Reviewed,
UniProtKB/Swiss-Prot P83842 (ADPP_ECOL6)
Last modified
June 16, 2009.
Version 35.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: ADP-ribose pyrophosphatase EC=3.6.1.13 Alternative name(s): ADP-ribose diphosphatase Adenosine diphosphoribose pyrophosphatase Short name=ADPR-PPase ADP-ribose phosphohydrolase Short name=ASPPase | ||||||
| Gene names |
| ||||||
| Organism | Escherichia coli O6 [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 217992 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia |
Protein attributes
| Sequence length | 209 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Acts on ADP-mannose and ADP-glucose as well as ADP-ribose. Prevents glycogen biosynthesis. The reaction catalyzed by this enzyme is a limiting step of the gluconeogenic process By similarity. |
| Catalytic activity | ADP-ribose + H2O = AMP + D-ribose 5-phosphate. |
| Cofactor | Binds 3 magnesium ions per subunit By similarity. |
| Enzyme regulation | Inhibited by phosphorylated compounds such as AMP, ADP, ATP, 3-phosphoglyceric acid and PPi. Not inhibited by orthophosphate. Activity is high in cells grown in low glucose concentrations and decreases dramatically as glucose concentration increases By similarity. |
| Subunit structure | Homodimer By similarity. |
| Sequence similarities | Belongs to the Nudix hydrolase family. NudF subfamily. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Manganese Metal-binding Zinc |
| Molecular function | Hydrolase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | ADP-ribose diphosphatase activity Inferred from electronic annotation. Source: EC magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW manganese ion bindingInferred from electronic annotation. Source: UniProtKB-KW zinc ion bindingInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 209 | 209 | ADP-ribose pyrophosphatase | PRO_0000057043 | |||||
Regions | |||||||||
| Motif | 97 – 118 | 22 | Nudix box | ||||||
Sites | |||||||||
| Active site | 162 | 1 | Proton acceptor By similarity | ||||||
| Metal binding | 112 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 112 | 1 | Magnesium 2 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 1 By similarity | ||||||
| Metal binding | 116 | 1 | Magnesium 3 By similarity | ||||||
| Metal binding | 164 | 1 | Magnesium 1 By similarity | ||||||
Sequences
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References
| [1] | "Extensive mosaic structure revealed by the complete genome sequence of uropathogenic Escherichia coli." Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T., Donnenberg M.S., Blattner F.R. Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002) [PubMed: 12471157] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O6:H1 / CFT073 / ATCC 700928 / UPEC. |
Cross-references
Sequence databases | |
|---|---|
| AE014075 Genomic DNA. Translation: AAN82224.1. | |
| RefSeq | NP_755651.1. |
3D structure databases | |
| SMR | P83842. Positions 8-209. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1039920. |
| GenomeReviews | Gene locus c3780 in contig AE014075_GR. |
| KEGG | ecc:c3780. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P83842. |
| OMA | P83842. YFPSPGG. |
Enzyme and pathway databases | |
| BRENDA | 3.6.1.13. 292881. |
Family and domain databases | |
| InterPro | IPR004385. NDP_pyrophos. IPR000086. NUDIX_hydrolase_core. [Graphical view] |
| Gene3D | G3DSA:3.90.79.10. NUDIX_hydrolase. 1 hit. |
| Pfam | PF00293. NUDIX. 1 hit. [Graphical view] |
| TIGRFAMs | TIGR00052. NDP_pyrophos. 1 hit. |
| PROSITE | PS00893. NUDIX. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ADPP_ECOL6 | ||||||||
| Accession | Primary (citable) accession number: P83842 Secondary accession number(s): P36651 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


