ADPP_ECOL6
ID ADPP_ECOL6 Reviewed; 209 AA.
AC P83842; P36651;
DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT 13-APR-2004, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=ADP-ribose pyrophosphatase;
DE EC=3.6.1.13;
DE AltName: Full=ADP-ribose diphosphatase;
DE AltName: Full=ADP-ribose phosphohydrolase;
DE Short=ASPPase;
DE AltName: Full=Adenosine diphosphoribose pyrophosphatase;
DE Short=ADPR-PPase;
GN Name=nudF; Synonyms=aspP; OrderedLocusNames=c3780;
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: Acts on ADP-mannose and ADP-glucose as well as ADP-ribose.
CC Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme
CC is a limiting step of the gluconeogenic process (By similarity).
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ADP-D-ribose + H2O = AMP + D-ribose 5-phosphate + 2 H(+);
CC Xref=Rhea:RHEA:10412, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57967, ChEBI:CHEBI:78346, ChEBI:CHEBI:456215;
CC EC=3.6.1.13;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- ACTIVITY REGULATION: Inhibited by phosphorylated compounds such as AMP,
CC ADP, ATP, 3-phosphoglyceric acid and PPi. Not inhibited by
CC orthophosphate. Activity is high in cells grown in low glucose
CC concentrations and decreases dramatically as glucose concentration
CC increases (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily.
CC {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; AE014075; AAN82224.1; -; Genomic_DNA.
DR RefSeq; WP_000917117.1; NC_004431.1.
DR AlphaFoldDB; P83842; -.
DR SMR; P83842; -.
DR STRING; 199310.c3780; -.
DR EnsemblBacteria; AAN82224; AAN82224; c3780.
DR GeneID; 66673067; -.
DR KEGG; ecc:c3780; -.
DR eggNOG; COG0494; Bacteria.
DR HOGENOM; CLU_062658_6_1_6; -.
DR OMA; TIIALQW; -.
DR BioCyc; ECOL199310:C3780-MON; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR InterPro; IPR004385; NDP_pyrophosphatase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR TIGRFAMs; TIGR00052; TIGR00052; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase; Magnesium; Manganese; Metal-binding.
FT CHAIN 1..209
FT /note="ADP-ribose pyrophosphatase"
FT /id="PRO_0000057043"
FT DOMAIN 55..193
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 97..118
FT /note="Nudix box"
FT ACT_SITE 162
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 28..29
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 51..52
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 56
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 79
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 112
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 116
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
FT BINDING 133..135
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 139
FT /ligand="substrate"
FT /ligand_note="ligand shared between dimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250"
FT BINDING 164
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250"
SQ SEQUENCE 209 AA; 23667 MW; 2CF77EA9D63B9615 CRC64;
MLKPDNLPVT FGKNDVEIIA RETLYRGFFS LDLYRFRHRL FNGQMSHEVR REIFERGHAA
VLLPFDPVRD EVVLIEQIRI AAYDTSETPW LLEMVAGMIE EGESVEDVAR REAIEEAGLI
VKRTKPVLSF LASPGGTSER SSIMVGEVDA TTASGIHGLA DENEDIRVHV VSREQAYQWV
EEGKIDNAAS VIALQWLQLH HQALKNEWA
