PubMed:27941785};
DE EC=3.2.2.- {ECO:0000269|PubMed:27941785};
DE EC=3.2.2.10 {ECO:0000269|PubMed:27941785};
DE AltName: Full=AMP nucleosidase {ECO:0000305|PubMed:27941785};
DE EC=3.2.2.4 {ECO:0000269|PubMed:27941785};
DE AltName: Full=CMP nucleosidase {ECO:0000305|PubMed:27941785};
DE AltName: Full=GMP nucleosidase {ECO:0000305|PubMed:27941785};
DE AltName: Full=IMP nucleosidase {ECO:0000305|PubMed:27941785};
DE AltName: Full=UMP nucleosidase {ECO:0000305|PubMed:27941785};
DE AltName: Full=dTMP nucleosidase {ECO:0000305|PubMed:27941785};
GN Name=ppnN {ECO:0000303|PubMed:27941785};
GN Synonyms=ygdH {ECO:0000312|EMBL:AAC75837.1};
GN OrderedLocusNames=b2795, JW2766;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 374-454.
RC STRAIN=K12;
RA Shao Z., Newman E.B.;
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP IDENTIFICATION.
RA Rudd K.E.;
RL Unpublished observations (FEB-1994).
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 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. Is
CC required for optimal growth in glucose minimal medium, possibly because
CC it contributes to nucleoside pool homeostasis by degrading excess
CC nucleotides and feeding back the ribose moiety to catabolism.
CC {ECO:0000269|PubMed:27941785}.
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
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:0000269|PubMed:27941785};
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene show a reduced growth
CC rate and yield in glucose minimal medium compared to wild-type. They
CC also show a consistent change in the level of several metabolites whose
CC masses can correspond to adenine, xanthine or 4-hydroxy-L-threonine.
CC {ECO:0000269|PubMed:27941785}.
CC -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; U29581; AAB40445.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75837.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76867.1; -; Genomic_DNA.
DR EMBL; U01233; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR PIR; G65061; G65061.
DR RefSeq; NP_417275.1; NC_000913.3.
DR RefSeq; WP_000627995.1; NZ_STEB01000030.1.
DR PDB; 6GFL; X-ray; 2.48 A; A/B=2-454.
DR PDB; 6GFM; X-ray; 2.77 A; A=2-454.
DR PDBsum; 6GFL; -.
DR PDBsum; 6GFM; -.
DR AlphaFoldDB; P0ADR8; -.
DR SMR; P0ADR8; -.
DR BioGRID; 4261305; 16.
DR BioGRID; 851596; 1.
DR DIP; DIP-47955N; -.
DR IntAct; P0ADR8; 4.
DR STRING; 511145.b2795; -.
DR jPOST; P0ADR8; -.
DR PaxDb; P0ADR8; -.
DR PRIDE; P0ADR8; -.
DR EnsemblBacteria; AAC75837; AAC75837; b2795.
DR EnsemblBacteria; BAE76867; BAE76867; BAE76867.
DR GeneID; 67413930; -.
DR GeneID; 947266; -.
DR KEGG; ecj:JW2766; -.
DR KEGG; eco:b2795; -.
DR PATRIC; fig|511145.12.peg.2895; -.
DR EchoBASE; EB2276; -.
DR eggNOG; COG1611; Bacteria.
DR HOGENOM; CLU_047550_0_0_6; -.
DR InParanoid; P0ADR8; -.
DR OMA; EYKYTKK; -.
DR PhylomeDB; P0ADR8; -.
DR BioCyc; EcoCyc:EG12373-MON; -.
DR BioCyc; MetaCyc:EG12373-MON; -.
DR PRO; PR:P0ADR8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0008714; F:AMP nucleosidase activity; IDA:EcoCyc.
DR GO; GO:0097216; F:guanosine tetraphosphate binding; IDA:EcoCyc.
DR GO; GO:0047723; F:inosinate nucleosidase activity; IDA:EcoCyc.
DR GO; GO:0047405; F:pyrimidine-5'-nucleotide nucleosidase activity; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Reference proteome.
FT CHAIN 1..454
FT /note="Pyrimidine/purine nucleotide 5'-monophosphate
FT nucleosidase"
FT /id="PRO_0000169334"
FT CONFLICT 389
FT /note="R -> A (in Ref. 3; U01233)"
FT /evidence="ECO:0000305"
FT STRAND 3..6
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 9..11
FT /evidence="ECO:0007829|PDB:6GFM"
FT HELIX 16..21
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 23..27
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 30..42
FT /evidence="ECO:0007829|PDB:6GFL"
FT TURN 43..45
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 52..57
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 62..68
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 71..78
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 91..111
FT /evidence="ECO:0007829|PDB:6GFL"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:6GFM"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 150..154
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 161..176
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 180..183
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:6GFM"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 192..203
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 211..215
FT /evidence="ECO:0007829|PDB:6GFL"
FT TURN 217..222
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 230..234
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 238..248
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 259..272
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 275..277
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 284..288
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 293..306
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 309..314
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 322..341
FT /evidence="ECO:0007829|PDB:6GFL"
FT TURN 342..344
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 347..349
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 357..360
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 367..371
FT /evidence="ECO:0007829|PDB:6GFL"
FT STRAND 375..379
FT /evidence="ECO:0007829|PDB:6GFM"
FT HELIX 381..400
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 402..411
FT /evidence="ECO:0007829|PDB:6GFL"
FT HELIX 422..435
FT /evidence="ECO:0007829|PDB:6GFL"
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
