Reviewed,
UniProtKB/Swiss-Prot P83844 (ADPP_SHIFL)
Last modified
June 16, 2009.
Version 41.
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 | Shigella flexneri [Complete proteome] [HAMAP] | ||||||
| Taxonomic identifier | 623 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Shigella |
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 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 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_0000057046 | |||||
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] | "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157." Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y. Yu J.Nucleic Acids Res. 30:4432-4441(2002) [PubMed: 12384590] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 301 / Serotype 2a. |
| [2] | "Complete genome sequence and comparative genomics of Shigella flexneri serotype 2a strain 2457T." Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G., Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T., Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R. Infect. Immun. 71:2775-2786(2003) [PubMed: 12704152] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 700930 / 2457T / Serotype 2a. |
Cross-references
Sequence databases | |
|---|---|
| AE005674 Genomic DNA. Translation: AAN44552.1. AE014073 Genomic DNA. Translation: AAP18365.1. | |
| RefSeq | NP_708845.1. NP_838555.1. |
3D structure databases | |
| SMR | P83844. Positions 8-209. |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 1026699. 1080971. |
| GenomeReviews | Gene locus SF3074 in contig AE005674_GR. Gene locus S3279 in contig AE014073_GR. |
| KEGG | sfl:SF3074. sfx:S3279. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| HOGENOM | P83844. |
| OMA | P83844. YFPSPGG. |
Enzyme and pathway databases | |
| BioCyc | SFLE198214:AAN44552.1-MON. |
| BRENDA | 3.6.1.13. 189495. |
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_SHIFL | ||||||||
| Accession | Primary (citable) accession number: P83844 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) | ||||||||

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